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HEK293 cells transfected with MT1-MMP cDNA invade 3D collagen gels in response to LPA . (A) Tumor cell lysates were prepared for Western blot analysis. Lysates were probed for MT1-MMP to assess protein expression in the four tumor cell lines. Lysates were probed for Actin as a loading control. (B) HEK293 cells were transfected with the pAdTrack-CMV plasmid as a control, or plasmids encoding MT1-MMP, MT2-MMP, or MT3-MMP cDNA 24 hours prior to placement in invasion assays. Cells were allowed to invade 2.0 mg/ml collagen gels in the presence or absence of 1 μM LPA. Data are expressed as mean numbers of invading cells per HPF (20×) (± S.D.) from a minimum of 20 fields. (C) Lysates from HEK293 cells transfected with cDNAs encoding the designated genes were prepared for Western blot analysis and probed for GFP, MT1-MMP, MT2-MMP, MT3-MMP, or Actin as a loading control. TRK = pAdTrack-CMV, MT1 = MT1-MMP, MT2 = MT2-MMP, MT3 = MT3-MMP.

Journal: Molecular Cancer

Article Title: Tumor cell invasion of collagen matrices requires coordinate lipid agonist-induced G-protein and membrane-type matrix metalloproteinase-1-dependent signaling

doi: 10.1186/1476-4598-5-69

Figure Lengend Snippet: HEK293 cells transfected with MT1-MMP cDNA invade 3D collagen gels in response to LPA . (A) Tumor cell lysates were prepared for Western blot analysis. Lysates were probed for MT1-MMP to assess protein expression in the four tumor cell lines. Lysates were probed for Actin as a loading control. (B) HEK293 cells were transfected with the pAdTrack-CMV plasmid as a control, or plasmids encoding MT1-MMP, MT2-MMP, or MT3-MMP cDNA 24 hours prior to placement in invasion assays. Cells were allowed to invade 2.0 mg/ml collagen gels in the presence or absence of 1 μM LPA. Data are expressed as mean numbers of invading cells per HPF (20×) (± S.D.) from a minimum of 20 fields. (C) Lysates from HEK293 cells transfected with cDNAs encoding the designated genes were prepared for Western blot analysis and probed for GFP, MT1-MMP, MT2-MMP, MT3-MMP, or Actin as a loading control. TRK = pAdTrack-CMV, MT1 = MT1-MMP, MT2 = MT2-MMP, MT3 = MT3-MMP.

Article Snippet: A plasmid encoding human MT2-MMP (TC118648) was purchased from Origene (Rockville, MD).

Techniques: Transfection, Western Blot, Expressing, Plasmid Preparation

Identification of the KLK14 hydrolysis sites within the CleavEx proMMP protein. CleavEx proMMP fusion proteins were separated using SDS-PAGE and electrotransferred for N-terminal sequencing. Identified sequences are represented in the bold font and the underscore denotes where the location of the expected activation cleavage P1-P1′ in the proMMP-derived sequence.

Journal: International Journal of Molecular Sciences

Article Title: Kallikrein-Related Peptidase 14 Activates Zymogens of Membrane Type Matrix Metalloproteinases (MT-MMPs)—A CleavEx Based Analysis

doi: 10.3390/ijms21124383

Figure Lengend Snippet: Identification of the KLK14 hydrolysis sites within the CleavEx proMMP protein. CleavEx proMMP fusion proteins were separated using SDS-PAGE and electrotransferred for N-terminal sequencing. Identified sequences are represented in the bold font and the underscore denotes where the location of the expected activation cleavage P1-P1′ in the proMMP-derived sequence.

Article Snippet: A total of 0.5 μg native proMMP2 (catalog no. 902-MP-010, R&D Systems, Abingdon, United Kingdom), 0.5 μg proMMP14 (catalog no. 918-MP-010, R&D Systems), 1 μg proMMP15 (catalog no. 916-MP-010, R&D Systems), 0.5 μg proMMP16 (catalog no. 1785-MP-010, R&D Systems), and 1 μg proMMP17 (catalog no. 7796-MP-010, R&D Systems) were separately incubated in 10 μL with a range of KLK14 concentrations (25–250 nM, with molar ratios from around 1:65 to 1:10 KLK14:MMP) in the presence of 5 μM batimastat (Sigma-Aldrich, St. Louis, MO, USA) for 1 h at 37 °C in PBS.

Techniques: Sequencing, Activation Assay

N-terminal identification of KLK14-mediated processing of recombinant proMMPs. The KLK14 hydrolysis product sequences were analyzed by N-terminal sequencing using Edman degradation. The bold font denotes the amino acid sequences identified. The underscored residues represent changes to the native protein sequence, as reported by the manufacturer (R&D Systems, Abingdon, United Kingdom). KLK14 recognized the sequence 3-aa upstream of the native MMP17 activation site, likely because the native site was modified by the manufacturer. All residues are numbered according to the Uniprot reported sequence of the full-length proteins. Bands are labeled according to the notation explained at <xref ref-type= Figure 2 ." width="100%" height="100%">

Journal: International Journal of Molecular Sciences

Article Title: Kallikrein-Related Peptidase 14 Activates Zymogens of Membrane Type Matrix Metalloproteinases (MT-MMPs)—A CleavEx Based Analysis

doi: 10.3390/ijms21124383

Figure Lengend Snippet: N-terminal identification of KLK14-mediated processing of recombinant proMMPs. The KLK14 hydrolysis product sequences were analyzed by N-terminal sequencing using Edman degradation. The bold font denotes the amino acid sequences identified. The underscored residues represent changes to the native protein sequence, as reported by the manufacturer (R&D Systems, Abingdon, United Kingdom). KLK14 recognized the sequence 3-aa upstream of the native MMP17 activation site, likely because the native site was modified by the manufacturer. All residues are numbered according to the Uniprot reported sequence of the full-length proteins. Bands are labeled according to the notation explained at Figure 2 .

Article Snippet: A total of 0.5 μg native proMMP2 (catalog no. 902-MP-010, R&D Systems, Abingdon, United Kingdom), 0.5 μg proMMP14 (catalog no. 918-MP-010, R&D Systems), 1 μg proMMP15 (catalog no. 916-MP-010, R&D Systems), 0.5 μg proMMP16 (catalog no. 1785-MP-010, R&D Systems), and 1 μg proMMP17 (catalog no. 7796-MP-010, R&D Systems) were separately incubated in 10 μL with a range of KLK14 concentrations (25–250 nM, with molar ratios from around 1:65 to 1:10 KLK14:MMP) in the presence of 5 μM batimastat (Sigma-Aldrich, St. Louis, MO, USA) for 1 h at 37 °C in PBS.

Techniques: Recombinant, Sequencing, Activation Assay, Modification, Labeling

Gelatin zymography of proMMPs by KLK14-mediated processing. Activation of proMMPs by KLK14 results in a fully functional mature enzyme. Each proMMP was incubated with the indicated concentrations of KLK14 for 1 h at 37 °C. The reaction was stopped by the addition of KLK14-specific inhibitors, and the reaction mixture was analyzed by SDS-PAGE, followed by a zymogram with gelatin as a substrate. The proMMP2 ( A ) negative control was not activated. ProMMP14 ( B ), proMMP15 ( C ), and proMMP16 ( D ) were activated, whereas proMMP17 ( E ) did not show hydrolysis of gelatin; yet a shift corresponding to the loss of the profragment was observed (note that an amino acid substitution was introduced in proMMP17 by the manufacturer (R&D Systems, Abingdon, United Kingdom)). KLK = kallikrein-related peptidase; MMP = matrix metalloproteinase.

Journal: International Journal of Molecular Sciences

Article Title: Kallikrein-Related Peptidase 14 Activates Zymogens of Membrane Type Matrix Metalloproteinases (MT-MMPs)—A CleavEx Based Analysis

doi: 10.3390/ijms21124383

Figure Lengend Snippet: Gelatin zymography of proMMPs by KLK14-mediated processing. Activation of proMMPs by KLK14 results in a fully functional mature enzyme. Each proMMP was incubated with the indicated concentrations of KLK14 for 1 h at 37 °C. The reaction was stopped by the addition of KLK14-specific inhibitors, and the reaction mixture was analyzed by SDS-PAGE, followed by a zymogram with gelatin as a substrate. The proMMP2 ( A ) negative control was not activated. ProMMP14 ( B ), proMMP15 ( C ), and proMMP16 ( D ) were activated, whereas proMMP17 ( E ) did not show hydrolysis of gelatin; yet a shift corresponding to the loss of the profragment was observed (note that an amino acid substitution was introduced in proMMP17 by the manufacturer (R&D Systems, Abingdon, United Kingdom)). KLK = kallikrein-related peptidase; MMP = matrix metalloproteinase.

Article Snippet: A total of 0.5 μg native proMMP2 (catalog no. 902-MP-010, R&D Systems, Abingdon, United Kingdom), 0.5 μg proMMP14 (catalog no. 918-MP-010, R&D Systems), 1 μg proMMP15 (catalog no. 916-MP-010, R&D Systems), 0.5 μg proMMP16 (catalog no. 1785-MP-010, R&D Systems), and 1 μg proMMP17 (catalog no. 7796-MP-010, R&D Systems) were separately incubated in 10 μL with a range of KLK14 concentrations (25–250 nM, with molar ratios from around 1:65 to 1:10 KLK14:MMP) in the presence of 5 μM batimastat (Sigma-Aldrich, St. Louis, MO, USA) for 1 h at 37 °C in PBS.

Techniques: Zymography, Activation Assay, Functional Assay, Incubation, SDS Page, Negative Control

Primers used for generating the proMMP CleavEx fusion proteins using three consecutive PCRs.

Journal: International Journal of Molecular Sciences

Article Title: Kallikrein-Related Peptidase 14 Activates Zymogens of Membrane Type Matrix Metalloproteinases (MT-MMPs)—A CleavEx Based Analysis

doi: 10.3390/ijms21124383

Figure Lengend Snippet: Primers used for generating the proMMP CleavEx fusion proteins using three consecutive PCRs.

Article Snippet: A total of 0.5 μg native proMMP2 (catalog no. 902-MP-010, R&D Systems, Abingdon, United Kingdom), 0.5 μg proMMP14 (catalog no. 918-MP-010, R&D Systems), 1 μg proMMP15 (catalog no. 916-MP-010, R&D Systems), 0.5 μg proMMP16 (catalog no. 1785-MP-010, R&D Systems), and 1 μg proMMP17 (catalog no. 7796-MP-010, R&D Systems) were separately incubated in 10 μL with a range of KLK14 concentrations (25–250 nM, with molar ratios from around 1:65 to 1:10 KLK14:MMP) in the presence of 5 μM batimastat (Sigma-Aldrich, St. Louis, MO, USA) for 1 h at 37 °C in PBS.

Techniques: Sequencing