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srebf1 −/− ZF alters the organization of slow muscle fibers (A) CRISPR-Cas9-induced srebf1 knockout in whole-cell lysate fraction of ZF larvae at 7 days post fertilization (dpf) was confirmed by western blot analysis. (B) Quantification of relative expression units showed that levels of the mature form of Srebp1 protein were significantly reduced in srebf1 −/− ZF compared to srebf1 +/+ siblings (∗∗ p < 0.002). Whole-cell lysate was extracted with n = 10 animals per genotype, and reduced expression of Srebp1 was determined in two pools. (C) Whole-mount immunostaining of slow muscle myosin in 5 dpf ZF larvae was performed using F59 antibody <t>(anti-MyHC).</t> The slow muscle fibers of srebf1 −/− larvae were found to be disorganized and gaps between fibers alignments indicated by orange arrow heads (bottom) as compared to srebf1 +/+ siblings (top). (D) Shorter somites with non-significant alteration of pennation angle (not shown) were found in srebf1 knockout with respect to fish with no genetic perturbation (∗∗ p < 0.001). (E) Using DanioVision apparatus, locomotion tracking (15 min light on, 5 min light off/dark, 15 min light on) of both srebf1 +/+ and srebf1 −/− larvae ( n = 46 per group) was determined at 7 dpf. Knockout larvae traveled faster in dark conditions compared to srebf1 +/+ . One-way ANOVA. This figure complementary of summarizes the gene expression of slow muscle genes, such as sm y hc1 and sm y hc 2 is unaltered while upregulation of the slow muscle-associated metabolic gene tnnt1 ( p = 0.0056) was found in KO larvae; moreover, expression of muscle progenitors i.e., pax3a/b significantly ( p = 4.57–06 and p = 0.001, respectively) was increased in mining of RNA-seq data in srebf1 KO larvae. Each dot represents the total distance traveled by the larva or the number of quantifications. Magnification: 5×, Mann-Whitney statistical test, ∗∗ p = 0.0036. Data are presented as mean ± standard deviation (SD).
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srebf1 −/− ZF alters the organization of slow muscle fibers (A) CRISPR-Cas9-induced srebf1 knockout in whole-cell lysate fraction of ZF larvae at 7 days post fertilization (dpf) was confirmed by western blot analysis. (B) Quantification of relative expression units showed that levels of the mature form of Srebp1 protein were significantly reduced in srebf1 −/− ZF compared to srebf1 +/+ siblings (∗∗ p < 0.002). Whole-cell lysate was extracted with n = 10 animals per genotype, and reduced expression of Srebp1 was determined in two pools. (C) Whole-mount immunostaining of slow muscle myosin in 5 dpf ZF larvae was performed using F59 antibody <t>(anti-MyHC).</t> The slow muscle fibers of srebf1 −/− larvae were found to be disorganized and gaps between fibers alignments indicated by orange arrow heads (bottom) as compared to srebf1 +/+ siblings (top). (D) Shorter somites with non-significant alteration of pennation angle (not shown) were found in srebf1 knockout with respect to fish with no genetic perturbation (∗∗ p < 0.001). (E) Using DanioVision apparatus, locomotion tracking (15 min light on, 5 min light off/dark, 15 min light on) of both srebf1 +/+ and srebf1 −/− larvae ( n = 46 per group) was determined at 7 dpf. Knockout larvae traveled faster in dark conditions compared to srebf1 +/+ . One-way ANOVA. This figure complementary of summarizes the gene expression of slow muscle genes, such as sm y hc1 and sm y hc 2 is unaltered while upregulation of the slow muscle-associated metabolic gene tnnt1 ( p = 0.0056) was found in KO larvae; moreover, expression of muscle progenitors i.e., pax3a/b significantly ( p = 4.57–06 and p = 0.001, respectively) was increased in mining of RNA-seq data in srebf1 KO larvae. Each dot represents the total distance traveled by the larva or the number of quantifications. Magnification: 5×, Mann-Whitney statistical test, ∗∗ p = 0.0036. Data are presented as mean ± standard deviation (SD).
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srebf1 −/− ZF alters the organization of slow muscle fibers (A) CRISPR-Cas9-induced srebf1 knockout in whole-cell lysate fraction of ZF larvae at 7 days post fertilization (dpf) was confirmed by western blot analysis. (B) Quantification of relative expression units showed that levels of the mature form of Srebp1 protein were significantly reduced in srebf1 −/− ZF compared to srebf1 +/+ siblings (∗∗ p < 0.002). Whole-cell lysate was extracted with n = 10 animals per genotype, and reduced expression of Srebp1 was determined in two pools. (C) Whole-mount immunostaining of slow muscle myosin in 5 dpf ZF larvae was performed using F59 antibody <t>(anti-MyHC).</t> The slow muscle fibers of srebf1 −/− larvae were found to be disorganized and gaps between fibers alignments indicated by orange arrow heads (bottom) as compared to srebf1 +/+ siblings (top). (D) Shorter somites with non-significant alteration of pennation angle (not shown) were found in srebf1 knockout with respect to fish with no genetic perturbation (∗∗ p < 0.001). (E) Using DanioVision apparatus, locomotion tracking (15 min light on, 5 min light off/dark, 15 min light on) of both srebf1 +/+ and srebf1 −/− larvae ( n = 46 per group) was determined at 7 dpf. Knockout larvae traveled faster in dark conditions compared to srebf1 +/+ . One-way ANOVA. This figure complementary of summarizes the gene expression of slow muscle genes, such as sm y hc1 and sm y hc 2 is unaltered while upregulation of the slow muscle-associated metabolic gene tnnt1 ( p = 0.0056) was found in KO larvae; moreover, expression of muscle progenitors i.e., pax3a/b significantly ( p = 4.57–06 and p = 0.001, respectively) was increased in mining of RNA-seq data in srebf1 KO larvae. Each dot represents the total distance traveled by the larva or the number of quantifications. Magnification: 5×, Mann-Whitney statistical test, ∗∗ p = 0.0036. Data are presented as mean ± standard deviation (SD).
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srebf1 −/− ZF alters the organization of slow muscle fibers (A) CRISPR-Cas9-induced srebf1 knockout in whole-cell lysate fraction of ZF larvae at 7 days post fertilization (dpf) was confirmed by western blot analysis. (B) Quantification of relative expression units showed that levels of the mature form of Srebp1 protein were significantly reduced in srebf1 −/− ZF compared to srebf1 +/+ siblings (∗∗ p < 0.002). Whole-cell lysate was extracted with n = 10 animals per genotype, and reduced expression of Srebp1 was determined in two pools. (C) Whole-mount immunostaining of slow muscle myosin in 5 dpf ZF larvae was performed using F59 antibody <t>(anti-MyHC).</t> The slow muscle fibers of srebf1 −/− larvae were found to be disorganized and gaps between fibers alignments indicated by orange arrow heads (bottom) as compared to srebf1 +/+ siblings (top). (D) Shorter somites with non-significant alteration of pennation angle (not shown) were found in srebf1 knockout with respect to fish with no genetic perturbation (∗∗ p < 0.001). (E) Using DanioVision apparatus, locomotion tracking (15 min light on, 5 min light off/dark, 15 min light on) of both srebf1 +/+ and srebf1 −/− larvae ( n = 46 per group) was determined at 7 dpf. Knockout larvae traveled faster in dark conditions compared to srebf1 +/+ . One-way ANOVA. This figure complementary of summarizes the gene expression of slow muscle genes, such as sm y hc1 and sm y hc 2 is unaltered while upregulation of the slow muscle-associated metabolic gene tnnt1 ( p = 0.0056) was found in KO larvae; moreover, expression of muscle progenitors i.e., pax3a/b significantly ( p = 4.57–06 and p = 0.001, respectively) was increased in mining of RNA-seq data in srebf1 KO larvae. Each dot represents the total distance traveled by the larva or the number of quantifications. Magnification: 5×, Mann-Whitney statistical test, ∗∗ p = 0.0036. Data are presented as mean ± standard deviation (SD).
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srebf1 −/− ZF alters the organization of slow muscle fibers (A) CRISPR-Cas9-induced srebf1 knockout in whole-cell lysate fraction of ZF larvae at 7 days post fertilization (dpf) was confirmed by western blot analysis. (B) Quantification of relative expression units showed that levels of the mature form of Srebp1 protein were significantly reduced in srebf1 −/− ZF compared to srebf1 +/+ siblings (∗∗ p < 0.002). Whole-cell lysate was extracted with n = 10 animals per genotype, and reduced expression of Srebp1 was determined in two pools. (C) Whole-mount immunostaining of slow muscle myosin in 5 dpf ZF larvae was performed using F59 antibody <t>(anti-MyHC).</t> The slow muscle fibers of srebf1 −/− larvae were found to be disorganized and gaps between fibers alignments indicated by orange arrow heads (bottom) as compared to srebf1 +/+ siblings (top). (D) Shorter somites with non-significant alteration of pennation angle (not shown) were found in srebf1 knockout with respect to fish with no genetic perturbation (∗∗ p < 0.001). (E) Using DanioVision apparatus, locomotion tracking (15 min light on, 5 min light off/dark, 15 min light on) of both srebf1 +/+ and srebf1 −/− larvae ( n = 46 per group) was determined at 7 dpf. Knockout larvae traveled faster in dark conditions compared to srebf1 +/+ . One-way ANOVA. This figure complementary of summarizes the gene expression of slow muscle genes, such as sm y hc1 and sm y hc 2 is unaltered while upregulation of the slow muscle-associated metabolic gene tnnt1 ( p = 0.0056) was found in KO larvae; moreover, expression of muscle progenitors i.e., pax3a/b significantly ( p = 4.57–06 and p = 0.001, respectively) was increased in mining of RNA-seq data in srebf1 KO larvae. Each dot represents the total distance traveled by the larva or the number of quantifications. Magnification: 5×, Mann-Whitney statistical test, ∗∗ p = 0.0036. Data are presented as mean ± standard deviation (SD).
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srebf1 −/− ZF alters the organization of slow muscle fibers (A) CRISPR-Cas9-induced srebf1 knockout in whole-cell lysate fraction of ZF larvae at 7 days post fertilization (dpf) was confirmed by western blot analysis. (B) Quantification of relative expression units showed that levels of the mature form of Srebp1 protein were significantly reduced in srebf1 −/− ZF compared to srebf1 +/+ siblings (∗∗ p < 0.002). Whole-cell lysate was extracted with n = 10 animals per genotype, and reduced expression of Srebp1 was determined in two pools. (C) Whole-mount immunostaining of slow muscle myosin in 5 dpf ZF larvae was performed using F59 antibody <t>(anti-MyHC).</t> The slow muscle fibers of srebf1 −/− larvae were found to be disorganized and gaps between fibers alignments indicated by orange arrow heads (bottom) as compared to srebf1 +/+ siblings (top). (D) Shorter somites with non-significant alteration of pennation angle (not shown) were found in srebf1 knockout with respect to fish with no genetic perturbation (∗∗ p < 0.001). (E) Using DanioVision apparatus, locomotion tracking (15 min light on, 5 min light off/dark, 15 min light on) of both srebf1 +/+ and srebf1 −/− larvae ( n = 46 per group) was determined at 7 dpf. Knockout larvae traveled faster in dark conditions compared to srebf1 +/+ . One-way ANOVA. This figure complementary of summarizes the gene expression of slow muscle genes, such as sm y hc1 and sm y hc 2 is unaltered while upregulation of the slow muscle-associated metabolic gene tnnt1 ( p = 0.0056) was found in KO larvae; moreover, expression of muscle progenitors i.e., pax3a/b significantly ( p = 4.57–06 and p = 0.001, respectively) was increased in mining of RNA-seq data in srebf1 KO larvae. Each dot represents the total distance traveled by the larva or the number of quantifications. Magnification: 5×, Mann-Whitney statistical test, ∗∗ p = 0.0036. Data are presented as mean ± standard deviation (SD).
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srebf1 −/− ZF alters the organization of slow muscle fibers (A) CRISPR-Cas9-induced srebf1 knockout in whole-cell lysate fraction of ZF larvae at 7 days post fertilization (dpf) was confirmed by western blot analysis. (B) Quantification of relative expression units showed that levels of the mature form of Srebp1 protein were significantly reduced in srebf1 −/− ZF compared to srebf1 +/+ siblings (∗∗ p < 0.002). Whole-cell lysate was extracted with n = 10 animals per genotype, and reduced expression of Srebp1 was determined in two pools. (C) Whole-mount immunostaining of slow muscle myosin in 5 dpf ZF larvae was performed using F59 antibody (anti-MyHC). The slow muscle fibers of srebf1 −/− larvae were found to be disorganized and gaps between fibers alignments indicated by orange arrow heads (bottom) as compared to srebf1 +/+ siblings (top). (D) Shorter somites with non-significant alteration of pennation angle (not shown) were found in srebf1 knockout with respect to fish with no genetic perturbation (∗∗ p < 0.001). (E) Using DanioVision apparatus, locomotion tracking (15 min light on, 5 min light off/dark, 15 min light on) of both srebf1 +/+ and srebf1 −/− larvae ( n = 46 per group) was determined at 7 dpf. Knockout larvae traveled faster in dark conditions compared to srebf1 +/+ . One-way ANOVA. This figure complementary of summarizes the gene expression of slow muscle genes, such as sm y hc1 and sm y hc 2 is unaltered while upregulation of the slow muscle-associated metabolic gene tnnt1 ( p = 0.0056) was found in KO larvae; moreover, expression of muscle progenitors i.e., pax3a/b significantly ( p = 4.57–06 and p = 0.001, respectively) was increased in mining of RNA-seq data in srebf1 KO larvae. Each dot represents the total distance traveled by the larva or the number of quantifications. Magnification: 5×, Mann-Whitney statistical test, ∗∗ p = 0.0036. Data are presented as mean ± standard deviation (SD).

Journal: iScience

Article Title: Loss of SREBF1 disrupts lipid signaling and causes slow muscle fiber degeneration

doi: 10.1016/j.isci.2026.117447

Figure Lengend Snippet: srebf1 −/− ZF alters the organization of slow muscle fibers (A) CRISPR-Cas9-induced srebf1 knockout in whole-cell lysate fraction of ZF larvae at 7 days post fertilization (dpf) was confirmed by western blot analysis. (B) Quantification of relative expression units showed that levels of the mature form of Srebp1 protein were significantly reduced in srebf1 −/− ZF compared to srebf1 +/+ siblings (∗∗ p < 0.002). Whole-cell lysate was extracted with n = 10 animals per genotype, and reduced expression of Srebp1 was determined in two pools. (C) Whole-mount immunostaining of slow muscle myosin in 5 dpf ZF larvae was performed using F59 antibody (anti-MyHC). The slow muscle fibers of srebf1 −/− larvae were found to be disorganized and gaps between fibers alignments indicated by orange arrow heads (bottom) as compared to srebf1 +/+ siblings (top). (D) Shorter somites with non-significant alteration of pennation angle (not shown) were found in srebf1 knockout with respect to fish with no genetic perturbation (∗∗ p < 0.001). (E) Using DanioVision apparatus, locomotion tracking (15 min light on, 5 min light off/dark, 15 min light on) of both srebf1 +/+ and srebf1 −/− larvae ( n = 46 per group) was determined at 7 dpf. Knockout larvae traveled faster in dark conditions compared to srebf1 +/+ . One-way ANOVA. This figure complementary of summarizes the gene expression of slow muscle genes, such as sm y hc1 and sm y hc 2 is unaltered while upregulation of the slow muscle-associated metabolic gene tnnt1 ( p = 0.0056) was found in KO larvae; moreover, expression of muscle progenitors i.e., pax3a/b significantly ( p = 4.57–06 and p = 0.001, respectively) was increased in mining of RNA-seq data in srebf1 KO larvae. Each dot represents the total distance traveled by the larva or the number of quantifications. Magnification: 5×, Mann-Whitney statistical test, ∗∗ p = 0.0036. Data are presented as mean ± standard deviation (SD).

Article Snippet: anti-Myhc , Santa Cruz Biotechnology , Cat#sc-32732.

Techniques: CRISPR, Knock-Out, Western Blot, Analysis, Expressing, Immunostaining, Gene Expression, RNA Sequencing, MANN-WHITNEY, Standard Deviation

Journal: iScience

Article Title: Loss of SREBF1 disrupts lipid signaling and causes slow muscle fiber degeneration

doi: 10.1016/j.isci.2026.117447

Figure Lengend Snippet:

Article Snippet: anti-Myhc , Santa Cruz Biotechnology , Cat#sc-32732.

Techniques: Cell-Signaling, Radio Immunoprecipitation, Lysis, Protease Inhibitor, Tissue, Microscopy, Knock-Out, Gene Knockout, Software, Micro-CT, Analysis