Foetal myosin light chain in human ventricle

Cummins, Peter L.; Price, Karen M.; Littler, W. A.

doi:10.1007/bf00711936

Cited by 66 publications

(26 citation statements)

References 22 publications

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“…The perinatal period in rat, rabbit, and other species is one of very rapid alterations in cardiac myosin heavy chain isoenzyme composition (17) (18,30), that the fetal light chain is not a proteolytic product of the myosin heavy chain. Our study shows that the fetal light chain appears to be relatively resistant to proteolysis, since it appears to persist following 10 min of digestion with chymotrypsin ( Fig.…”

Section: Discussionmentioning

confidence: 99%

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Structural and Enzymatic Comparison of Human Cardiac Muscle Myosins Isolated from Infants, Adults, and Patients with Hypertrophic Cardiomyopathy

Schier¹,

Adelstein²

1982

J. Clin. Invest.

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A B S T R A C T Human cardiac ventricular myosins were prepared from autopsy samples from nine adults, seven infants, and from surgical specimens from seven patients undergoing left ventricular septal myectomy for obstructive hypertrophic cardiomyopathy. Infant myosin differed from adult myosin in two important characteristics: (a) t-30% of the 27,000-dalton myosin light chain is replaced by a 28,000-dalton light chain, and (b) the actin-activated myosin MgATPase activity of infant myosin is significantly lower than that of adult myosin (64 nmol phosphate released/mg myosin per min vs. 124 nmol/mg per min at 37°C). The K+-EDTA ATPase activity of the myosin measured in 0.5M KC1 is also lower in infants (1,210 nmol/mg per min vs. 620 nmol/mg per min at 37°C), but the Ca++-activated ATPase is not significantly different. There were no differences in enzymatic activity between the normal adult and cardiomyopathic myosins.A detailed study was performed to investigate possible variations in the structure of the myosin heavy chain in infant, adult, and cardiomyopathic samples. There were no significant differences between infant and normal adult, or between normal adult and cardiomyopathic myosins seen in pyrophosphate polyacrylamide gel electrophoresis, or peptide mapping using alpha-chymotrypsin, papain, or cyanogen bromide to generate peptides.These results suggest that isoenzymes of human ventricular myosin do not exist for the myosin heavy chain in the specimens examined from infants, adults, and patients with obstructive hypertrophic cardiomyopaDr. Schier's present address is

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Section: Discussionmentioning

confidence: 99%

“…In addition to isoenzymes of the myosin heavy chain, the existence of a unique human fetal cardiac muscle myosin light chain isoenzyme has recently been demonstrated by Cummins (18). This light chain of myosin (Mr, 28,000) is detectable in decreasing amounts from birth to 8 mo of age.…”

Section: Introductionmentioning

confidence: 99%

Structural and Enzymatic Comparison of Human Cardiac Muscle Myosins Isolated from Infants, Adults, and Patients with Hypertrophic Cardiomyopathy

Schier¹,

Adelstein²

1982

J. Clin. Invest.

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“…The long ELC isoforms are also expressed in slow skeletal muscle and in myocardium ( (Fig. 2B) (15,54). ELC a is found in both the atria and ventricles during embryonic development (6,42,74) and in fetal skeletal muscle (Table 1) (42).…”

Section: Elc Isoformsmentioning

confidence: 99%

Myosin essential light chain in health and disease

Hernandez¹,

Jones²,

Guzman³

et al. 2007

American Journal of Physiology-Heart and Circulatory Physiology

115

113

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The essential light chain of myosin (ELC) is known to be important for structural stability of the ␣-helical lever arm domain of the myosin head, but its function in striated muscle contraction is poorly understood. Two ELC isoforms are expressed in fast skeletal muscle, a long isoform and its NH 2-terminal ϳ40 amino acid shorter counterpart, whereas only the long ELC is observed in the heart. Biochemical and structural studies revealed that the NH 2-terminus of the long ELC can make direct contacts with actin, but the effects of the ELC on the affinity of myosin for actin, ATPase, force, and the kinetics of force generating myosin cross-bridges are inconclusive. Myosin containing the long ELC has been shown to have slower cross-bridge kinetics than myosin with the short isoform. A difference was also reported among myosins with long isoforms. Increased shortening velocity was observed in atrial compared with ventricular muscle fibers. The common findings suggest that ELC provides the fine tuning of the myosin motor function, which is regulated in an isoform and tissue-dependent manner. The functional importance of the ELC is further implicated by the discovery of ELC mutations associated with Familial Hypertrophic Cardiomyopathy. The pathological phenotypes vary in severity, but more notably, almost all ELC mutations result in sudden cardiac death at a young age. This review summarizes the functional roles of striated muscle ELC in normal healthy muscle and in disease. Transgenic animal models and phenotypic characterization of ELC-mediated remodeling of the heart are also discussed.cross-bridge kinetics; striated muscle contraction; familial hypertrophic cardiomyopathy; sarcomeric mutations; failing heart; sudden cardiac death STRIATED MUSCLE MYOSIN

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“…A common feature seen during early development in both cardiac and skeletal muscles is the expression of foetal or embryonic light chain isotypes [5,8]. In the mammalian foetal ventricle, a foetal light chain (FLC-1) is present which disappears during the early neonatal period to be replaced quantitatively by the adult ventricular light chain (VLC-1) [4].…”

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Isolation of cardiac myosin light‐chain isotypes by chromatofocusing

Vincent

Cummins

1985

European Journal of Biochemistry

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1. Cardiac myosin light chain isotypes have been resolved using chromatofocusing, a new preparative column chromatographic technique. The method relies on production of narrow-range, shallow and stable pH gradients using ion-exchange resins and buffers with even buffering capacity over the required pH range.2. Light chains were resolved in order of decreasing isoelectric point in the pH range 5.2-4.5. Gradients of ApH = 0.004 -0.006/ml elution volume were achieved which were capable of resolving light chains with isoelectric point differences of only 0.03.3. Analytical isoelectric focusing of light chains in polyacrylamide gels could be used to predict the results of preparative chromatofocusing for method development.4. Chromatofocusing was capable of resolving human and bovine cardiac light chain 1 and 2 subunits, atrial (ALC) and ventricular (VLC) light chain isotypes and homologous VLC-2 and VLC-2* light chains. .The technique was used to purify and resolve the human foetal ventricular light chain 1 (FLC-1) from adult ventricular light chain 1 (VLC-1) present in foetal ventricles and the atrial light chain 1 (ALC-1) in adult atria.6. Comparative peptide mapping studies and amino acid analyses were carried out on FLC-1 and ALC-1. No differences were detected between FLC-1 and ALC-1 using three different proteases and amino acid compositions were similar with the exception of glycine content. The studies indicate that FLC-1 and ALC-1 are homologous, and possibly identical, light chains.

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Foetal myosin light chain in human ventricle

Cited by 66 publications

References 22 publications

Structural and Enzymatic Comparison of Human Cardiac Muscle Myosins Isolated from Infants, Adults, and Patients with Hypertrophic Cardiomyopathy

Structural and Enzymatic Comparison of Human Cardiac Muscle Myosins Isolated from Infants, Adults, and Patients with Hypertrophic Cardiomyopathy

Myosin essential light chain in health and disease

Isolation of cardiac myosin light‐chain isotypes by chromatofocusing

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