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Of a total of three Friesian cows, two of which had been treated with adrenalin before slaughter, Mm longissimus (LO), supraspinatus (SS), triceps brachii (TB) and rectus abdominis (RA) were sampled at different times post mortem (pm). pH, calpain/calpastatin activities and degradation of myofibrillar proteins, as evidenced by SDS-PAGE, were assessed. Contraction characteristics were measured by determining myofibrillar ATPase activities. Adrenalin treatment resulted in a high ultimate pH (6.48 +/- 0.40) and a faster decline pm of calpain I activity. The effect was similar in all four investigated muscles (72.4 +/- 5.4% decline at 24 h pm). The decline in calpain I activity in the control muscles was muscle-dependent and ranged from 22.8-74.3% at 24 h pm. Differences in ultimate pH did not lead to distinct rates of breakdown of proteins with molecular weights lower than that of myosin heavy chain. Calpastatin levels were muscle-dependent and correlated with myofibrillar ATPase activity (r = -0.99). In a second experiment Mm rectus abdominis (RA) and psoas major (PM) of adrenalin-treated (n = 6) and control (n = 6) Friesian-Holstein calves were sampled at 1 and 29 h pm for assessment of calpain activities. At seven days pm the M longissimus (LO) was sampled for tenderness evaluation. pH values were measured at 30 min, 4 h and 29 h pm. Adrenalin treatment resulted in a higher ultimate pH in the three muscles. Higher ultimate pH resulted in lower calpain activities in the RA at 29 h pm (P less than or equal to 0.025).(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:The role of ultimate pH in proteolysis and calpain/calpastatin activity in bovine muscle. 153 28

Three mouse IgG1 monoclonal antibodies (MAbs), named FA1, FA2, and FA3, against cardiac myosin heavy chain (MHC) with high specificity have been obtained. The immunogen used to generate these MAbs was the high-salt- and detergent-insoluble fraction of adult rat myocardial tissue. Western blots showed that these MAbs reacted with a 200 kD protein band, which comigrated with the heavy chain of purified rat cardiac myosin in SDS-PAGE. Immunofluorescence microscopy revealed that the antigen recognized by these MAbs was localized at the A-band of isolated myofibrils. The tissue-, species-, and isoform-specificities of these MAbs were examined by Western blots on various muscle samples. FA2 recognized fish, frog, chicken, rabbit, bovine, mouse and rat cardiac MHC, as well as rabbit skeletal and rat aorta smooth muscle MHC. This antibody reacted equally well with both alpha- and beta-isoforms of MHC. FA1 did not crossreact with any MHC tested so far but with rat cardiac MHC. It appeared to react only with alpha-isoform of MHC. FA3 recognized only rat, bovine and rabbit cardiac MHC with the specificity to bovine and rabbit atrial MHC. Elisa competition assay revealed that different epitopes on the antigen molecules were recognized by these three MAbs, although there was a partial overlap between the epitopes for FA1 and FA2. These anti-MHC MAbs will be most useful in investigating the expression of MHC during myocardial development.
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PMID:Monoclonal antibodies against cardiac myosin heavy chain. 170 14

1. Actomyosin extracts of trunk, heart, and head muscles from barbel (Barbus barbus L.) were analyzed by SDS-polyacrylamide gel electrophoresis to study their myosin heavy chain composition. 2. Four heavy chain isoforms were found: trunk white, trunk red, and ventricle muscles yielded one heavy chain typical of the muscle type; head muscles devoid of red fibers displayed two heavy chain isoforms, the slow migrating one corresponding to the trunk white muscle type. 3. The electrophoretic mobility of red and ventricle myosin heavy chains related to that of white isoforms appeared highly modified by the glycerol content of the gels.
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PMID:Myosin heavy chain isoforms in white, red and ventricle muscles of barbel (Barbus barbus L.). 179 73

Using isoform specific antibodies we have verified the presence of two distinct muscle type myosin heavy chain isoforms in rat uterine muscle. We have shown that an endogenous protease can cleave a small 4 kDa region from the C-terminal of the SM1 isoform which generates a pSM1 species which comigrates with the SM2 isoform on low density SDS gels. While this cleavage can complicate isoform identification, more importantly, this cleavage was associated with a substantial increase in the actomyosin ATPase. Thus we have identified a domain at the C-terminal which may be involved in regulation of the ATPase activity. Interestingly, it is at this C-terminal, tail region of the smooth muscle myosin molecule where the only known isoform specific sequence differences are located. In skinned smooth muscle fibers of rat uterine muscle, we have also shown that differences in myosin heavy chain distribution, induced by beta-estradiol treatment of ovariectomized rats, are correlated with changes in unloaded shortening velocity. Thus our work suggests that the functional significance of myosin heavy chain isoforms in smooth muscle may be similar to that observed in striated muscle.
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PMID:Myosin heavy chain isoforms and smooth muscle function. 180 96

The expression of myosin isoforms and their subunit composition in the white skeletal body musculature of Arctic charr (Salvelinus alpinus) of different ages (from 77-day embryos until about 5 years old) was studied at the protein level by means of electrophoretic techniques. Myosin from the white muscle displayed three types of light chain during all the developmental stages examined: two myosin light chains type 1 (LC1F) differing in both apparent molecular mass and pI, one myosin light chain type 2 (LC2F) and one myosin light chain type 3 (LC3F). The fastest-migrating form of LC1F seemed to be predominant during the embryonic and eleutheroembryonic periods. The slowest-migrating form of LC1F was predominant in the 5-year-old fish. Between 1 year and 4 years, both types of LC1F were present in similar amounts. Cardiac as well as red muscle myosin from 3-year-old fish had two types of light chain. The myosin light chains from atria and ventriculi were indistinguishable by two-dimensional electrophoresis, but were different from the myosin light chains from red muscle. Neither the light chains from cardiac nor red muscle were coexpressed with the myosin light chains of white muscle at any of the developmental stages examined. Two myosin heavy chain bands were resolved by SDS/glycerol/polyacrylamide gel electrophoresis of the extract from embryos. One of the bands was present in minor amounts. The other, and most abundant, band comigrated with the only band found in the extracts of white muscle myosin from older fish. One-dimensional Staphylococcus aureus V8 protease peptide mapping of these bands revealed some differences during development of the white muscle tentatively interpreted as follows. The myosin heavy chain band present in minor amounts in the embryos may represent an early embryonic form that is replaced by a late embryonic or foetal form in the eleutheroembryos. The foetal myosin heavy chain appears to be present until the resorption of the yolk sack and beginning of the free-swimming stage. A new form of myosin heavy chain, termed neonatal and probably expressed around hatching, is present until about 1 year of age.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Comparison of myosin isoenzymes present in skeletal and cardiac muscles of the Arctic charr Salvelinus alpinus (L.). Sequential expression of different myosin heavy chains during development of the fast white skeletal muscle. 182 32

Immunohistochemical analysis of myosin heavy chain (MHC) isoform expression in perinatal and adult rat diaphragm muscles was performed with antibodies which permitted the identification of all known MHC isoforms found in typical rat muscles. Isoform switching, leading to the emergence of the adult phenotype, was more complex than had been previously described. As many as four isoforms could be coexpressed in a single myofiber. Elimination of developmental isoforms did not usually result in the myofiber immediately achieving its adult phenotype. Activation of genes for specific adult isoforms might be delayed to puberty. For example, two of the three fast MHCs, MHC2X and MHC2A appeared perinatally, while MHC2B did not appear until 30 days postnatal. By Day 60 this isoform was present in approximately 27% of the myofibers, but in most myofibers expression of this isoform was transient (i.e., at Day greater than or equal to 115, less than 4% of the myofibers expressed MHC2B). Fibers which contained MHC beta/slow during the late fetal and early neonatal period coexpressed MHCemb. A marked increase in the frequency of fibers containing MHC beta/slow occurred between 4 and 21 days postnatal. These slow fibers arose from a population of myofibers which expressed MHCemb and MHCneo during their development, and they accounted for the majority of slow fibers found in the adult diaphragm. The adult myosin phenotype of the diaphragm myofibers (as determined with immunocytochemistry, and 5% SDS-PAGE) was not achieved until the rat was greater than or equal to 115 days old.
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PMID:Emergence of the mature myosin phenotype in the rat diaphragm muscle. 199 90

Two different mRNAs encoding two different nonmuscle myosin heavy chains (MHCs) of approximately 200 kD have been identified in chicken nonmuscle cells, in agreement with the results of Katsuragawa et al. (Katsuragawa, Y., M. Yanagisawa, A. Inoue, and T. Masaki. 1989. Eur. J. Biochem. 184:611-616). In this paper, we quantitate the content of mRNA encoding the two MHCs in a number of different tissues using RNA blot analysis with two specific oligonucleotide probes. Our results show that the relative content of mRNA encoding MHC-A and MHC-B differs in a tissue-dependent manner. Thus the ratio of mRNA encoding MHC-A versus MHC-B varies from greater than 9:1 in spleen and intestinal epithelial cells, to 6:4 in kidney and 2:8 in brain. The effect of serum on MHC mRNA expression was studied in serum-starved cultures of chick embryo fibroblasts. Serum stimulation results in a threefold increase in the mRNA encoding MHC-A and a threefold decrease in mRNA encoding MHC-B. Using SDS polyacrylamide gels, we have separated two nonmuscle MHC isoforms (198 and 196 kD) that can be distinguished from each other by two-dimensional peptide mapping of chymotryptic digests. We provide preliminary evidence that the MHC-A mRNA encodes the 196-kD polypeptide and that the MHC-B mRNA encodes the 198-kD polypeptide.
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PMID:Chicken nonmuscle myosin heavy chains: differential expression of two mRNAs and evidence for two different polypeptides. 199 62

Previous studies demonstrated two myosin heavy chain isoforms in vascular smooth muscles with SDS-polyacrylamide gel electrophoresis; MHC1 (204 kDa) and MHC2 (200 kDa). We report the existence of a novel myosin heavy chain isoform, MHC3 (196 kDa), which was exclusively contained in inferior vena cava. Equal amount of MHC1 and MHC2 was observed in aorta and pulmonary artery, respectively. However, inferior vena cava contained only MHC3. Proteolytic artifact was refuted by immunoblotting of tissue homogenates without purification, or SDS-polyacrylamide gel electrophoresis of myosin bands isolated by pyrophosphate gel electrophoresis. Furthermore, alpha-chymotryptic cleavage of MHC1, MHC2, and MHC3 displayed different peptide maps, indicating the primary structural difference among all three isoforms.
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PMID:A novel myosin heavy chain isoform in vascular smooth muscle. 203 19

Actomyosin was prepared from human myocardium and its protein composition was examined by SDS-polyacrylamide gel electrophoresis. For some preparations, particularly actomyosin isolated from elderly subjects, a high molecular weight (HMW) band (identified as a breakdown product of myosin heavy chain) appeared, while the troponin-T subunit decreased. Myofibril associated protease (MFP) activity showed no significant difference as a function of proteolysis. In agreement with the proteolysis of troponin-T and myosin, the Ca2+ sensitivity of Mg2(+)-ATPase activity decreased while the extent of the stimulation of Ca2(+)-ATPase by N-ethylmaleimide remained unchanged. This type of proteolysis would affect the Ca2(+)-dependent regulation of muscle contraction but not the contractility per se.
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PMID:Proteolysis of myosin and troponin in human myocardium of elderly subjects. 227 58

Mammalian muscle undergoes significant alterations morphologically, ultrastructurally, and biochemically following infection by Trichinella spiralis larvae. To investigate this host/parasite relationship in more detail, a new method to isolate T. spiralis-infected cells (nurse cells) in preparative quantities was developed. Nurse cells isolated by sequential protease treatments contain larvae and retain many of the characteristics of those in situ. When analyzed by SDS-PAGE, a wide range of proteins detected in nurse cells were not apparent in muscle by the methods employed. Proteins associated with the nurse cell capsule and organellar fractions appear to account for most of the dominant nurse cell proteins. In contrast, most major muscle proteins were either reduced in abundance or undetectable in nurse cells. The myofibrillar proteins myosin heavy chain, alpha-actin, and alpha- and beta-tropomyosin were identified using antibody reagents and two-dimensional PAGE analysis. None of these proteins were detectable in nurse cells and except for beta-tropomyosin, the relative abundance of these proteins was a minimum 100-fold lower compared to muscle. The data indicate that the reduction of muscle products in the nurse cell is much greater than previously reported. The inability to detect myofibrillar proteins raises the possibility that the nurse cell is not blocked in a regenerating muscle phenotype as previously suggested. Availability of isolated nurse cells in large quantity should facilitate resolution of this and other issues regarding the T. spiralis/skeletal muscle relationship.
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PMID:Trichinella spiralis: altered expression of muscle proteins in trichinosis. 232 97


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