Publications by authors named "Rosetta Rossi"

Duchenne muscular dystrophy (DMD) is a genetic disease characterized by skeletal muscle wasting and atrophy. Recent evidence suggests that the impaired skeletal muscle performance in DMD is not solely dependent on a loss of contractile muscle mass. In this study the myosin motor function of mdx and control (wildtype, WT) mice was compared using pure myosin isoforms in an "in vitro motility assay" (IVMA).

View Article and Find Full Text PDF

A balanced redox status is necessary to optimize force production in contractile apparatus, where free radicals generated by skeletal muscle are involved in some basic physiological processes like excitation-contraction coupling. Protein glutathionylation has a key role in redox regulation of proteins and signal transduction. Here we show that myosin is sensitive to in vitro glutathionylation and MALDI-TOF analysis identified three potential sites of glutathione binding, two of them locating on the myosin head.

View Article and Find Full Text PDF

This study was aimed to achieve a definitive and unambiguous identification of fiber types in canine skeletal muscles and of myosin isoforms that are expressed therein. Correspondence of canine myosin isoforms with orthologs in other species as assessed by base sequence comparison was the basis for primer preparation and for expression analysis with RT-PCR. Expression was confirmed at protein level with histochemistry, immunohistochemistry, and SDS-PAGE combined together and showed that limb and trunk muscles of the dog express myosin heavy chain (MHC) type 1, 2A, and 2X isoforms and the so-called "type 2dog" fibers express the MHC-2X isoform.

View Article and Find Full Text PDF

In rat skeletal muscle the unloaded shortening velocity (Vo) is defined by the myosin isoform expressed in the muscle fibre. In 2001 we suggested that ADP release from actomyosin in solution (controlled by k(-AD)) was of the right size to limit Vo. However, to compare mechanical and solution kinetic data required a series of corrections to compensate for the differences in experimental conditions (0.

View Article and Find Full Text PDF
Article Synopsis
  • The study explores how different Myosin Heavy Chain (MHC) isoforms affect the muscle fiber properties in pigs, specifically looking at samples from various muscles, including the masseter and diaphragm.
  • Researchers used techniques like RT-PCR and gel electrophoresis to isolate and identify four MHC isoforms: slow, 2A, 2X, and 2B, and measured their contractile properties.
  • Findings revealed significant differences in maximum shortening velocity (V(o)) and isometric tension (P(o)) across muscle fiber types, with fast fibers showing higher V(o) than anticipated based on body size, highlighting the dominance of fast MHC isoforms in pig muscles.
View Article and Find Full Text PDF

Biopsy samples were taken from vastus lateralis muscle of seven young (YO, age 30.2 +/- 2.2 years), and seven elderly (EL, age 72.

View Article and Find Full Text PDF