Home LiteratureArticle Details
PMID: 3897279 Published · ppublish English Journal Article

Location of C-protein, H-protein and X-protein in rabbit skeletal muscle fibre types.

Journal of muscle research and cell motility ·Vol. 6 ·No. 2 ·1985-04-00 ·Pages 227-56

Starr R, Almond R, Offer G

Abstract

The locations of C-protein, H-protein and X-protein in rabbit psoas, plantaris and soleus muscles have been investigated with fluorescently tagged specific antibodies. Two systems have been examined: isolated myofibrils allowed the locations of these proteins within the sarcomere to be determined, while cryosections allowed a comparison of the amounts of these proteins between different types of fibre in the three muscles. Using antibody-labelled cryosections, we find that the amounts of each of these proteins depends closely on the fibre type. In all the muscles studied, C-protein is present in the largest amounts in fast white and fast intermediate fibres and is absent from slow red fibres, while X-protein is absent from fast white fibres and is present in the largest amounts in fast and slow red fibres. In psoas muscle, H-protein is present in the largest amounts in fast white fibres and is absent in fast and slow red fibres. In plantaris muscle, however, H-protein is absent from fast white fibres but occurs in some slow red fibres. All psoas myofibrils label with anti-C and anti-H and a minority label with anti-X. In each case the pattern of labelling is a zone in each half of the A-band. Measured across the middle of the A-band, the zones for H-protein are much closer together than for C-protein; the centre-to-centre spacings are 0.35 micron for anti-H and 0.64 micron for anti-C. The fluorescent zones for X-protein are slightly but significantly closer (0.52 micron) than those for C-protein. All soleus myofibrils label with anti-X but the centre-to-centre spacing was greater (0.67 micron). With plantaris myofibrils, where labelling occurs with anti-C or anti-H, the spacings resemble those in psoas myofibrils, but with anti-X the spacing resembles that in soleus myofibrils. The spacing of the fluorescent zones in an A-band, whether produced by anti-C, anti-X or anti-H does not vary with sarcomere length. We conclude that X-protein and H-protein, like C-protein, are thick filament components. With both fibres and myofibrils, there is no simple relationship between the amount of X-protein and the amount of C-protein. Many fast intermediate fibres in psoas and plantaris muscle label as strongly with anti-C as do fast white fibres but also label as strongly with anti-X as do fast and slow red fibres.(ABSTRACT TRUNCATED AT 400 WORDS)

MeSH Terms
Animals Carrier Proteins Female Fluorescent Antibody Technique Frozen Sections Histocytochemistry Muscle Proteins/analysis Muscles/analysis Myofibrils/analysis Rabbits Sarcomeres/analysis
Chemicals
Carrier Proteins H-Protein, Oryctolagus cuniculus Muscle Proteins X-Protein, muscle, Oryctolagus cuniculus myosin-binding protein C
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Starr R
Almond R
Offer G
References (28)
28 references, click to expand
  1. Structure of A-segments from frog and rabbit skeletal muscle.
    J Mol Biol. 1977 Jan 5;109(1):69-81 PMID: 300111
  2. C-protein from rabbit soleus (red) muscle.
    Biochem J. 1981 May 1;195(2):463-9 PMID: 6797400
  3. Procedure for the histochemical demonstration of actomyosin ATPase.
    Exp Neurol. 1970 Aug;28(2):365-7 PMID: 4248172
  4. Isoforms of C-protein in adult chicken skeletal muscle: detection with monoclonal antibodies.
    J Cell Biol. 1982 Oct;95(1):78-84 PMID: 6183271
  5. The myosin filament. III. C-protein.
    J Mol Biol. 1975 Dec 25;99(4):609-17 PMID: 814246
  6. Relationship among fibre type, myosin ATPase activity and contractile properties.
    Histochem J. 1982 Nov;14(6):981-97 PMID: 6217171
  7. Preparation of C-protein, H-protein, X-protein, and phosphofructokinase.
    Methods Enzymol. 1982;85 Pt B:130-8 PMID: 6214690
  8. Polymorphism of myofibrillar proteins of rabbit skeletal-muscle fibres. An electrophoretic study of single fibres.
    Biochem J. 1982 Nov 1;207(2):261-72 PMID: 6186242
  9. Molecular properties and functions in vitro of chicken smooth-muscle alpha-actinin in comparison with those of striated-muscle alpha-actinins.
    J Biochem. 1982 Nov;92 (5):1457-68 PMID: 6218160
  10. ATPase activity of myosin correlated with speed of muscle shortening.
    J Gen Physiol. 1967 Jul;50(6):Suppl:197-218 PMID: 4227924
  11. The size of the fibre populations in rabbit skeletal muscles as revealed by indirect immunofluorescence with anti-myosin sera.
    Histochemistry. 1978 Sep 15;57(3):223-35 PMID: 361653
  12. Improved histochemical method for the demonstration of the activity of alpha-glucan phosphorylase. I. The use of glucosyl acceptor dextran.
    Histochemie. 1968;12 (3):244-52 PMID: 5742691
  13. Activities of malate dehydrogenase, 3-hydroxyacyl-CoA dehydrogenase and fructose-1,6-diphosphatase with regard to metabolic subpopulations of fast- and slow-twitch fibres in rabbit muscles.
    Histochemistry. 1979 Feb 26;60(1):9-19 PMID: 218915
  14. Polypeptide chains of intermediate molecular weight in myosin preparations.
    FEBS Lett. 1971 Jun 2;15(1):40-44 PMID: 11945810
  15. The C-proteins of rabbit red, white, and cardiac muscles.
    J Biol Chem. 1983 Jul 10;258(13):8395-401 PMID: 6134729
  16. Distribution of polymorphic forms of troponin components and tropomyosin in skeletal muscle.
    Nature. 1979 Apr 19;278(5706):714-8 PMID: 372827
  17. Cytochemical demonstration of succinic dehydrogenase by the use of a new p-nitrophenyl substituted ditetrazole.
    J Histochem Cytochem. 1957 Jul;5(4):420-36 PMID: 13463314
  18. Characterization of the C-protein from posterior latissimus dorsi muscle of the adult chicken: heterogeneity within a single sarcomere.
    J Cell Biol. 1983 Jan;96(1):297-300 PMID: 6687470
  19. Activity patterns of phosphofructokinase, glyceraldehydephosphate dehydrogenase, lactate dehydrogenase and malate dehydrogenase in microdissected fast and slow fibres from rabbit psoas and soleus muscle.
    Histochemistry. 1977 Jun 8;52(3):201-16 PMID: 142072
  20. Polymorphism of myosin among skeletal muscle fiber types.
    J Cell Biol. 1977 Sep;74(3):760-79 PMID: 71302
  21. Analysis of myosin light and heavy chain types in single human skeletal muscle fibers.
    Eur J Biochem. 1981 May 15;116(2):389-95 PMID: 6454576
  22. Myosin isozymes in normal and cross-reinnervated cat skeletal muscle fibers.
    J Cell Biol. 1983 Sep;97(3):756-71 PMID: 6885917
  23. Distribution of myosin isoenzymes among skeletal muscle fiber types.
    J Cell Biol. 1979 Apr;81(1):10-25 PMID: 90047
  24. H-protein and X-protein. Two new components of the thick filaments of vertebrate skeletal muscle.
    J Mol Biol. 1983 Nov 5;170(3):675-98 PMID: 6415290
  25. A new protein of the thick filaments of vertebrate skeletal myofibrils. Extractions, purification and characterization.
    J Mol Biol. 1973 Mar 15;74(4):653-76 PMID: 4269687
  26. Objective characterization of cells in terms of microscopical parameters: an example from muscle histochemistry.
    Histochem J. 1981 Mar;13(2):269-317 PMID: 6166594
  27. Two kinds of slow skeletal muscle fibers which differ in their myosin light chain complements.
    FEBS Lett. 1980 Dec 15;122(1):80-2 PMID: 7215548
  28. The location of C-protein in rabbit skeletal muscle.
    Proc R Soc Lond B Biol Sci. 1976 Mar 16;192(1109):451-61 PMID: 4802
Article Info
Journal
Journal of muscle research and cell motility
Abbr.
J Muscle Res Cell Motil
ISSN
0142-4319
Published
1985-04-00
Pages
227-56
Language
English
Region
Netherlands
NLM ID
8006298
Subset
IM
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com