Literature DB >> 3897279

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

R Starr, R Almond, G Offer.   

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)

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Year:  1985        PMID: 3897279     DOI: 10.1007/bf00713063

Source DB:  PubMed          Journal:  J Muscle Res Cell Motil        ISSN: 0142-4319            Impact factor:   2.698


  28 in total

1.  Structure of A-segments from frog and rabbit skeletal muscle.

Authors:  R Craig
Journal:  J Mol Biol       Date:  1977-01-05       Impact factor: 5.469

2.  Procedure for the histochemical demonstration of actomyosin ATPase.

Authors:  L Guth; F J Samaha
Journal:  Exp Neurol       Date:  1970-08       Impact factor: 5.330

3.  The myosin filament. III. C-protein.

Authors:  F A Pepe; B Drucker
Journal:  J Mol Biol       Date:  1975-12-25       Impact factor: 5.469

4.  Preparation of C-protein, H-protein, X-protein, and phosphofructokinase.

Authors:  R Starr; G Offer
Journal:  Methods Enzymol       Date:  1982       Impact factor: 1.600

5.  Relationship among fibre type, myosin ATPase activity and contractile properties.

Authors:  L C Maxwell; J A Faulkner; R A Murphy
Journal:  Histochem J       Date:  1982-11

6.  C-protein from rabbit soleus (red) muscle.

Authors:  J E Callaway; P J Bechtel
Journal:  Biochem J       Date:  1981-05-01       Impact factor: 3.857

7.  Polymorphism of myofibrillar proteins of rabbit skeletal-muscle fibres. An electrophoretic study of single fibres.

Authors:  G Salviati; R Betto; D Danieli Betto
Journal:  Biochem J       Date:  1982-11-01       Impact factor: 3.857

8.  Molecular properties and functions in vitro of chicken smooth-muscle alpha-actinin in comparison with those of striated-muscle alpha-actinins.

Authors:  T Endo; T Masaki
Journal:  J Biochem       Date:  1982-11       Impact factor: 3.387

9.  Isoforms of C-protein in adult chicken skeletal muscle: detection with monoclonal antibodies.

Authors:  F C Reinach; T Masaki; S Shafiq; T Obinata; D A Fischman
Journal:  J Cell Biol       Date:  1982-10       Impact factor: 10.539

10.  ATPase activity of myosin correlated with speed of muscle shortening.

Authors:  M Bárány
Journal:  J Gen Physiol       Date:  1967-07       Impact factor: 4.086

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  13 in total

1.  Modification of myofibrils by fluorophore-induced photo-oxidation.

Authors:  P Knight; N Parsons
Journal:  J Muscle Res Cell Motil       Date:  1991-04       Impact factor: 2.698

2.  The extent of amino-terminal heterogeneity in rabbit fast skeletal muscle troponin T.

Authors:  M M Briggs; J J Lin; F H Schachat
Journal:  J Muscle Res Cell Motil       Date:  1987-02       Impact factor: 2.698

3.  Identification and distribution of the fast class of troponin T in the adult and developing avian skeletal muscle.

Authors:  G K Dhoot
Journal:  J Muscle Res Cell Motil       Date:  1988-10       Impact factor: 2.698

4.  The immunohistochemical location of cathepsin L in rabbit skeletal muscle. Evidence for a fibre type dependent distribution.

Authors:  M A Taylor; R E Almond; D J Etherington
Journal:  Histochemistry       Date:  1987

5.  Characterization and fibre type distribution of a new myofibrillar protein of molecular weight 32 kDa.

Authors:  W Y Chen; G K Dhoot; S V Perry
Journal:  J Muscle Res Cell Motil       Date:  1986-12       Impact factor: 2.698

6.  The ultrastructural location of C-protein, X-protein and H-protein in rabbit muscle.

Authors:  P Bennett; R Craig; R Starr; G Offer
Journal:  J Muscle Res Cell Motil       Date:  1986-12       Impact factor: 2.698

7.  The chicken muscle thick filament: temperature and the relaxed cross-bridge arrangement.

Authors:  R W Kensler; J L Woodhead
Journal:  J Muscle Res Cell Motil       Date:  1995-02       Impact factor: 2.698

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

Authors:  S H Seiler; D A Fischman; L A Leinwand
Journal:  Mol Biol Cell       Date:  1996-01       Impact factor: 4.138

9.  Different domains of the M-band protein myomesin are involved in myosin binding and M-band targeting.

Authors:  D Auerbach; S Bantle; S Keller; V Hinderling; M Leu; E Ehler; J C Perriard
Journal:  Mol Biol Cell       Date:  1999-05       Impact factor: 4.138

10.  Patterns of troponin T expression in mammalian fast, slow and promiscuous muscle fibres.

Authors:  G E Moore; M M Briggs; F H Schachat
Journal:  J Muscle Res Cell Motil       Date:  1987-02       Impact factor: 2.698

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