Human muscle proteins

Abstract

Proteins from single frozen sections of human muscle were separated by two-dimensional gel electrophoresis and detected by fluorography or Coomassie Blue staining. The major proteins were identical in different normal muscles obtained from either sex at different ages, and in Duchenne and myotonic dystrophy samples. Congenital myopathy, denervation atrophy, polymyositis, and Becker's muscular dystrophy samples, however, showed abnormal myosin light chain compositions, some with a decrease of fast-fiber myosin light chains and others with a decrease of slow-fiber light chains. These protein alterations did not correlate with any specific disease, and may be caused by generalized muscle-fiber damage.

Post mortem muscle protein degradation during ice‐storage of Arctic (Pandalus borealis) and tropical (Penaeus japonicus and Penaeus monodon) shrimps: a comparative electrophoretic and immunological study

“…As to the identity of the other three spots of molecular mass of about 50 kDa (Fig 6), the smallest and most alkaline might be desmin, by comparison with published 2D patterns of muscle extracts of human, 41 mouse 42 and Atlantic salmon (Salmo salar). 44 If this identi®cation is correct, then desmin would not be severely affected by post mortem deterioration during ice-storage in any of the three shrimp species, as seems to be the case in ®sh but not in bovine muscles.…”

“…13,14 The 67 kDa band also seemed to be subject to proteolysis during ice-storage of P borealis but not of P japonicus or P monodon. In the absence, to our knowledge, of published works on 2D patterns of crustacean muscles, we have tried to identify this band by comparison with our own analysis of minke whale muscles (unpublished), rat diaphragm, soleus and gastrocnemius (Fig 6) and red and white muscles of lean and fatty ®sh species, 39 and with published 2D patterns of muscle extracts from chicken, 40 human deltoid muscle 41 and mouse gastrocnemius. 42 Only in the 2D analysis of Arctic charr embryos (Salvelinus alpinus) was a spot with similar molecular mass and pI noticed.…”

Gene expression patterns in the black blowfly (Phormia regina) as revealed by two-dimensional electrophoresis of proteins. I. Developmental stage-specific and sex-specific differences

“…Such differences are known to occur during the transitions from egg to larva and pupa to adult; yet without additional analyses, such as Western blotting with specific antisera, we cannot distinctly assign enzymatic peptides. Identification of major proteins such as actin, tubulin, and the tropomyosins is presumptively based on positional location relative to known mobilities of these proteins in humans and other species (Giometti et al, 1983;Giometti and Anderson, 1984). i.e., saline-insoluble, proteins, and brackets show sex-specific protein differences that occur near the end of the CK charge scale.…”

Comparative Skeletal Muscle Proteomics Using Two-Dimensional Gel Electrophoresis

“…However, following the publication of high-resolution 2D-IEF/SDS-PAGE methods [9,10,11,12], this new and more refined approach was quickly adapted in the field of basic and applied myology [24]. Initial studies included the analysis of major structural and regulatory proteins of muscle fibers [33,34], the evaluation of human muscle biopsy specimens [35,36] and the identification of contractile protein isoforms in single skeletal muscle fibers [37,38]. In the pre-proteomic era of 2D-GE biochemistry [39], the technique was extensively applied to the detailed analysis of subunit structures and isoform expression patterns of major skeletal muscle proteins and their changes during development, fiber adaptations, contractile fatigue and denervation, as reviewed by Bárány et al [40].…”