cp rat model Search Results


high fat western type diet  (Inotiv)
99
Inotiv high fat western type diet
Effects of adenoviral-mediated expression of kinase-inactive (KI) PKC-ζ on basal and feeding-induced activities of aPKC (A), PKB (B), and IRS-1–dependent PI3K (C) in vastus lateralis muscle, serum insulin levels (D), and basal and feeding-induced activity of aPKC (E), expression and nuclear levels of SREBP-1c (F), and expression of FAS (G) and ACC (H) in liver of <t>high-fat–fed</t> mice. High-fat–fed mice were injected IV with adenovirus vector (Vec) or adenovirus encoding KI-PKC-ζ (KI-ζ) and 4 days later (to allow time for expression), mice were fasted overnight 16–20 h (clear bars) or maintained on the high-fat diet (shaded bars). For comparisons in assays, normal-chow–fed mice were similarly fasted or maintained on their usual normal chow (low-fat) diet. The mice were killed on the next day (fifth day after initial virus treatment), and muscles, livers, and sera were harvested. In the inset in panel A, aPKCs were immunoprecipitated from muscles of normal-chow–fed (LO) or high-fat–fed (HI) mice treated with adenovirus vector (VEC) or adenovirus encoding KI-ζ, and assayed in absence (clear bars) or presence (shaded bars) of 10 μM PIP3. Values are mean ± SEM of (N) determinations. Asterisks indicate P < 0.05 (*), P < 0.01 (**), and P < 0.001 (***) for feeding-stimulated values versus adjacent fasting values of mice fed a comparable high or normal (low fat) diet, or in the inset of panel A, PIP3-treated versus untreated. Portrayed P values depict comparisons of indicated groups (viz., insulin-stimulated adenovirus vector versus insulin-stimulated adenovirus encoding KI-PKC-ζ in high-fat–fed mice). All P values were determined by ANOVA. Insets show 10 μM PIP3-dependent activation of aPKC immunoprecipitated from muscles of indicated mice (Panel A); representative autoradiograms of PI-3-32PO4, the lipid product of the PI3K assay (C); expressed KI-PKC-ζ–induced increases in levels of hepatic total aPKC (E); and a representative immunoblot of the active nuclear SREBP-1 fragment (F).
High Fat Western Type Diet, supplied by Inotiv, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/cp+rat+model/pmc02681395-39-54-58?v=Inotiv
Average 99 stars, based on 1 article reviews
high fat western type diet - by Bioz Stars, 2026-08
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drug model pathway taxol  (Gilead Sciences)
97
Gilead Sciences drug model pathway taxol
Effects of adenoviral-mediated expression of kinase-inactive (KI) PKC-ζ on basal and feeding-induced activities of aPKC (A), PKB (B), and IRS-1–dependent PI3K (C) in vastus lateralis muscle, serum insulin levels (D), and basal and feeding-induced activity of aPKC (E), expression and nuclear levels of SREBP-1c (F), and expression of FAS (G) and ACC (H) in liver of <t>high-fat–fed</t> mice. High-fat–fed mice were injected IV with adenovirus vector (Vec) or adenovirus encoding KI-PKC-ζ (KI-ζ) and 4 days later (to allow time for expression), mice were fasted overnight 16–20 h (clear bars) or maintained on the high-fat diet (shaded bars). For comparisons in assays, normal-chow–fed mice were similarly fasted or maintained on their usual normal chow (low-fat) diet. The mice were killed on the next day (fifth day after initial virus treatment), and muscles, livers, and sera were harvested. In the inset in panel A, aPKCs were immunoprecipitated from muscles of normal-chow–fed (LO) or high-fat–fed (HI) mice treated with adenovirus vector (VEC) or adenovirus encoding KI-ζ, and assayed in absence (clear bars) or presence (shaded bars) of 10 μM PIP3. Values are mean ± SEM of (N) determinations. Asterisks indicate P < 0.05 (*), P < 0.01 (**), and P < 0.001 (***) for feeding-stimulated values versus adjacent fasting values of mice fed a comparable high or normal (low fat) diet, or in the inset of panel A, PIP3-treated versus untreated. Portrayed P values depict comparisons of indicated groups (viz., insulin-stimulated adenovirus vector versus insulin-stimulated adenovirus encoding KI-PKC-ζ in high-fat–fed mice). All P values were determined by ANOVA. Insets show 10 μM PIP3-dependent activation of aPKC immunoprecipitated from muscles of indicated mice (Panel A); representative autoradiograms of PI-3-32PO4, the lipid product of the PI3K assay (C); expressed KI-PKC-ζ–induced increases in levels of hepatic total aPKC (E); and a representative immunoblot of the active nuclear SREBP-1 fragment (F).
Drug Model Pathway Taxol, supplied by Gilead Sciences, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/cp+rat+model/pm25124145-66-0-22?v=Gilead+Sciences
Average 97 stars, based on 1 article reviews
drug model pathway taxol - by Bioz Stars, 2026-08
97/100 stars
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Image Search Results


Effects of adenoviral-mediated expression of kinase-inactive (KI) PKC-ζ on basal and feeding-induced activities of aPKC (A), PKB (B), and IRS-1–dependent PI3K (C) in vastus lateralis muscle, serum insulin levels (D), and basal and feeding-induced activity of aPKC (E), expression and nuclear levels of SREBP-1c (F), and expression of FAS (G) and ACC (H) in liver of high-fat–fed mice. High-fat–fed mice were injected IV with adenovirus vector (Vec) or adenovirus encoding KI-PKC-ζ (KI-ζ) and 4 days later (to allow time for expression), mice were fasted overnight 16–20 h (clear bars) or maintained on the high-fat diet (shaded bars). For comparisons in assays, normal-chow–fed mice were similarly fasted or maintained on their usual normal chow (low-fat) diet. The mice were killed on the next day (fifth day after initial virus treatment), and muscles, livers, and sera were harvested. In the inset in panel A, aPKCs were immunoprecipitated from muscles of normal-chow–fed (LO) or high-fat–fed (HI) mice treated with adenovirus vector (VEC) or adenovirus encoding KI-ζ, and assayed in absence (clear bars) or presence (shaded bars) of 10 μM PIP3. Values are mean ± SEM of (N) determinations. Asterisks indicate P < 0.05 (*), P < 0.01 (**), and P < 0.001 (***) for feeding-stimulated values versus adjacent fasting values of mice fed a comparable high or normal (low fat) diet, or in the inset of panel A, PIP3-treated versus untreated. Portrayed P values depict comparisons of indicated groups (viz., insulin-stimulated adenovirus vector versus insulin-stimulated adenovirus encoding KI-PKC-ζ in high-fat–fed mice). All P values were determined by ANOVA. Insets show 10 μM PIP3-dependent activation of aPKC immunoprecipitated from muscles of indicated mice (Panel A); representative autoradiograms of PI-3-32PO4, the lipid product of the PI3K assay (C); expressed KI-PKC-ζ–induced increases in levels of hepatic total aPKC (E); and a representative immunoblot of the active nuclear SREBP-1 fragment (F).

Journal:

Article Title: The critical role of atypical protein kinase C in activating hepatic SREBP-1c and NF?B in obesity

doi: 10.1194/jlr.M800520-JLR200

Figure Lengend Snippet: Effects of adenoviral-mediated expression of kinase-inactive (KI) PKC-ζ on basal and feeding-induced activities of aPKC (A), PKB (B), and IRS-1–dependent PI3K (C) in vastus lateralis muscle, serum insulin levels (D), and basal and feeding-induced activity of aPKC (E), expression and nuclear levels of SREBP-1c (F), and expression of FAS (G) and ACC (H) in liver of high-fat–fed mice. High-fat–fed mice were injected IV with adenovirus vector (Vec) or adenovirus encoding KI-PKC-ζ (KI-ζ) and 4 days later (to allow time for expression), mice were fasted overnight 16–20 h (clear bars) or maintained on the high-fat diet (shaded bars). For comparisons in assays, normal-chow–fed mice were similarly fasted or maintained on their usual normal chow (low-fat) diet. The mice were killed on the next day (fifth day after initial virus treatment), and muscles, livers, and sera were harvested. In the inset in panel A, aPKCs were immunoprecipitated from muscles of normal-chow–fed (LO) or high-fat–fed (HI) mice treated with adenovirus vector (VEC) or adenovirus encoding KI-ζ, and assayed in absence (clear bars) or presence (shaded bars) of 10 μM PIP3. Values are mean ± SEM of (N) determinations. Asterisks indicate P < 0.05 (*), P < 0.01 (**), and P < 0.001 (***) for feeding-stimulated values versus adjacent fasting values of mice fed a comparable high or normal (low fat) diet, or in the inset of panel A, PIP3-treated versus untreated. Portrayed P values depict comparisons of indicated groups (viz., insulin-stimulated adenovirus vector versus insulin-stimulated adenovirus encoding KI-PKC-ζ in high-fat–fed mice). All P values were determined by ANOVA. Insets show 10 μM PIP3-dependent activation of aPKC immunoprecipitated from muscles of indicated mice (Panel A); representative autoradiograms of PI-3-32PO4, the lipid product of the PI3K assay (C); expressed KI-PKC-ζ–induced increases in levels of hepatic total aPKC (E); and a representative immunoblot of the active nuclear SREBP-1 fragment (F).

Article Snippet: Experimental mice In HFF studies, male C57Bl/6 mice, 8–12 weeks of age, were obtained from Harlan Industries, housed in a temperature-controlled environment with alternating 12-h light and dark cycles, and fed ad lib with either a standard low-fat laboratory chow diet [Harlan Teklad 20/18 with 5% fat (i.e., 10% of calories)] or a moderately high-fat Western-type diet [Harlan Teklad {"type":"entrez-nucleotide","attrs":{"text":"T01064","term_id":"277545","term_text":"T01064"}} T01064 with 20% by weight anhydrous milk fat and 1% corn oil (i.e., 42% of calories with fatty acid composition in g fatty acid-length:unsaturation/kg diet as follows: butyric-4:0, 7.6; caproic-6:0, 4.6; caprylic-8:0, 2.2; capric-10:0, 4; capric-11:0, 0.2; lauric-12:0, 6.2; myristic-14:0, 23.4; myristic-14:1, 1.6; myristic-15:0, 3.2; palmitic-16:0, 53.6; palmitoleic-16:1, 3.8; margaric-17:0, 1.4; margaric-17:1, 0.4; stearic-18:0, 25.2; oleic-18:1, 59.15; linoleic-18:2; 11.5; linolenic-18:3, 1.1; linolenic-20:1, 0.4; arachidonic-20:4; 0.2)] for 3–4 weeks prior to experimental use.

Techniques: Expressing, Activity Assay, Injection, Plasmid Preparation, Virus, Muscles, Immunoprecipitation, Activation Assay, Western Blot

Effects of insulin on [3H]2-deoxyglucose uptake (A), and effects of insulin and/or PIP3 on aPKC activity (B) and phosphorylation of the activation loop site in aPKC (C) in vastus lateralis muscles of high-fat–fed (high fat) and chow-fed (low fat) mice. Mice were injected IP as described in Experimental Procedures (A). aPKCs were immunoprecipitated from muscles of mice treated IM with saline vehicle or insulin (1U/kg) in saline for 15 min, and then assayed in absence or presence of 10 μM PIP3 (B and C). It was necessary to first immunoprecipitate (IP) aPKC (because other 70–80 kDa PKCs have similar activation loop phosphorylation sites) before Western analyses for phospho-thr-411/410-PKC-λ/ζ; shown here is a blot representative of four determinations (C). Values in panels A and B are mean ± SE of (N) determinations. P values were determined by ANOVA.

Journal:

Article Title: The critical role of atypical protein kinase C in activating hepatic SREBP-1c and NF?B in obesity

doi: 10.1194/jlr.M800520-JLR200

Figure Lengend Snippet: Effects of insulin on [3H]2-deoxyglucose uptake (A), and effects of insulin and/or PIP3 on aPKC activity (B) and phosphorylation of the activation loop site in aPKC (C) in vastus lateralis muscles of high-fat–fed (high fat) and chow-fed (low fat) mice. Mice were injected IP as described in Experimental Procedures (A). aPKCs were immunoprecipitated from muscles of mice treated IM with saline vehicle or insulin (1U/kg) in saline for 15 min, and then assayed in absence or presence of 10 μM PIP3 (B and C). It was necessary to first immunoprecipitate (IP) aPKC (because other 70–80 kDa PKCs have similar activation loop phosphorylation sites) before Western analyses for phospho-thr-411/410-PKC-λ/ζ; shown here is a blot representative of four determinations (C). Values in panels A and B are mean ± SE of (N) determinations. P values were determined by ANOVA.

Article Snippet: Experimental mice In HFF studies, male C57Bl/6 mice, 8–12 weeks of age, were obtained from Harlan Industries, housed in a temperature-controlled environment with alternating 12-h light and dark cycles, and fed ad lib with either a standard low-fat laboratory chow diet [Harlan Teklad 20/18 with 5% fat (i.e., 10% of calories)] or a moderately high-fat Western-type diet [Harlan Teklad {"type":"entrez-nucleotide","attrs":{"text":"T01064","term_id":"277545","term_text":"T01064"}} T01064 with 20% by weight anhydrous milk fat and 1% corn oil (i.e., 42% of calories with fatty acid composition in g fatty acid-length:unsaturation/kg diet as follows: butyric-4:0, 7.6; caproic-6:0, 4.6; caprylic-8:0, 2.2; capric-10:0, 4; capric-11:0, 0.2; lauric-12:0, 6.2; myristic-14:0, 23.4; myristic-14:1, 1.6; myristic-15:0, 3.2; palmitic-16:0, 53.6; palmitoleic-16:1, 3.8; margaric-17:0, 1.4; margaric-17:1, 0.4; stearic-18:0, 25.2; oleic-18:1, 59.15; linoleic-18:2; 11.5; linolenic-18:3, 1.1; linolenic-20:1, 0.4; arachidonic-20:4; 0.2)] for 3–4 weeks prior to experimental use.

Techniques: Activity Assay, Phospho-proteomics, Activation Assay, Muscles, Injection, Immunoprecipitation, Saline, Western Blot

Effects of adenoviral-mediated expression of kinase-inactive PKC-ζ on hepatic IKKβ activity (A), hepatic nuclear levels of the p65RelA subunit of NFκB (B), and NFκB-dependent EMSA mobility shifts (B), in high-fat–fed (HFF) mice. As in Fig. 1, where indicated, HFF mice were injected IV with adenovirus vector (Vec) or adenovirus encoding KI-PKC-ζ (KI-ζ), and 5 days later (to allow time for expression), mice were either fasted overnight or fed, or fed and treated IM for 15 min with saline or insulin in saline. For comparisons in assays, chow-fed (low fat) mice were similarly examined. Values are mean ± SEM of (N) determinations and P values (as per ANOVA) depict comparisons of indicated groups. Representative immunoblot of nuclear levels of the p65/RelA subunit of NFκB, and a representative autoradiogram of NFκB-dependent EMSA mobility shifts (arrow indicates electrophoretic mobility of the NFκB-DNA complex as determined with the kit standard (B). F indicates the electrophoretic front, as well as relative changes in multiple samples in the indicated groups.

Journal:

Article Title: The critical role of atypical protein kinase C in activating hepatic SREBP-1c and NF?B in obesity

doi: 10.1194/jlr.M800520-JLR200

Figure Lengend Snippet: Effects of adenoviral-mediated expression of kinase-inactive PKC-ζ on hepatic IKKβ activity (A), hepatic nuclear levels of the p65RelA subunit of NFκB (B), and NFκB-dependent EMSA mobility shifts (B), in high-fat–fed (HFF) mice. As in Fig. 1, where indicated, HFF mice were injected IV with adenovirus vector (Vec) or adenovirus encoding KI-PKC-ζ (KI-ζ), and 5 days later (to allow time for expression), mice were either fasted overnight or fed, or fed and treated IM for 15 min with saline or insulin in saline. For comparisons in assays, chow-fed (low fat) mice were similarly examined. Values are mean ± SEM of (N) determinations and P values (as per ANOVA) depict comparisons of indicated groups. Representative immunoblot of nuclear levels of the p65/RelA subunit of NFκB, and a representative autoradiogram of NFκB-dependent EMSA mobility shifts (arrow indicates electrophoretic mobility of the NFκB-DNA complex as determined with the kit standard (B). F indicates the electrophoretic front, as well as relative changes in multiple samples in the indicated groups.

Article Snippet: Experimental mice In HFF studies, male C57Bl/6 mice, 8–12 weeks of age, were obtained from Harlan Industries, housed in a temperature-controlled environment with alternating 12-h light and dark cycles, and fed ad lib with either a standard low-fat laboratory chow diet [Harlan Teklad 20/18 with 5% fat (i.e., 10% of calories)] or a moderately high-fat Western-type diet [Harlan Teklad {"type":"entrez-nucleotide","attrs":{"text":"T01064","term_id":"277545","term_text":"T01064"}} T01064 with 20% by weight anhydrous milk fat and 1% corn oil (i.e., 42% of calories with fatty acid composition in g fatty acid-length:unsaturation/kg diet as follows: butyric-4:0, 7.6; caproic-6:0, 4.6; caprylic-8:0, 2.2; capric-10:0, 4; capric-11:0, 0.2; lauric-12:0, 6.2; myristic-14:0, 23.4; myristic-14:1, 1.6; myristic-15:0, 3.2; palmitic-16:0, 53.6; palmitoleic-16:1, 3.8; margaric-17:0, 1.4; margaric-17:1, 0.4; stearic-18:0, 25.2; oleic-18:1, 59.15; linoleic-18:2; 11.5; linolenic-18:3, 1.1; linolenic-20:1, 0.4; arachidonic-20:4; 0.2)] for 3–4 weeks prior to experimental use.

Techniques: Expressing, Activity Assay, Injection, Plasmid Preparation, Saline, Western Blot

Effects of administration of adenovirus encoding kinase-inactive PKC-ζ (KI-ζ) on fasting and fed levels of hepatic G6Pase mRNA and PEPCK mRNA in high-fat–fed mice (left) and heterozygous muscle-specific PKC-λ knockout (Mλ-Het-KO) mice (right). For comparisons in assays, samples from control mice on normal mouse chow (low fat) and wild-type (WT) littermates of Mλ-Het-KO mice were employed. Vec = adenovirus vector. Values are mean ± SEM of (N) determinations. Asterisks indicate P < 0.05 (*) and P < 0.01 (**) for feeding-stimulated values (shaded bars) versus adjacent fasting values (clear bars). P values depict comparisons of indicated groups. All P values were determined by ANOVA.

Journal:

Article Title: The critical role of atypical protein kinase C in activating hepatic SREBP-1c and NF?B in obesity

doi: 10.1194/jlr.M800520-JLR200

Figure Lengend Snippet: Effects of administration of adenovirus encoding kinase-inactive PKC-ζ (KI-ζ) on fasting and fed levels of hepatic G6Pase mRNA and PEPCK mRNA in high-fat–fed mice (left) and heterozygous muscle-specific PKC-λ knockout (Mλ-Het-KO) mice (right). For comparisons in assays, samples from control mice on normal mouse chow (low fat) and wild-type (WT) littermates of Mλ-Het-KO mice were employed. Vec = adenovirus vector. Values are mean ± SEM of (N) determinations. Asterisks indicate P < 0.05 (*) and P < 0.01 (**) for feeding-stimulated values (shaded bars) versus adjacent fasting values (clear bars). P values depict comparisons of indicated groups. All P values were determined by ANOVA.

Article Snippet: Experimental mice In HFF studies, male C57Bl/6 mice, 8–12 weeks of age, were obtained from Harlan Industries, housed in a temperature-controlled environment with alternating 12-h light and dark cycles, and fed ad lib with either a standard low-fat laboratory chow diet [Harlan Teklad 20/18 with 5% fat (i.e., 10% of calories)] or a moderately high-fat Western-type diet [Harlan Teklad {"type":"entrez-nucleotide","attrs":{"text":"T01064","term_id":"277545","term_text":"T01064"}} T01064 with 20% by weight anhydrous milk fat and 1% corn oil (i.e., 42% of calories with fatty acid composition in g fatty acid-length:unsaturation/kg diet as follows: butyric-4:0, 7.6; caproic-6:0, 4.6; caprylic-8:0, 2.2; capric-10:0, 4; capric-11:0, 0.2; lauric-12:0, 6.2; myristic-14:0, 23.4; myristic-14:1, 1.6; myristic-15:0, 3.2; palmitic-16:0, 53.6; palmitoleic-16:1, 3.8; margaric-17:0, 1.4; margaric-17:1, 0.4; stearic-18:0, 25.2; oleic-18:1, 59.15; linoleic-18:2; 11.5; linolenic-18:3, 1.1; linolenic-20:1, 0.4; arachidonic-20:4; 0.2)] for 3–4 weeks prior to experimental use.

Techniques: Knock-Out, Control, Plasmid Preparation

Effects of administration of adenovirus encoding kinase-inactive PKC-ζ (KI-ζ) on fasting serum levels of triglycerides, free fatty acids (FFA), total cholesterol, and glucose; and hepatic levels of triglycerides, ACC mRNA, IL-1β mRNA, and TNFα mRNA in high-fat–fed mice (A) and heterozygous muscle-specific PKC-λ knockout (Mλ-Het-KO) mice (B). WT = wild-type mice. Vec = adenovirus vector. Rel U = relative units. Values are mean ± SEM of (N) determinations and P values (as per ANOVA) depict comparisons of indicated groups.

Journal:

Article Title: The critical role of atypical protein kinase C in activating hepatic SREBP-1c and NF?B in obesity

doi: 10.1194/jlr.M800520-JLR200

Figure Lengend Snippet: Effects of administration of adenovirus encoding kinase-inactive PKC-ζ (KI-ζ) on fasting serum levels of triglycerides, free fatty acids (FFA), total cholesterol, and glucose; and hepatic levels of triglycerides, ACC mRNA, IL-1β mRNA, and TNFα mRNA in high-fat–fed mice (A) and heterozygous muscle-specific PKC-λ knockout (Mλ-Het-KO) mice (B). WT = wild-type mice. Vec = adenovirus vector. Rel U = relative units. Values are mean ± SEM of (N) determinations and P values (as per ANOVA) depict comparisons of indicated groups.

Article Snippet: Experimental mice In HFF studies, male C57Bl/6 mice, 8–12 weeks of age, were obtained from Harlan Industries, housed in a temperature-controlled environment with alternating 12-h light and dark cycles, and fed ad lib with either a standard low-fat laboratory chow diet [Harlan Teklad 20/18 with 5% fat (i.e., 10% of calories)] or a moderately high-fat Western-type diet [Harlan Teklad {"type":"entrez-nucleotide","attrs":{"text":"T01064","term_id":"277545","term_text":"T01064"}} T01064 with 20% by weight anhydrous milk fat and 1% corn oil (i.e., 42% of calories with fatty acid composition in g fatty acid-length:unsaturation/kg diet as follows: butyric-4:0, 7.6; caproic-6:0, 4.6; caprylic-8:0, 2.2; capric-10:0, 4; capric-11:0, 0.2; lauric-12:0, 6.2; myristic-14:0, 23.4; myristic-14:1, 1.6; myristic-15:0, 3.2; palmitic-16:0, 53.6; palmitoleic-16:1, 3.8; margaric-17:0, 1.4; margaric-17:1, 0.4; stearic-18:0, 25.2; oleic-18:1, 59.15; linoleic-18:2; 11.5; linolenic-18:3, 1.1; linolenic-20:1, 0.4; arachidonic-20:4; 0.2)] for 3–4 weeks prior to experimental use.

Techniques: Knock-Out, Plasmid Preparation