» Articles » PMID: 6183271

Isoforms of C-protein in Adult Chicken Skeletal Muscle: Detection with Monoclonal Antibodies

Overview
Journal J Cell Biol
Specialty Cell Biology
Date 1982 Oct 1
PMID 6183271
Citations 27
Authors
Affiliations
Soon will be listed here.
Abstract

Monoclonal antibodies (McAbs) specific for the C-proteins of chicken pectoralis major and anterior latissimus dorsi (ALD) muscles have been produced and characterized. Antibody specificity was demonstrated by solid phase radioimmunoassay (RIA), immunoblots, and immunofluorescence cytochemistry. Both McAbs MF-1 (or MF-21) and ALD-66 bound to myofibrillar proteins of approximately 150,000 daltons; the former antibody reacted with pectoralis but not ALD myofibrils, whereas the latter recognized ALD but not pectoralis myofibrils. Chromatographic elution of the antigens from DEAE-Sephadex, and their distribution in the A-band, support the conclusion that both of these antibodies recognize variant isoforms of C-protein. Since both McAbs react with a protein of similar molecular weight in the A-band of all myofibrils of the posterior latissimus dorsi (PLD) muscle, we suggest that either another isoform of C-protein exists in the PLD muscle or both pectoralis and ALD-like isoforms coexist in the A-bands of PLD muscle.

Citing Articles

Bringing into focus the central domains C3-C6 of myosin binding protein C.

Doh C, Schmidt A, Chinthalapudi K, Stelzer J Front Physiol. 2024; 15:1370539.

PMID: 38487262 PMC: 10937550. DOI: 10.3389/fphys.2024.1370539.


Etiology of genetic muscle disorders induced by mutations in fast and slow skeletal MyBP-C paralogs.

Song T, Landim-Vieira M, Ozdemir M, Gott C, Kanisicak O, Pinto J Exp Mol Med. 2023; 55(3):502-509.

PMID: 36854776 PMC: 10073172. DOI: 10.1038/s12276-023-00953-x.


Dysregulation of lipid metabolism and appearance of slow myofiber-specific isoforms accompany the development of Wooden Breast myopathy in modern broiler chickens.

Papah M, Abasht B Sci Rep. 2019; 9(1):17170.

PMID: 31748687 PMC: 6868161. DOI: 10.1038/s41598-019-53728-8.


Overview of the Muscle Cytoskeleton.

Henderson C, Gomez C, Novak S, Mi-Mi L, Gregorio C Compr Physiol. 2017; 7(3):891-944.

PMID: 28640448 PMC: 5890934. DOI: 10.1002/cphy.c160033.


Modulation of myosin filament organization by C-protein family members.

Seiler S, Fischman D, Leinwand L Mol Biol Cell. 1996; 7(1):113-27.

PMID: 8741844 PMC: 278617. DOI: 10.1091/mbc.7.1.113.


References
1.
Starr R, Offer G . The interaction of C-protein with heavy meromyosin and subfragment-2. Biochem J. 1978; 171(3):813-6. PMC: 1184031. DOI: 10.1042/bj1710813. View

2.
Callaway J, Bechtel P . C-protein from rabbit soleus (red) muscle. Biochem J. 1981; 195(2):463-9. PMC: 1162910. DOI: 10.1042/bj1950463. View

3.
Mikawa T, Takeda S, Shimizu T, Kitaura T . Gene expression of myofibrillar proteins in single muscle fibers of adult chicken: micro two dimensional gel electrophoretic analysis. J Biochem. 1981; 89(6):1951-62. DOI: 10.1093/oxfordjournals.jbchem.a133397. View

4.
Pepe F, Drucker B . The myosin filament. III. C-protein. J Mol Biol. 1975; 99(4):609-17. DOI: 10.1016/s0022-2836(75)80175-6. View

5.
Jeacocke S, England P . Phosphorylation of a myofibrillar protein of Mr 150 000 in perfused rat heart, and the tentative indentification of this as C-protein. FEBS Lett. 1980; 122(1):129-32. DOI: 10.1016/0014-5793(80)80418-2. View