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. 2020 Dec 17;12(12):3810. doi: 10.3390/cancers12123810

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© 2020 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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The effect of irinotecan (IRI) and IRI with BGP-15 (IRI+BGP) treatments on molecular markers of sarcolemmal integrity and extracellular matrix (ECM) remodeling. Western blotting experiments were undertaken in tibialis anterior (TA) muscle, with samples probed for (A) Laminin, (B) Dystrophin, (C) β-dystroglycan (β-DGC), (D) α-sarcoglycan (α-SGC), (E) δ-sarcoglycan (δ-SGC), (F) Desmin, (G) Rac1 and matrix metalloproteinase (MMP) isoforms (H) MMP-9 and (I) MMP-2. Gelatin zymography experiments were conducted using extensor digitorum longus (EDL) muscle homogenate (same anterior hindlimb muscle compartment as the TA) to assess the activity of (J) MMP-9 and (K) MMP-2. (L) The ratio of MMP-9 to MMP-2 was utilized to indicate the shift of gelatinolytic MMP activity. Western blotting data are expressed as a relative percentage of the vehicle (VEH) control group and (M) representative images are displayed alongside the Coomassie Blue representative image, which was used as the protein loading control. (N) Representative image of zymography data is displayed. * = p < 0.05 compared to VEH; ^ = p < 0.05 compared to IRI; n = 5–8.

The effect of irinotecan (IRI) and IRI with BGP-15 (IRI+BGP) treatments on molecular markers of sarcolemmal integrity and extracellular matrix (ECM) remodeling. Western blotting experiments were undertaken in tibialis anterior (TA) muscle, with samples probed for (A) Laminin, (B) Dystrophin, (C) β-dystroglycan (β-DGC), (D) α-sarcoglycan (α-SGC), (E) δ-sarcoglycan (δ-SGC), (F) Desmin, (G) Rac1 and matrix metalloproteinase (MMP) isoforms (H) MMP-9 and (I) MMP-2. Gelatin zymography experiments were conducted using extensor digitorum longus (EDL) muscle homogenate (same anterior hindlimb muscle compartment as the TA) to assess the activity of (J) MMP-9 and (K) MMP-2. (L) The ratio of MMP-9 to MMP-2 was utilized to indicate the shift of gelatinolytic MMP activity. Western blotting data are expressed as a relative percentage of the vehicle (VEH) control group and (M) representative images are displayed alongside the Coomassie Blue representative image, which was used as the protein loading control. (N) Representative image of zymography data is displayed. * = p < 0.05 compared to VEH; ^ = p < 0.05 compared to IRI; n = 5–8.