Expression of atrial myosin light chains but not α-myosin heavy chains is correlated in vivo with increased ventricular function in patients with hypertrophic obstructive cardiomyopathy

We present evidence that M proteins from three different serotypes of group A streptococci share epitopes with cardiac myosin. Rabbit antisera evoked by a purified fragment of type 5 M protein crossreacted with myosin, but not alpha-tropomyosin, actin, or myosin light chains. In enzyme-linked immunosorbent assays, the myosin-crossreactive antibodies were totally inhibited by type 5 M protein and partially inhibited by types 6 and 19 M proteins. The affinity-purified myosin antibodies opsonized type 5 streptococci, indicating that they were directed against protective M protein epitopes on the surface of the organisms. Immunoblot analyses demonstrated the binding of the crossreactive antibodies to myosin heavy chains. Sera from patients with acute rheumatic fever showed significantly stronger reactions with myosin than did sera from their siblings, hospitalized controls, or patients with poststreptococcal glomerulonephritis.

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Intracompartmental sorting of essential myosin light chains: Molecular dissection and in vivo monitoring by epitope tagging

Cell ◽

10.1016/0092-8674(91)90618-9 ◽

1991 ◽

Vol 66 (2) ◽

pp. 277-289 ◽

Cited By ~ 44

Author(s):

Thierry Soldati ◽

Jean-Claude Perriard

Keyword(s):

Light Chains ◽

Myosin Light Chains ◽

Molecular Dissection ◽

Epitope Tagging ◽

In Vivo Monitoring

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Current understanding of conventional and novel co-expression patterns of mammalian sarcomeric myosin heavy chains and light chains

Archives of Biochemistry and Biophysics ◽

10.1016/j.abb.2018.12.009 ◽

2019 ◽

Vol 662 ◽

pp. 129-133 ◽

Cited By ~ 8

Author(s):

Peter J. Reiser

Keyword(s):

Expression Patterns ◽

Current Understanding ◽

Light Chains ◽

Myosin Heavy Chains ◽

Heavy Chains

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Relative synthesis of cardiac contractile proteins. Evidence for synthesis from the same precursor pool

Biochemical Journal ◽

10.1042/bj1940673 ◽

1981 ◽

Vol 194 (3) ◽

pp. 673-678 ◽

Cited By ~ 11

Author(s):

C D Evans ◽

S S Schreiber ◽

M Oratz ◽

M A Rothschild

Keyword(s):

Light Chain ◽

Contractile Proteins ◽

Light Chains ◽

Myosin Heavy Chains ◽

Perfused Heart ◽

Precursor Pool ◽

Heavy Chains ◽

Cardiac Contractile ◽

Specific Activities ◽

Cardiac Contractile Proteins

The relative molar synthesis of cardiac contractile proteins has been measured in the perfused heart under control haemodynamic conditions. This synthesis, of myosin heavy chains, individual light chains (1 and 2), actin and tropomyosin, was determined from isolated guinea-pig hearts perfused for 3h simultaneously with constant specific radioactivities and concentrations of [3H]lysine and [3H]phenylalanine.The data strongly suggest that all of the proteins studied were synthesized from the same precursor pools of lysine and phenylalanine, since the ratio of the specific activities of the two labels was the same in all of the proteins. Measurement of molar synthesis of each contractile protein was the same with either labelled amino acid. Under control haemodynamic-perfusion conditions, the relative molar synthesis of the contractile proteins was actin greater than heavy chains greater than light chain 2 greater than light chain 1 greater than tropomyosin.

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