Isoforms of heavy and light chains of cardiac myosins from rat and rabbit

Srihari, Thota; Tuchschmid, C. R.; Schaub, Marcus C.

doi:10.1007/bf01908313

Cited by 22 publications

(12 citation statements)

References 25 publications

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“…For example, differences in myosin light chain were observed between fetal and adult rat ventricular tissue, suggesting differences in developmental growth [25]. Studies in genetically derived cardiomyopathy, muscular sub- functional and metabolic abnormalities in heart muscle disorders.…”

Section: Application Of 2-de To Other Heart Pathologiesmentioning

confidence: 96%

Protein profiling in cardiac tissue in response to the chronic effects of alcohol

et al. 1997

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An investigation was made into cardiac protein levels after chronic ethanol consumption to examine whether specific proteins are affected by alcohol. Ethanol was administered for six weeks to male Wistar rats which were fed a nutritionally complete liquid diet containing 35% of total calories as ethanol. Controls were pair-fed identical amounts of the same diet in which ethanol was replaced by isocaloric glucose; thus both groups had identical nutritional intakes, albeit differences in ethanol or carbohydrate. After six weeks' feeding, cardiac tissue was removed and analyzed by two-dimensional electrophoresis, where equal amounts of proteins were studied. Protein patterns were analyzed by computerized densitometry and characterized by comparison with a database of known cardiac proteins. Chronic alcohol feeding caused significant decreases in the relative amounts of various proteins, including several tentatively identified as heat shock protein (HSP) 60, HSP70, and desmin. The relative proportions of actin, vimentin, myosin light chain 1, myosin light chain 2, and albumin, remained unchanged. Examination of antibodies raised against HSP65 showed no overt differences in plasma levels following chronic alcohol consumption, and liver changes as assessed by histology were mild. In conclusion, chronic alcohol appears to have selective effects on particular proteins, and the effects were not directly ascribed to overt liver dysfunction or malnutrition. This may explain some of the functional and morphological characteristics observed in alcohol-induced heart muscle disease, including reduced contractility.

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Section: Application Of 2-de To Other Heart Pathologiesmentioning

confidence: 96%

Protein profiling in cardiac tissue in response to the chronic effects of alcohol

et al. 1997

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“…(Price et al, 1980;Srihari et al, 1982), which are evident in the gels shown in Figure 6 as a band running with a mobility just ahead of light chain 1 (LCI). There are also four unidentified, low-molecular-weight bands below TnC, which are prominent in the myofibrils from perinatal dog hearts.…”

Section: Figure 5 Comparison Of Ventricular Myosin Isoenzymes From Amentioning

confidence: 99%

Differential effects of pH on calcium activation of myofilaments of adult and perinatal dog hearts. Evidence for developmental differences in thin filament regulation.

Solaro¹,

Kumar

Blanchard

et al. 1986

Circulation Research

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Our results show that calcium activation of myofilament preparations of dog heart in the perinatal period is unaffected by a reduction in pH from 7.0 to 6.5, which, in adult heart myofilaments, induces a 0.4 pCa unit (-log molar free calcium concentration) rightward shift in the relation between pCa and myofibrillar adenosine triphosphatase activity. Acidic pH also had no effect on calcium binding to myofibrillar troponin C of perinatal hearts. The stoichiometry of troponin C bound calcium at full myofilament activation (about 3 mol calcium/mol troponin C) was the same for adult and perinatal heart myofibrils, as was their myofibrillar troponin C content. Moreover, there were no differences in isoelectric pH of troponin C from adult and perinatal hearts. We tested whether variants of myofilament proteins other than troponin C could account for the differential effects of acidic pH. In adult and perinatal dog heart preparations, myosin heavy chain isoenzymes appeared the same as measured, using native pyrophosphate gel electrophoresis. No evidence for thick filament-related calcium regulation in the perinatal heart myofilaments was obtained, when tested in studies in which native thin filaments were displaced with a 10-fold molar excess of pure actin. In preparations in which native thick filaments were displaced with a 10-fold molar excess of pure skeletal muscle myosin, the effects of acidic pH on calcium activation were the same as in native adult and perinatal preparations. Our major conclusion from these results is that the perinatal heart myofilaments are likely to possess variations in thin filament activity and structure. Although not conclusive, preliminary investigations of this question by means of polyacrylamide gel electrophoresis of the adult and perinatal myofilaments in the presence of sodium dodecyl sulfate or urea at basic pH and acidic pH provide evidence that there may be variants of troponin I in the thin filaments of the perinatal hearts. It is also possible that variants of troponin T or unidentified low molecular weight polypeptides associated with the thin filaments may also be important in the relative insensitivity of calcium activation of perinatal heart myofilaments to acidic pH. (Circ Res 58: 721-729, 1986)

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“…Most atrial myosin differs from ventricular myosin in both heavy and light chain composition (4,8,13,15,(19)(20)(21)25). The Ca2+-activated ATPase activity of atrial myosin exceeds that of ventricular myosin (8,13,21,26).…”

Section: Introductionmentioning

confidence: 96%

Myosin light chain compositions of the interatrial and interventricular septa of sheep heart

1985

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The myosin light chain composition of sheep interatrial and interventricular septa were analysed by one- and two-dimensional polyacrylamide gel. The interventricular septum has myosin light chain composition indistinguishable from that of ventricular myosin. Myosin from the interatrial septum contains three light chains, two of which co-migrated with the two atrial light chains (ALC1 and ALC2), while the third co-migrated with ventricular light chain 2 (VLC2). ALC1 are more abundant than ALC2 or VLC2 suggesting a mixed myosin population. Myosin with ALC1 and VLC2 light chain composition may be present, and its possible relationship with cardiac "conducting" cells is discussed.

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Isoforms of heavy and light chains of cardiac myosins from rat and rabbit

Cited by 22 publications

References 25 publications

Protein profiling in cardiac tissue in response to the chronic effects of alcohol

Protein profiling in cardiac tissue in response to the chronic effects of alcohol

Differential effects of pH on calcium activation of myofilaments of adult and perinatal dog hearts. Evidence for developmental differences in thin filament regulation.

Myosin light chain compositions of the interatrial and interventricular septa of sheep heart

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