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Diabetes induces differences in the F‐actin spatial organization of striated muscles
Author(s) -
Romanelli Gerardo,
Varela Rocío,
Benech Juan C.
Publication year - 2020
Publication title -
cytoskeleton
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.95
H-Index - 86
eISSN - 1949-3592
pISSN - 1949-3584
DOI - 10.1002/cm.21600
Subject(s) - phalloidin , actin , biology , skeletal muscle , sarcomere , actinin , actin cytoskeleton , filamin , microbiology and biotechnology , myofilament , anatomy , myocyte , cytoskeleton , medicine , cell , biochemistry
Abstract Studies have shown the cytoskeleton disorganization produced by diabetes and quantified F‐actin fluorescence in the striated muscles of diabetic animals. However, at present, there are no studies that have quantified F‐actin spatial organization (F‐actin‐SO). Through our research, we analyzed the effect of diabetes on F‐actin‐SO in the cardiac and skeletal muscles of a mouse model. The muscle samples were labeled with phalloidin–rhodamine and analyzed with confocal microscopy. The analysis was done in two dimensions using four approaches: quantitation of (a) phalloidin‐occupied areas; (b) number of F‐actin‐unoccupied areas per muscular fiber; (c) F‐actin filament discontinuity; and (d) costamere periodicity. Our results showed that both the cardiac and skeletal muscles of the control mice had more phalloidin‐occupied areas than the diabetic mice. The skeletal muscles had a significantly higher number of F‐actin‐unoccupied areas per muscular fiber and more F‐actin discontinuities. Additionally, using western blot analyses, we showed that those differences were not due to α‐actin protein expression. Finally, we considered the importance of these findings in dysfunctional contraction, disassembly in cell–cell communication, conduction of muscle impulse, and changes in cell nanomechanics. Our results quantitatively demonstrated that diabetes severely affects F‐actin‐SO in striated muscles.