cathepsin l inhibitor ii  (Millipore)


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    Name:
    Cathepsin L Inhibitor
    Description:

    Catalog Number:
    scp0110
    Price:
    None
    Applications:
    Cathepsin L is a lysosomal cysteine proteinase that metabolizes collagens and elastins. The roles and activity of Cathepsin L can be studied with the aid of peptide inhibitors such as the pentapeptide amide RKLLW-NH2 (Arg-Lys-Leu-Leu-Trp-NH2).
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    Structured Review

    Millipore cathepsin l inhibitor ii
    PGRN processing into GRNs is mediated by proper lysosome function and cysteine protease activity. A , HAP1 WT cells were treated for 24 h with the pan-lysosome inhibitors chloroquine (CQ; 50 µM), BafA1 (50 nM), or concanamycin A (ConA; 50 nM) and conditioned media were analyzed for secreted PGRN by ELISA. B , Lysates from HAP1 WT cells treated as in A were analyzed for PGRN and GRN-2,3 by immunoblot. C , D , Quantification of ( C ) PGRN and ( D ) GRN-2,3 from the experiment in B . E , HAP1 WT cells were treated with the indicated protease inhibitors for 24 h and analyzed for PGRN and GRN-2,3 by immunoblot. The inhibitors, their primary targets, and concentrations used are shown in the table at right. F , Time-dependent cleavage of C-TAP PGRN by recombinant <t>cathepsin</t> L in vitro . G , C-TAP PGRN was incubated with or without cathepsin L for 2 h in vitro and analyzed for multiple GRNs by immunoblot. H , HAP1 WT cells were treated with increasing concentrations of cathepsin L inhibitor II (Z-FY-CHO) for 40 h and lysates were analyzed for PGRN and GRN-2,3 by immunoblot. I , J , Quantification of ( I ) PGRN and ( J ) GRN-2,3 from the experiment in H . B , E , H , Arrows denote endogenous, intermediate PGRN cleavage products. For all immunoblots, PGRN and GRN-2,3 were detected with R D AF2420 and Sigma antibodies respectively. All immunoblot images are representative of at least three independent experiments and quantitative data are presented as mean ± SEM of three independent experiments; *differs from control p

    https://www.bioz.com/result/cathepsin l inhibitor ii/product/Millipore
    Average 99 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    cathepsin l inhibitor ii - by Bioz Stars, 2020-09
    99/100 stars

    Images

    1) Product Images from "Intracellular Proteolysis of Progranulin Generates Stable, Lysosomal Granulins that Are Haploinsufficient in Patients with Frontotemporal Dementia Caused by GRN Mutations"

    Article Title: Intracellular Proteolysis of Progranulin Generates Stable, Lysosomal Granulins that Are Haploinsufficient in Patients with Frontotemporal Dementia Caused by GRN Mutations

    Journal: eNeuro

    doi: 10.1523/ENEURO.0100-17.2017

    PGRN processing into GRNs is mediated by proper lysosome function and cysteine protease activity. A , HAP1 WT cells were treated for 24 h with the pan-lysosome inhibitors chloroquine (CQ; 50 µM), BafA1 (50 nM), or concanamycin A (ConA; 50 nM) and conditioned media were analyzed for secreted PGRN by ELISA. B , Lysates from HAP1 WT cells treated as in A were analyzed for PGRN and GRN-2,3 by immunoblot. C , D , Quantification of ( C ) PGRN and ( D ) GRN-2,3 from the experiment in B . E , HAP1 WT cells were treated with the indicated protease inhibitors for 24 h and analyzed for PGRN and GRN-2,3 by immunoblot. The inhibitors, their primary targets, and concentrations used are shown in the table at right. F , Time-dependent cleavage of C-TAP PGRN by recombinant cathepsin L in vitro . G , C-TAP PGRN was incubated with or without cathepsin L for 2 h in vitro and analyzed for multiple GRNs by immunoblot. H , HAP1 WT cells were treated with increasing concentrations of cathepsin L inhibitor II (Z-FY-CHO) for 40 h and lysates were analyzed for PGRN and GRN-2,3 by immunoblot. I , J , Quantification of ( I ) PGRN and ( J ) GRN-2,3 from the experiment in H . B , E , H , Arrows denote endogenous, intermediate PGRN cleavage products. For all immunoblots, PGRN and GRN-2,3 were detected with R D AF2420 and Sigma antibodies respectively. All immunoblot images are representative of at least three independent experiments and quantitative data are presented as mean ± SEM of three independent experiments; *differs from control p
    Figure Legend Snippet: PGRN processing into GRNs is mediated by proper lysosome function and cysteine protease activity. A , HAP1 WT cells were treated for 24 h with the pan-lysosome inhibitors chloroquine (CQ; 50 µM), BafA1 (50 nM), or concanamycin A (ConA; 50 nM) and conditioned media were analyzed for secreted PGRN by ELISA. B , Lysates from HAP1 WT cells treated as in A were analyzed for PGRN and GRN-2,3 by immunoblot. C , D , Quantification of ( C ) PGRN and ( D ) GRN-2,3 from the experiment in B . E , HAP1 WT cells were treated with the indicated protease inhibitors for 24 h and analyzed for PGRN and GRN-2,3 by immunoblot. The inhibitors, their primary targets, and concentrations used are shown in the table at right. F , Time-dependent cleavage of C-TAP PGRN by recombinant cathepsin L in vitro . G , C-TAP PGRN was incubated with or without cathepsin L for 2 h in vitro and analyzed for multiple GRNs by immunoblot. H , HAP1 WT cells were treated with increasing concentrations of cathepsin L inhibitor II (Z-FY-CHO) for 40 h and lysates were analyzed for PGRN and GRN-2,3 by immunoblot. I , J , Quantification of ( I ) PGRN and ( J ) GRN-2,3 from the experiment in H . B , E , H , Arrows denote endogenous, intermediate PGRN cleavage products. For all immunoblots, PGRN and GRN-2,3 were detected with R D AF2420 and Sigma antibodies respectively. All immunoblot images are representative of at least three independent experiments and quantitative data are presented as mean ± SEM of three independent experiments; *differs from control p

    Techniques Used: Activity Assay, Enzyme-linked Immunosorbent Assay, Recombinant, In Vitro, Incubation, Western Blot

    Model of intracellular processing of PGRN into stable, lysosomal GRNs. Sortilin and other receptors target endocytosed and newly synthesized PGRN to lysosomes. Within lysosomes, PGRN is proteolytically cleaved, in part, by cysteine proteases (i.e., cathepsin L) into mature, stable GRN proteins. Ablation of sortilin results in the reduced production of GRNs. Further, lysosome dysfunction caused by alkalizing agents or TMEM106B overexpression inhibits the processing of PGRN into GRNs. FTD- GRN  patients are haploinsufficient for GRNs, which may drive lysosome dysfunction leading to neurodegeneration.
    Figure Legend Snippet: Model of intracellular processing of PGRN into stable, lysosomal GRNs. Sortilin and other receptors target endocytosed and newly synthesized PGRN to lysosomes. Within lysosomes, PGRN is proteolytically cleaved, in part, by cysteine proteases (i.e., cathepsin L) into mature, stable GRN proteins. Ablation of sortilin results in the reduced production of GRNs. Further, lysosome dysfunction caused by alkalizing agents or TMEM106B overexpression inhibits the processing of PGRN into GRNs. FTD- GRN patients are haploinsufficient for GRNs, which may drive lysosome dysfunction leading to neurodegeneration.

    Techniques Used: Synthesized, Over Expression

    2) Product Images from "Cathepsin L Mediates the Degradation of Novel APP C-Terminal Fragments"

    Article Title: Cathepsin L Mediates the Degradation of Novel APP C-Terminal Fragments

    Journal: Biochemistry

    doi: 10.1021/acs.biochem.5b00329

    Accumulation of novel APP CTFs was mediated by cathepsin L inhibition. (A) Naïve HEK293 cells were treated with vehicle or MDL28170 (20 or 40 μ M) for 24 h before being collected. The Western blot was probed with C1/6.1 and anti-actin antibody.
    Figure Legend Snippet: Accumulation of novel APP CTFs was mediated by cathepsin L inhibition. (A) Naïve HEK293 cells were treated with vehicle or MDL28170 (20 or 40 μ M) for 24 h before being collected. The Western blot was probed with C1/6.1 and anti-actin antibody.

    Techniques Used: Inhibition, Western Blot

    3) Product Images from "Inhibition of cathepsin L sensitizes human glioma cells to ionizing radiation in vitro through NF-κB signaling pathway"

    Article Title: Inhibition of cathepsin L sensitizes human glioma cells to ionizing radiation in vitro through NF-κB signaling pathway

    Journal: Acta Pharmacologica Sinica

    doi: 10.1038/aps.2014.148

    Altered IR-induced nuclear translocation of NF-κB following selective inhibition of cathepsin L with Z-FY-CHO or cathepsin L shRNA. (A) p65 protein immunofluorescence in U251 cells treated with Z-FY-CHO, IR, or both. (B) p65 protein immunofluorescence
    Figure Legend Snippet: Altered IR-induced nuclear translocation of NF-κB following selective inhibition of cathepsin L with Z-FY-CHO or cathepsin L shRNA. (A) p65 protein immunofluorescence in U251 cells treated with Z-FY-CHO, IR, or both. (B) p65 protein immunofluorescence

    Techniques Used: Translocation Assay, Inhibition, shRNA, Immunofluorescence

    Reduced NF-κB-dependent transcriptional activation in U251 cells following IR with selective inhibition of cathepsin L with Z-FY-CHO (A) or cathepsin L shRNA (B). NF-κB activity was assessed using an NF-κB-RE firefly luciferase
    Figure Legend Snippet: Reduced NF-κB-dependent transcriptional activation in U251 cells following IR with selective inhibition of cathepsin L with Z-FY-CHO (A) or cathepsin L shRNA (B). NF-κB activity was assessed using an NF-κB-RE firefly luciferase

    Techniques Used: Activation Assay, Inhibition, shRNA, Activity Assay, Luciferase

    The inhibition of cathepsin L sensitized U251 cells to IR. (A) Clonogenic survival curves for U251 cells treated with radiation (0, 2, 4, 6, and 8 Gy) alone or in combination with Z-FY-CHO. (B) Western blot of CTSL in whole cell extracts from parental
    Figure Legend Snippet: The inhibition of cathepsin L sensitized U251 cells to IR. (A) Clonogenic survival curves for U251 cells treated with radiation (0, 2, 4, 6, and 8 Gy) alone or in combination with Z-FY-CHO. (B) Western blot of CTSL in whole cell extracts from parental

    Techniques Used: Inhibition, Western Blot

    Altered IR-induced nuclear translocation of NF-κB following selective inhibition of cathepsin L with Z-FY-CHO or cathepsin L shRNA. (A) Western blot analysis of IκBα expression and the nuclear translocation of NF-κB in
    Figure Legend Snippet: Altered IR-induced nuclear translocation of NF-κB following selective inhibition of cathepsin L with Z-FY-CHO or cathepsin L shRNA. (A) Western blot analysis of IκBα expression and the nuclear translocation of NF-κB in

    Techniques Used: Translocation Assay, Inhibition, shRNA, Western Blot, Expressing

    The expression of cathepsin L protein and nuclear translocation of NF-κB p65 and p50 in U251 cells following IR was analyzed by Western blot. (A) Western blot analysis of cathepsin L in U251 cells treated with IR (10 Gy). β-Actin was used
    Figure Legend Snippet: The expression of cathepsin L protein and nuclear translocation of NF-κB p65 and p50 in U251 cells following IR was analyzed by Western blot. (A) Western blot analysis of cathepsin L in U251 cells treated with IR (10 Gy). β-Actin was used

    Techniques Used: Expressing, Translocation Assay, Western Blot

    Effect of p65 shRNA on the expression of p65 and cathepsin L in U251 and MCF-7 cells. (A) Western blot of p65 whole cell extracts from normal U251, U251-consh and U251-p65sh cells. β-Actin was used as an internal control. c P
    Figure Legend Snippet: Effect of p65 shRNA on the expression of p65 and cathepsin L in U251 and MCF-7 cells. (A) Western blot of p65 whole cell extracts from normal U251, U251-consh and U251-p65sh cells. β-Actin was used as an internal control. c P

    Techniques Used: shRNA, Expressing, Western Blot

    4) Product Images from "Intracellular Proteolysis of Progranulin Generates Stable, Lysosomal Granulins that Are Haploinsufficient in Patients with Frontotemporal Dementia Caused by GRN Mutations"

    Article Title: Intracellular Proteolysis of Progranulin Generates Stable, Lysosomal Granulins that Are Haploinsufficient in Patients with Frontotemporal Dementia Caused by GRN Mutations

    Journal: eNeuro

    doi: 10.1523/ENEURO.0100-17.2017

    PGRN processing into GRNs is mediated by proper lysosome function and cysteine protease activity. A , HAP1 WT cells were treated for 24 h with the pan-lysosome inhibitors chloroquine (CQ; 50 µM), BafA1 (50 nM), or concanamycin A (ConA; 50 nM) and conditioned media were analyzed for secreted PGRN by ELISA. B , Lysates from HAP1 WT cells treated as in A were analyzed for PGRN and GRN-2,3 by immunoblot. C , D , Quantification of ( C ) PGRN and ( D ) GRN-2,3 from the experiment in B . E , HAP1 WT cells were treated with the indicated protease inhibitors for 24 h and analyzed for PGRN and GRN-2,3 by immunoblot. The inhibitors, their primary targets, and concentrations used are shown in the table at right. F , Time-dependent cleavage of C-TAP PGRN by recombinant cathepsin L in vitro . G , C-TAP PGRN was incubated with or without cathepsin L for 2 h in vitro and analyzed for multiple GRNs by immunoblot. H , HAP1 WT cells were treated with increasing concentrations of cathepsin L inhibitor II (Z-FY-CHO) for 40 h and lysates were analyzed for PGRN and GRN-2,3 by immunoblot. I , J , Quantification of ( I ) PGRN and ( J ) GRN-2,3 from the experiment in H . B , E , H , Arrows denote endogenous, intermediate PGRN cleavage products. For all immunoblots, PGRN and GRN-2,3 were detected with R D AF2420 and Sigma antibodies respectively. All immunoblot images are representative of at least three independent experiments and quantitative data are presented as mean ± SEM of three independent experiments; *differs from control p
    Figure Legend Snippet: PGRN processing into GRNs is mediated by proper lysosome function and cysteine protease activity. A , HAP1 WT cells were treated for 24 h with the pan-lysosome inhibitors chloroquine (CQ; 50 µM), BafA1 (50 nM), or concanamycin A (ConA; 50 nM) and conditioned media were analyzed for secreted PGRN by ELISA. B , Lysates from HAP1 WT cells treated as in A were analyzed for PGRN and GRN-2,3 by immunoblot. C , D , Quantification of ( C ) PGRN and ( D ) GRN-2,3 from the experiment in B . E , HAP1 WT cells were treated with the indicated protease inhibitors for 24 h and analyzed for PGRN and GRN-2,3 by immunoblot. The inhibitors, their primary targets, and concentrations used are shown in the table at right. F , Time-dependent cleavage of C-TAP PGRN by recombinant cathepsin L in vitro . G , C-TAP PGRN was incubated with or without cathepsin L for 2 h in vitro and analyzed for multiple GRNs by immunoblot. H , HAP1 WT cells were treated with increasing concentrations of cathepsin L inhibitor II (Z-FY-CHO) for 40 h and lysates were analyzed for PGRN and GRN-2,3 by immunoblot. I , J , Quantification of ( I ) PGRN and ( J ) GRN-2,3 from the experiment in H . B , E , H , Arrows denote endogenous, intermediate PGRN cleavage products. For all immunoblots, PGRN and GRN-2,3 were detected with R D AF2420 and Sigma antibodies respectively. All immunoblot images are representative of at least three independent experiments and quantitative data are presented as mean ± SEM of three independent experiments; *differs from control p

    Techniques Used: Activity Assay, Enzyme-linked Immunosorbent Assay, Recombinant, In Vitro, Incubation, Western Blot

    Model of intracellular processing of PGRN into stable, lysosomal GRNs. Sortilin and other receptors target endocytosed and newly synthesized PGRN to lysosomes. Within lysosomes, PGRN is proteolytically cleaved, in part, by cysteine proteases (i.e., cathepsin L) into mature, stable GRN proteins. Ablation of sortilin results in the reduced production of GRNs. Further, lysosome dysfunction caused by alkalizing agents or TMEM106B overexpression inhibits the processing of PGRN into GRNs. FTD- GRN  patients are haploinsufficient for GRNs, which may drive lysosome dysfunction leading to neurodegeneration.
    Figure Legend Snippet: Model of intracellular processing of PGRN into stable, lysosomal GRNs. Sortilin and other receptors target endocytosed and newly synthesized PGRN to lysosomes. Within lysosomes, PGRN is proteolytically cleaved, in part, by cysteine proteases (i.e., cathepsin L) into mature, stable GRN proteins. Ablation of sortilin results in the reduced production of GRNs. Further, lysosome dysfunction caused by alkalizing agents or TMEM106B overexpression inhibits the processing of PGRN into GRNs. FTD- GRN patients are haploinsufficient for GRNs, which may drive lysosome dysfunction leading to neurodegeneration.

    Techniques Used: Synthesized, Over Expression

    5) Product Images from "Intracellular Proteolysis of Progranulin Generates Stable, Lysosomal Granulins that Are Haploinsufficient in Patients with Frontotemporal Dementia Caused by GRN Mutations"

    Article Title: Intracellular Proteolysis of Progranulin Generates Stable, Lysosomal Granulins that Are Haploinsufficient in Patients with Frontotemporal Dementia Caused by GRN Mutations

    Journal: eNeuro

    doi: 10.1523/ENEURO.0100-17.2017

    PGRN processing into GRNs is mediated by proper lysosome function and cysteine protease activity. A , HAP1 WT cells were treated for 24 h with the pan-lysosome inhibitors chloroquine (CQ; 50 µM), BafA1 (50 nM), or concanamycin A (ConA; 50 nM) and conditioned media were analyzed for secreted PGRN by ELISA. B , Lysates from HAP1 WT cells treated as in A were analyzed for PGRN and GRN-2,3 by immunoblot. C , D , Quantification of ( C ) PGRN and ( D ) GRN-2,3 from the experiment in B . E , HAP1 WT cells were treated with the indicated protease inhibitors for 24 h and analyzed for PGRN and GRN-2,3 by immunoblot. The inhibitors, their primary targets, and concentrations used are shown in the table at right. F , Time-dependent cleavage of C-TAP PGRN by recombinant cathepsin L in vitro . G , C-TAP PGRN was incubated with or without cathepsin L for 2 h in vitro and analyzed for multiple GRNs by immunoblot. H , HAP1 WT cells were treated with increasing concentrations of cathepsin L inhibitor II (Z-FY-CHO) for 40 h and lysates were analyzed for PGRN and GRN-2,3 by immunoblot. I , J , Quantification of ( I ) PGRN and ( J ) GRN-2,3 from the experiment in H . B , E , H , Arrows denote endogenous, intermediate PGRN cleavage products. For all immunoblots, PGRN and GRN-2,3 were detected with R D AF2420 and Sigma antibodies respectively. All immunoblot images are representative of at least three independent experiments and quantitative data are presented as mean ± SEM of three independent experiments; *differs from control p
    Figure Legend Snippet: PGRN processing into GRNs is mediated by proper lysosome function and cysteine protease activity. A , HAP1 WT cells were treated for 24 h with the pan-lysosome inhibitors chloroquine (CQ; 50 µM), BafA1 (50 nM), or concanamycin A (ConA; 50 nM) and conditioned media were analyzed for secreted PGRN by ELISA. B , Lysates from HAP1 WT cells treated as in A were analyzed for PGRN and GRN-2,3 by immunoblot. C , D , Quantification of ( C ) PGRN and ( D ) GRN-2,3 from the experiment in B . E , HAP1 WT cells were treated with the indicated protease inhibitors for 24 h and analyzed for PGRN and GRN-2,3 by immunoblot. The inhibitors, their primary targets, and concentrations used are shown in the table at right. F , Time-dependent cleavage of C-TAP PGRN by recombinant cathepsin L in vitro . G , C-TAP PGRN was incubated with or without cathepsin L for 2 h in vitro and analyzed for multiple GRNs by immunoblot. H , HAP1 WT cells were treated with increasing concentrations of cathepsin L inhibitor II (Z-FY-CHO) for 40 h and lysates were analyzed for PGRN and GRN-2,3 by immunoblot. I , J , Quantification of ( I ) PGRN and ( J ) GRN-2,3 from the experiment in H . B , E , H , Arrows denote endogenous, intermediate PGRN cleavage products. For all immunoblots, PGRN and GRN-2,3 were detected with R D AF2420 and Sigma antibodies respectively. All immunoblot images are representative of at least three independent experiments and quantitative data are presented as mean ± SEM of three independent experiments; *differs from control p

    Techniques Used: Activity Assay, Enzyme-linked Immunosorbent Assay, Recombinant, In Vitro, Incubation, Western Blot

    Model of intracellular processing of PGRN into stable, lysosomal GRNs. Sortilin and other receptors target endocytosed and newly synthesized PGRN to lysosomes. Within lysosomes, PGRN is proteolytically cleaved, in part, by cysteine proteases (i.e., cathepsin L) into mature, stable GRN proteins. Ablation of sortilin results in the reduced production of GRNs. Further, lysosome dysfunction caused by alkalizing agents or TMEM106B overexpression inhibits the processing of PGRN into GRNs. FTD- GRN  patients are haploinsufficient for GRNs, which may drive lysosome dysfunction leading to neurodegeneration.
    Figure Legend Snippet: Model of intracellular processing of PGRN into stable, lysosomal GRNs. Sortilin and other receptors target endocytosed and newly synthesized PGRN to lysosomes. Within lysosomes, PGRN is proteolytically cleaved, in part, by cysteine proteases (i.e., cathepsin L) into mature, stable GRN proteins. Ablation of sortilin results in the reduced production of GRNs. Further, lysosome dysfunction caused by alkalizing agents or TMEM106B overexpression inhibits the processing of PGRN into GRNs. FTD- GRN patients are haploinsufficient for GRNs, which may drive lysosome dysfunction leading to neurodegeneration.

    Techniques Used: Synthesized, Over Expression

    Related Articles

    Concentration Assay:

    Article Title: Cathepsin B inhibition interferes with metastatic potential of human melanoma: an in vitro and in vivo study
    Article Snippet: .. For cell migration and invasion assays, cells were seeded in the presence of the cathepsin D inhibitor (Pepstatin A, 100 μM, Calbiochem), the cathepsin L inhibitor (cathepsin L inhibitor II, Z-FY-CHO, 10 μM, Calbiochem) as well as two cathepsin B inhibitors: CA-074 (cell unpermeant) and CA-074Me (cell permeant) (both given at a concentration of 10 μM, Calbiochem, Nottingham, UK). ..

    Article Title: Multiple Cationic Amphiphiles Induce a Niemann-Pick C Phenotype and Inhibit Ebola Virus Entry and Infection
    Article Snippet: .. Briefly, after a 1 hr incubation at 37°C with inhibitor at the indicated concentration, cathepsin B activity in cell lysates was determined using the cathepsin B substrate Z-Arg-Arg-7-AMC (Calbiochem). .. Cathepsin L was assayed using the cathepsin L substrate Z-Phe-Arg-7-AMC (Calbiochem) in the presence of 1 µM CA074, a cathepsin B inhibitor (Calbiochem).

    Incubation:

    Article Title: Synthetic Reconstruction of Zoonotic and Early Human Severe Acute Respiratory Syndrome Coronavirus Isolates That Produce Fatal Disease in Aged Mice ▿
    Article Snippet: .. The cells were incubated with twofold dilutions of cathepsin K inhibitor II, cathepsin L inhibitor III, or cathepsin S inhibitor (Calbiochem, San Diego, CA) starting at 10−4 M/well for 1 h at 37°C. ..

    Article Title: Multiple Cationic Amphiphiles Induce a Niemann-Pick C Phenotype and Inhibit Ebola Virus Entry and Infection
    Article Snippet: .. Briefly, after a 1 hr incubation at 37°C with inhibitor at the indicated concentration, cathepsin B activity in cell lysates was determined using the cathepsin B substrate Z-Arg-Arg-7-AMC (Calbiochem). .. Cathepsin L was assayed using the cathepsin L substrate Z-Phe-Arg-7-AMC (Calbiochem) in the presence of 1 µM CA074, a cathepsin B inhibitor (Calbiochem).

    other:

    Article Title: Intracellular Proteolysis of Progranulin Generates Stable, Lysosomal Granulins that Are Haploinsufficient in Patients with Frontotemporal Dementia Caused by GRN Mutations
    Article Snippet: Cathepsin L inhibitor II (Z-FY-CHO) and ALLN were from Calbiochem.

    Activity Assay:

    Article Title: Cathepsin B Mediates the pH-Dependent Proinvasive Activity of Tumor-Shed Microvesicles 1
    Article Snippet: .. To distinguish the gelatinolytic activity due to cathepsin B activity, the cathepsin L inhibitor Z-FY-CHO (Calbiochem, San Diego, CA) was used. .. Cathepsin B activity in vesicles or cell extracts was determined using a spectrophotometric assay.

    Article Title: Multiple Cationic Amphiphiles Induce a Niemann-Pick C Phenotype and Inhibit Ebola Virus Entry and Infection
    Article Snippet: .. Briefly, after a 1 hr incubation at 37°C with inhibitor at the indicated concentration, cathepsin B activity in cell lysates was determined using the cathepsin B substrate Z-Arg-Arg-7-AMC (Calbiochem). .. Cathepsin L was assayed using the cathepsin L substrate Z-Phe-Arg-7-AMC (Calbiochem) in the presence of 1 µM CA074, a cathepsin B inhibitor (Calbiochem).

    Migration:

    Article Title: Cathepsin B inhibition interferes with metastatic potential of human melanoma: an in vitro and in vivo study
    Article Snippet: .. For cell migration and invasion assays, cells were seeded in the presence of the cathepsin D inhibitor (Pepstatin A, 100 μM, Calbiochem), the cathepsin L inhibitor (cathepsin L inhibitor II, Z-FY-CHO, 10 μM, Calbiochem) as well as two cathepsin B inhibitors: CA-074 (cell unpermeant) and CA-074Me (cell permeant) (both given at a concentration of 10 μM, Calbiochem, Nottingham, UK). ..

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  • 99
    Millipore cathepsin l inhibitor ii
    PGRN processing into GRNs is mediated by proper lysosome function and cysteine protease activity. A , HAP1 WT cells were treated for 24 h with the pan-lysosome inhibitors chloroquine (CQ; 50 µM), BafA1 (50 nM), or concanamycin A (ConA; 50 nM) and conditioned media were analyzed for secreted PGRN by ELISA. B , Lysates from HAP1 WT cells treated as in A were analyzed for PGRN and GRN-2,3 by immunoblot. C , D , Quantification of ( C ) PGRN and ( D ) GRN-2,3 from the experiment in B . E , HAP1 WT cells were treated with the indicated protease inhibitors for 24 h and analyzed for PGRN and GRN-2,3 by immunoblot. The inhibitors, their primary targets, and concentrations used are shown in the table at right. F , Time-dependent cleavage of C-TAP PGRN by recombinant <t>cathepsin</t> L in vitro . G , C-TAP PGRN was incubated with or without cathepsin L for 2 h in vitro and analyzed for multiple GRNs by immunoblot. H , HAP1 WT cells were treated with increasing concentrations of cathepsin L inhibitor II (Z-FY-CHO) for 40 h and lysates were analyzed for PGRN and GRN-2,3 by immunoblot. I , J , Quantification of ( I ) PGRN and ( J ) GRN-2,3 from the experiment in H . B , E , H , Arrows denote endogenous, intermediate PGRN cleavage products. For all immunoblots, PGRN and GRN-2,3 were detected with R D AF2420 and Sigma antibodies respectively. All immunoblot images are representative of at least three independent experiments and quantitative data are presented as mean ± SEM of three independent experiments; *differs from control p
    Cathepsin L Inhibitor Ii, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/cathepsin l inhibitor ii/product/Millipore
    Average 99 stars, based on 12 article reviews
    Price from $9.99 to $1999.99
    cathepsin l inhibitor ii - by Bioz Stars, 2020-09
    99/100 stars
      Buy from Supplier

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    PGRN processing into GRNs is mediated by proper lysosome function and cysteine protease activity. A , HAP1 WT cells were treated for 24 h with the pan-lysosome inhibitors chloroquine (CQ; 50 µM), BafA1 (50 nM), or concanamycin A (ConA; 50 nM) and conditioned media were analyzed for secreted PGRN by ELISA. B , Lysates from HAP1 WT cells treated as in A were analyzed for PGRN and GRN-2,3 by immunoblot. C , D , Quantification of ( C ) PGRN and ( D ) GRN-2,3 from the experiment in B . E , HAP1 WT cells were treated with the indicated protease inhibitors for 24 h and analyzed for PGRN and GRN-2,3 by immunoblot. The inhibitors, their primary targets, and concentrations used are shown in the table at right. F , Time-dependent cleavage of C-TAP PGRN by recombinant cathepsin L in vitro . G , C-TAP PGRN was incubated with or without cathepsin L for 2 h in vitro and analyzed for multiple GRNs by immunoblot. H , HAP1 WT cells were treated with increasing concentrations of cathepsin L inhibitor II (Z-FY-CHO) for 40 h and lysates were analyzed for PGRN and GRN-2,3 by immunoblot. I , J , Quantification of ( I ) PGRN and ( J ) GRN-2,3 from the experiment in H . B , E , H , Arrows denote endogenous, intermediate PGRN cleavage products. For all immunoblots, PGRN and GRN-2,3 were detected with R D AF2420 and Sigma antibodies respectively. All immunoblot images are representative of at least three independent experiments and quantitative data are presented as mean ± SEM of three independent experiments; *differs from control p

    Journal: eNeuro

    Article Title: Intracellular Proteolysis of Progranulin Generates Stable, Lysosomal Granulins that Are Haploinsufficient in Patients with Frontotemporal Dementia Caused by GRN Mutations

    doi: 10.1523/ENEURO.0100-17.2017

    Figure Lengend Snippet: PGRN processing into GRNs is mediated by proper lysosome function and cysteine protease activity. A , HAP1 WT cells were treated for 24 h with the pan-lysosome inhibitors chloroquine (CQ; 50 µM), BafA1 (50 nM), or concanamycin A (ConA; 50 nM) and conditioned media were analyzed for secreted PGRN by ELISA. B , Lysates from HAP1 WT cells treated as in A were analyzed for PGRN and GRN-2,3 by immunoblot. C , D , Quantification of ( C ) PGRN and ( D ) GRN-2,3 from the experiment in B . E , HAP1 WT cells were treated with the indicated protease inhibitors for 24 h and analyzed for PGRN and GRN-2,3 by immunoblot. The inhibitors, their primary targets, and concentrations used are shown in the table at right. F , Time-dependent cleavage of C-TAP PGRN by recombinant cathepsin L in vitro . G , C-TAP PGRN was incubated with or without cathepsin L for 2 h in vitro and analyzed for multiple GRNs by immunoblot. H , HAP1 WT cells were treated with increasing concentrations of cathepsin L inhibitor II (Z-FY-CHO) for 40 h and lysates were analyzed for PGRN and GRN-2,3 by immunoblot. I , J , Quantification of ( I ) PGRN and ( J ) GRN-2,3 from the experiment in H . B , E , H , Arrows denote endogenous, intermediate PGRN cleavage products. For all immunoblots, PGRN and GRN-2,3 were detected with R D AF2420 and Sigma antibodies respectively. All immunoblot images are representative of at least three independent experiments and quantitative data are presented as mean ± SEM of three independent experiments; *differs from control p

    Article Snippet: Cathepsin L inhibitor II (Z-FY-CHO) and ALLN were from Calbiochem.

    Techniques: Activity Assay, Enzyme-linked Immunosorbent Assay, Recombinant, In Vitro, Incubation, Western Blot

    Model of intracellular processing of PGRN into stable, lysosomal GRNs. Sortilin and other receptors target endocytosed and newly synthesized PGRN to lysosomes. Within lysosomes, PGRN is proteolytically cleaved, in part, by cysteine proteases (i.e., cathepsin L) into mature, stable GRN proteins. Ablation of sortilin results in the reduced production of GRNs. Further, lysosome dysfunction caused by alkalizing agents or TMEM106B overexpression inhibits the processing of PGRN into GRNs. FTD- GRN  patients are haploinsufficient for GRNs, which may drive lysosome dysfunction leading to neurodegeneration.

    Journal: eNeuro

    Article Title: Intracellular Proteolysis of Progranulin Generates Stable, Lysosomal Granulins that Are Haploinsufficient in Patients with Frontotemporal Dementia Caused by GRN Mutations

    doi: 10.1523/ENEURO.0100-17.2017

    Figure Lengend Snippet: Model of intracellular processing of PGRN into stable, lysosomal GRNs. Sortilin and other receptors target endocytosed and newly synthesized PGRN to lysosomes. Within lysosomes, PGRN is proteolytically cleaved, in part, by cysteine proteases (i.e., cathepsin L) into mature, stable GRN proteins. Ablation of sortilin results in the reduced production of GRNs. Further, lysosome dysfunction caused by alkalizing agents or TMEM106B overexpression inhibits the processing of PGRN into GRNs. FTD- GRN patients are haploinsufficient for GRNs, which may drive lysosome dysfunction leading to neurodegeneration.

    Article Snippet: Cathepsin L inhibitor II (Z-FY-CHO) and ALLN were from Calbiochem.

    Techniques: Synthesized, Over Expression

    Cathepsin activity and cystatin C amount in primary and metastatic human melanoma cells . ( A ) Quantitative cytofluorimetric analysis of plasma membrane cathepsin B, D and L in four different primary (white columns) and metastatic (black columns) melanoma cell lines. Numbers represent the mean values among four different primary or metastatic melanoma cell lines analyzed. ( B ) Fluorimetric assays for cathepsin B (black columns), cathepsin D (grey columns) and cathepsin L (white columns) activity in the cell medium of two representative primary and metastatic melanoma cell lines. Results are reported as fluorescence units. ( C ) Concentration of cystatin C in the growth medium of two representative primary and metastatic melanoma cell lines obtained by ELISA test. Results are reported as ng/ml. (*) p

    Journal: Molecular Cancer

    Article Title: Cathepsin B inhibition interferes with metastatic potential of human melanoma: an in vitro and in vivo study

    doi: 10.1186/1476-4598-9-207

    Figure Lengend Snippet: Cathepsin activity and cystatin C amount in primary and metastatic human melanoma cells . ( A ) Quantitative cytofluorimetric analysis of plasma membrane cathepsin B, D and L in four different primary (white columns) and metastatic (black columns) melanoma cell lines. Numbers represent the mean values among four different primary or metastatic melanoma cell lines analyzed. ( B ) Fluorimetric assays for cathepsin B (black columns), cathepsin D (grey columns) and cathepsin L (white columns) activity in the cell medium of two representative primary and metastatic melanoma cell lines. Results are reported as fluorescence units. ( C ) Concentration of cystatin C in the growth medium of two representative primary and metastatic melanoma cell lines obtained by ELISA test. Results are reported as ng/ml. (*) p

    Article Snippet: For cell migration and invasion assays, cells were seeded in the presence of the cathepsin D inhibitor (Pepstatin A, 100 μM, Calbiochem), the cathepsin L inhibitor (cathepsin L inhibitor II, Z-FY-CHO, 10 μM, Calbiochem) as well as two cathepsin B inhibitors: CA-074 (cell unpermeant) and CA-074Me (cell permeant) (both given at a concentration of 10 μM, Calbiochem, Nottingham, UK).

    Techniques: Activity Assay, Fluorescence, Concentration Assay, Enzyme-linked Immunosorbent Assay

    Cathepsins and in vitro invasiveness: effect of chemical and biological inhibitors . ( A ) Invasion test on primary (white columns) and metastatic (black columns) melanoma cell lines. ( B ) Invasion test on two representative cell lines from primary (white columns) and metastatic (black columns) melanoma in the presence of CA-074 (left panel), Pepstatin A (central panel) or cathepsin L inhibitor (right panel). Dotted lines represent the mean of the results obtained in primary melanoma cell lines, and dashed lines indicate the mean of the results obtained in metastatic melanoma cell lines by using DMSO (vehicle of the cathepsin inhibitors). ( C ) Invasion test on two representative cell lines from primary (white columns) and metastatic (black columns) melanoma in the absence or in the presence of specific antibodies against cathepsin B (left panel), cathepsin D (central panel) or cathepsin L (right panel). Dotted lines represent the mean of the results obtained in primary melanoma cell lines, and dashed lines indicate the mean of the results obtained in metastatic melanoma cell lines by using IgG1 as positive control. ( D ) Histogram showing the results obtained from four different primary melanoma (white columns) or metastatic melanoma (black columns) cell lines in the absence or in the presence of CA-074 or antibodies against cathepsin B. Data are reported as mean ± SD of the percentage of invading cells. Student's t -test indicates: p = 0.0097 for untreated MM cells vs. CA-074-treated MM cells and p = 0.0030 for untreated MM cells vs. MM cells treated with anti-cathepsin B antibodies.

    Journal: Molecular Cancer

    Article Title: Cathepsin B inhibition interferes with metastatic potential of human melanoma: an in vitro and in vivo study

    doi: 10.1186/1476-4598-9-207

    Figure Lengend Snippet: Cathepsins and in vitro invasiveness: effect of chemical and biological inhibitors . ( A ) Invasion test on primary (white columns) and metastatic (black columns) melanoma cell lines. ( B ) Invasion test on two representative cell lines from primary (white columns) and metastatic (black columns) melanoma in the presence of CA-074 (left panel), Pepstatin A (central panel) or cathepsin L inhibitor (right panel). Dotted lines represent the mean of the results obtained in primary melanoma cell lines, and dashed lines indicate the mean of the results obtained in metastatic melanoma cell lines by using DMSO (vehicle of the cathepsin inhibitors). ( C ) Invasion test on two representative cell lines from primary (white columns) and metastatic (black columns) melanoma in the absence or in the presence of specific antibodies against cathepsin B (left panel), cathepsin D (central panel) or cathepsin L (right panel). Dotted lines represent the mean of the results obtained in primary melanoma cell lines, and dashed lines indicate the mean of the results obtained in metastatic melanoma cell lines by using IgG1 as positive control. ( D ) Histogram showing the results obtained from four different primary melanoma (white columns) or metastatic melanoma (black columns) cell lines in the absence or in the presence of CA-074 or antibodies against cathepsin B. Data are reported as mean ± SD of the percentage of invading cells. Student's t -test indicates: p = 0.0097 for untreated MM cells vs. CA-074-treated MM cells and p = 0.0030 for untreated MM cells vs. MM cells treated with anti-cathepsin B antibodies.

    Article Snippet: For cell migration and invasion assays, cells were seeded in the presence of the cathepsin D inhibitor (Pepstatin A, 100 μM, Calbiochem), the cathepsin L inhibitor (cathepsin L inhibitor II, Z-FY-CHO, 10 μM, Calbiochem) as well as two cathepsin B inhibitors: CA-074 (cell unpermeant) and CA-074Me (cell permeant) (both given at a concentration of 10 μM, Calbiochem, Nottingham, UK).

    Techniques: In Vitro, Positive Control

    Cathepsin B expression in cells from primary and metastatic human melanomas . Western blot analysis (left panels) of cathepsin B, cathepsin D, cathepsin L and tubulin in the primary melanoma cell lines PM1 ( A ) and PM2 ( B) and in the metastatic melanoma cell lines MM1 ( A ) and MM2 ( B ). Quantitative flow cytometry analysis (right panels) of plasma membrane cathepsin B in PM1 ( A ) and PM2 ( B ) cell lines and in MM1 ( A ) and MM2 ( B ) cell lines. The values of Western blot signals, reported in the bottom panels of ( A ) and ( B ), were obtained by densitometric analysis and expressed as arbitrary units (a.u.). Numbers in the right panels of ( A ) and ( B ) represent the median fluorescence values. In the right panels of ( A ) and ( B ) statistical analysis performed by non-parametric K/S test is reported.

    Journal: Molecular Cancer

    Article Title: Cathepsin B inhibition interferes with metastatic potential of human melanoma: an in vitro and in vivo study

    doi: 10.1186/1476-4598-9-207

    Figure Lengend Snippet: Cathepsin B expression in cells from primary and metastatic human melanomas . Western blot analysis (left panels) of cathepsin B, cathepsin D, cathepsin L and tubulin in the primary melanoma cell lines PM1 ( A ) and PM2 ( B) and in the metastatic melanoma cell lines MM1 ( A ) and MM2 ( B ). Quantitative flow cytometry analysis (right panels) of plasma membrane cathepsin B in PM1 ( A ) and PM2 ( B ) cell lines and in MM1 ( A ) and MM2 ( B ) cell lines. The values of Western blot signals, reported in the bottom panels of ( A ) and ( B ), were obtained by densitometric analysis and expressed as arbitrary units (a.u.). Numbers in the right panels of ( A ) and ( B ) represent the median fluorescence values. In the right panels of ( A ) and ( B ) statistical analysis performed by non-parametric K/S test is reported.

    Article Snippet: For cell migration and invasion assays, cells were seeded in the presence of the cathepsin D inhibitor (Pepstatin A, 100 μM, Calbiochem), the cathepsin L inhibitor (cathepsin L inhibitor II, Z-FY-CHO, 10 μM, Calbiochem) as well as two cathepsin B inhibitors: CA-074 (cell unpermeant) and CA-074Me (cell permeant) (both given at a concentration of 10 μM, Calbiochem, Nottingham, UK).

    Techniques: Expressing, Western Blot, Flow Cytometry, Cytometry, Fluorescence

    Effect of cathepsin K inhibitor II on resting cell length ( A ), PS ( B ), and time to 90% relengthening ( C ) of cardiomyocytes isolated from normal diet (ND)-fed and high-fat diet (HFD)-fed wild-type mice. Data are means ± SEM, n = 50 cardiomyocytes per group. * P

    Journal: Diabetes

    Article Title: Cathepsin K Knockout Mitigates High-Fat Diet-Induced Cardiac Hypertrophy and Contractile Dysfunction

    doi: 10.2337/db12-0350

    Figure Lengend Snippet: Effect of cathepsin K inhibitor II on resting cell length ( A ), PS ( B ), and time to 90% relengthening ( C ) of cardiomyocytes isolated from normal diet (ND)-fed and high-fat diet (HFD)-fed wild-type mice. Data are means ± SEM, n = 50 cardiomyocytes per group. * P

    Article Snippet: For experiments involving the inhibition of cathepsin K, isolated cardiomyocyte from high-fat diet–fed wild-type mice were incubated for 2 h with various concentration of cathepsin K inhibitor II (Calbiochem).

    Techniques: Isolation, Mouse Assay

    Echocardiographic features in wild-type (WT) and cathepsin K knockout mice fed normal diet or high-fat diet. A : Left ventricular wall thickness. B : LVEDD. C : LVESD. D : Fraction shortening [(LVEDD − LVESD) / LVEDD × 100]. Mean ± SEM, n = 6–7 mice per group, * P

    Journal: Diabetes

    Article Title: Cathepsin K Knockout Mitigates High-Fat Diet-Induced Cardiac Hypertrophy and Contractile Dysfunction

    doi: 10.2337/db12-0350

    Figure Lengend Snippet: Echocardiographic features in wild-type (WT) and cathepsin K knockout mice fed normal diet or high-fat diet. A : Left ventricular wall thickness. B : LVEDD. C : LVESD. D : Fraction shortening [(LVEDD − LVESD) / LVEDD × 100]. Mean ± SEM, n = 6–7 mice per group, * P

    Article Snippet: For experiments involving the inhibition of cathepsin K, isolated cardiomyocyte from high-fat diet–fed wild-type mice were incubated for 2 h with various concentration of cathepsin K inhibitor II (Calbiochem).

    Techniques: Knock-Out, Mouse Assay

    A and B : Effect of cathepsin K knockout on glucose disposal in mice fed a normal diet (ND) or a high-fat diet (HFD) after an intraperitoneal glucose (2 g/kg, body weight) challenge ( A ). Integrated area under the postglucose challenge, glucose-disposal curve ( B ). C : Effect of ND and HFD, respectively, on body weight gain over a 20-week period in wild-type and cathepsin K knockout mice. D : Representative images of wild-type (WT) and cathepsin K knockout mice fed ND or HFD and representative hearts from each group. E–H : Effect of cathepsin K knockout on HFD-induced cardiac hypertrophy. Representative images using wheat germ agglutinin staining of the left ventricular tissue ( E ), quantitation of cardiomyocyte cross-sectional area ( F ), and representative gel blots for GATA4, NFATc3, ANP, and GAPDH (loading control) ( G ), and size of isolated cardiomyocytes ( H ). Data are represented as mean ± SEM, n = 5–7 mice per group, * P

    Journal: Diabetes

    Article Title: Cathepsin K Knockout Mitigates High-Fat Diet-Induced Cardiac Hypertrophy and Contractile Dysfunction

    doi: 10.2337/db12-0350

    Figure Lengend Snippet: A and B : Effect of cathepsin K knockout on glucose disposal in mice fed a normal diet (ND) or a high-fat diet (HFD) after an intraperitoneal glucose (2 g/kg, body weight) challenge ( A ). Integrated area under the postglucose challenge, glucose-disposal curve ( B ). C : Effect of ND and HFD, respectively, on body weight gain over a 20-week period in wild-type and cathepsin K knockout mice. D : Representative images of wild-type (WT) and cathepsin K knockout mice fed ND or HFD and representative hearts from each group. E–H : Effect of cathepsin K knockout on HFD-induced cardiac hypertrophy. Representative images using wheat germ agglutinin staining of the left ventricular tissue ( E ), quantitation of cardiomyocyte cross-sectional area ( F ), and representative gel blots for GATA4, NFATc3, ANP, and GAPDH (loading control) ( G ), and size of isolated cardiomyocytes ( H ). Data are represented as mean ± SEM, n = 5–7 mice per group, * P

    Article Snippet: For experiments involving the inhibition of cathepsin K, isolated cardiomyocyte from high-fat diet–fed wild-type mice were incubated for 2 h with various concentration of cathepsin K inhibitor II (Calbiochem).

    Techniques: Knock-Out, Mouse Assay, Staining, Quantitation Assay, Aqueous Normal-phase Chromatography, Isolation

    Cardiomyocyte contractile properties in wild-type (WT) and cathepsin K knockout mice fed normal diet (ND) or high-fat diet (HFD). A and B : Representative traces from cardiomyocytes isolated from wild-type and cathepsin K knockout mice. C–H : Resting cell length, peak shortening (normalized to cell length), maximal velocity of shortening (+dL/dt), maximal velocity of relengthening (−dL/dt), time-to-peak shortening (TPS), and time to 90% relengthening (TR 90 ), respectively. Mean ± SEM, n = 76–87 cells per group. * P

    Journal: Diabetes

    Article Title: Cathepsin K Knockout Mitigates High-Fat Diet-Induced Cardiac Hypertrophy and Contractile Dysfunction

    doi: 10.2337/db12-0350

    Figure Lengend Snippet: Cardiomyocyte contractile properties in wild-type (WT) and cathepsin K knockout mice fed normal diet (ND) or high-fat diet (HFD). A and B : Representative traces from cardiomyocytes isolated from wild-type and cathepsin K knockout mice. C–H : Resting cell length, peak shortening (normalized to cell length), maximal velocity of shortening (+dL/dt), maximal velocity of relengthening (−dL/dt), time-to-peak shortening (TPS), and time to 90% relengthening (TR 90 ), respectively. Mean ± SEM, n = 76–87 cells per group. * P

    Article Snippet: For experiments involving the inhibition of cathepsin K, isolated cardiomyocyte from high-fat diet–fed wild-type mice were incubated for 2 h with various concentration of cathepsin K inhibitor II (Calbiochem).

    Techniques: Knock-Out, Mouse Assay, Isolation

    Intracellular Ca 2+ transients in cardiomyocytes and expression levels of proteins related to intracellular Ca 2+ handling in wild-type (WT) and cathepsin K knockout mice fed a normal diet (ND) or high-fat diet (HFD). A–D : Resting fura-2 fluorescence intensity (FFI), electrically stimulated increase in FFI (ΔFFI), single exponential intracellular Ca 2+ decay, and peak FFI, respectively. E : Representative Western blot images for phospho-phospholamban, phospholamban (PLB), SERCA2, and GAPDH (loading control). F–H : Densitometric quantitation of SERCA normalized to GAPDH, PLB normalized to GAPDH, and PBL-to-SERCA ratio, respectively. Mean ± SEM, n = 94–100 cells or 5–7 mice per group. * P

    Journal: Diabetes

    Article Title: Cathepsin K Knockout Mitigates High-Fat Diet-Induced Cardiac Hypertrophy and Contractile Dysfunction

    doi: 10.2337/db12-0350

    Figure Lengend Snippet: Intracellular Ca 2+ transients in cardiomyocytes and expression levels of proteins related to intracellular Ca 2+ handling in wild-type (WT) and cathepsin K knockout mice fed a normal diet (ND) or high-fat diet (HFD). A–D : Resting fura-2 fluorescence intensity (FFI), electrically stimulated increase in FFI (ΔFFI), single exponential intracellular Ca 2+ decay, and peak FFI, respectively. E : Representative Western blot images for phospho-phospholamban, phospholamban (PLB), SERCA2, and GAPDH (loading control). F–H : Densitometric quantitation of SERCA normalized to GAPDH, PLB normalized to GAPDH, and PBL-to-SERCA ratio, respectively. Mean ± SEM, n = 94–100 cells or 5–7 mice per group. * P

    Article Snippet: For experiments involving the inhibition of cathepsin K, isolated cardiomyocyte from high-fat diet–fed wild-type mice were incubated for 2 h with various concentration of cathepsin K inhibitor II (Calbiochem).

    Techniques: Expressing, Knock-Out, Mouse Assay, Fluorescence, Western Blot, Quantitation Assay

    A : Immunolocalization of cathepsin K in cultured cells. H9c2 myoblasts were labeled using lysosomal dye and fluorogenic substrate MR-(LR) 2 , which detects active cathepsin K. Upper panel (merged figure) shows colocalization of cathepsin K in lysosomes under basal conditions. On stimulation with palmitic acid, active cathepsin K was released from lysosomes to the cytoplasm (indicated by arrows). B–E . Effect of cathepsin K knockout on cardiac insulin signaling molecules in normal diet (ND)-fed and high-fat diet (HFD)-fed mice. Mice were challenged with insulin (1.5 U/100 g body weight, intraperitoneally) for 10 min before isolation of the heart tissue for Western blot. Insulin-stimulated phosphorylation of Akt (indicated by an asterisk), total Akt, basal phospho-Akt, basal levels of insulin receptor-β, and glucose transporter-4 (Glut4) were assessed by Western blotting ( B ) and quantitated by densitometry ( C–E ). F and G : Effect of cathepsin K knockout on the protein levels of other cathepsins in ND-fed and HFD-fed mice. Mean ± SEM, n = 3–4 per group. WT, wild-type. * P

    Journal: Diabetes

    Article Title: Cathepsin K Knockout Mitigates High-Fat Diet-Induced Cardiac Hypertrophy and Contractile Dysfunction

    doi: 10.2337/db12-0350

    Figure Lengend Snippet: A : Immunolocalization of cathepsin K in cultured cells. H9c2 myoblasts were labeled using lysosomal dye and fluorogenic substrate MR-(LR) 2 , which detects active cathepsin K. Upper panel (merged figure) shows colocalization of cathepsin K in lysosomes under basal conditions. On stimulation with palmitic acid, active cathepsin K was released from lysosomes to the cytoplasm (indicated by arrows). B–E . Effect of cathepsin K knockout on cardiac insulin signaling molecules in normal diet (ND)-fed and high-fat diet (HFD)-fed mice. Mice were challenged with insulin (1.5 U/100 g body weight, intraperitoneally) for 10 min before isolation of the heart tissue for Western blot. Insulin-stimulated phosphorylation of Akt (indicated by an asterisk), total Akt, basal phospho-Akt, basal levels of insulin receptor-β, and glucose transporter-4 (Glut4) were assessed by Western blotting ( B ) and quantitated by densitometry ( C–E ). F and G : Effect of cathepsin K knockout on the protein levels of other cathepsins in ND-fed and HFD-fed mice. Mean ± SEM, n = 3–4 per group. WT, wild-type. * P

    Article Snippet: For experiments involving the inhibition of cathepsin K, isolated cardiomyocyte from high-fat diet–fed wild-type mice were incubated for 2 h with various concentration of cathepsin K inhibitor II (Calbiochem).

    Techniques: Cell Culture, Labeling, Knock-Out, Mouse Assay, Isolation, Western Blot

    Altered IR-induced nuclear translocation of NF-κB following selective inhibition of cathepsin L with Z-FY-CHO or cathepsin L shRNA. (A) p65 protein immunofluorescence in U251 cells treated with Z-FY-CHO, IR, or both. (B) p65 protein immunofluorescence

    Journal: Acta Pharmacologica Sinica

    Article Title: Inhibition of cathepsin L sensitizes human glioma cells to ionizing radiation in vitro through NF-κB signaling pathway

    doi: 10.1038/aps.2014.148

    Figure Lengend Snippet: Altered IR-induced nuclear translocation of NF-κB following selective inhibition of cathepsin L with Z-FY-CHO or cathepsin L shRNA. (A) p65 protein immunofluorescence in U251 cells treated with Z-FY-CHO, IR, or both. (B) p65 protein immunofluorescence

    Article Snippet: Cathepsin L inhibitor II (Z-FY-CHO) was purchased from Calbiochem (La Jolla, CA, USA).

    Techniques: Translocation Assay, Inhibition, shRNA, Immunofluorescence

    Reduced NF-κB-dependent transcriptional activation in U251 cells following IR with selective inhibition of cathepsin L with Z-FY-CHO (A) or cathepsin L shRNA (B). NF-κB activity was assessed using an NF-κB-RE firefly luciferase

    Journal: Acta Pharmacologica Sinica

    Article Title: Inhibition of cathepsin L sensitizes human glioma cells to ionizing radiation in vitro through NF-κB signaling pathway

    doi: 10.1038/aps.2014.148

    Figure Lengend Snippet: Reduced NF-κB-dependent transcriptional activation in U251 cells following IR with selective inhibition of cathepsin L with Z-FY-CHO (A) or cathepsin L shRNA (B). NF-κB activity was assessed using an NF-κB-RE firefly luciferase

    Article Snippet: Cathepsin L inhibitor II (Z-FY-CHO) was purchased from Calbiochem (La Jolla, CA, USA).

    Techniques: Activation Assay, Inhibition, shRNA, Activity Assay, Luciferase

    The inhibition of cathepsin L sensitized U251 cells to IR. (A) Clonogenic survival curves for U251 cells treated with radiation (0, 2, 4, 6, and 8 Gy) alone or in combination with Z-FY-CHO. (B) Western blot of CTSL in whole cell extracts from parental

    Journal: Acta Pharmacologica Sinica

    Article Title: Inhibition of cathepsin L sensitizes human glioma cells to ionizing radiation in vitro through NF-κB signaling pathway

    doi: 10.1038/aps.2014.148

    Figure Lengend Snippet: The inhibition of cathepsin L sensitized U251 cells to IR. (A) Clonogenic survival curves for U251 cells treated with radiation (0, 2, 4, 6, and 8 Gy) alone or in combination with Z-FY-CHO. (B) Western blot of CTSL in whole cell extracts from parental

    Article Snippet: Cathepsin L inhibitor II (Z-FY-CHO) was purchased from Calbiochem (La Jolla, CA, USA).

    Techniques: Inhibition, Western Blot

    Altered IR-induced nuclear translocation of NF-κB following selective inhibition of cathepsin L with Z-FY-CHO or cathepsin L shRNA. (A) Western blot analysis of IκBα expression and the nuclear translocation of NF-κB in

    Journal: Acta Pharmacologica Sinica

    Article Title: Inhibition of cathepsin L sensitizes human glioma cells to ionizing radiation in vitro through NF-κB signaling pathway

    doi: 10.1038/aps.2014.148

    Figure Lengend Snippet: Altered IR-induced nuclear translocation of NF-κB following selective inhibition of cathepsin L with Z-FY-CHO or cathepsin L shRNA. (A) Western blot analysis of IκBα expression and the nuclear translocation of NF-κB in

    Article Snippet: Cathepsin L inhibitor II (Z-FY-CHO) was purchased from Calbiochem (La Jolla, CA, USA).

    Techniques: Translocation Assay, Inhibition, shRNA, Western Blot, Expressing

    The expression of cathepsin L protein and nuclear translocation of NF-κB p65 and p50 in U251 cells following IR was analyzed by Western blot. (A) Western blot analysis of cathepsin L in U251 cells treated with IR (10 Gy). β-Actin was used

    Journal: Acta Pharmacologica Sinica

    Article Title: Inhibition of cathepsin L sensitizes human glioma cells to ionizing radiation in vitro through NF-κB signaling pathway

    doi: 10.1038/aps.2014.148

    Figure Lengend Snippet: The expression of cathepsin L protein and nuclear translocation of NF-κB p65 and p50 in U251 cells following IR was analyzed by Western blot. (A) Western blot analysis of cathepsin L in U251 cells treated with IR (10 Gy). β-Actin was used

    Article Snippet: Cathepsin L inhibitor II (Z-FY-CHO) was purchased from Calbiochem (La Jolla, CA, USA).

    Techniques: Expressing, Translocation Assay, Western Blot

    Effect of p65 shRNA on the expression of p65 and cathepsin L in U251 and MCF-7 cells. (A) Western blot of p65 whole cell extracts from normal U251, U251-consh and U251-p65sh cells. β-Actin was used as an internal control. c P

    Journal: Acta Pharmacologica Sinica

    Article Title: Inhibition of cathepsin L sensitizes human glioma cells to ionizing radiation in vitro through NF-κB signaling pathway

    doi: 10.1038/aps.2014.148

    Figure Lengend Snippet: Effect of p65 shRNA on the expression of p65 and cathepsin L in U251 and MCF-7 cells. (A) Western blot of p65 whole cell extracts from normal U251, U251-consh and U251-p65sh cells. β-Actin was used as an internal control. c P

    Article Snippet: Cathepsin L inhibitor II (Z-FY-CHO) was purchased from Calbiochem (La Jolla, CA, USA).

    Techniques: shRNA, Expressing, Western Blot