The ultrastructural location of C-protein, X-protein and H-protein in rabbit muscle
- 1 December 1986
- journal article
- conference paper
- Published by Springer Nature in Journal of Muscle Research and Cell Motility
- Vol. 7 (6) , 550-567
- https://doi.org/10.1007/bf01753571
Abstract
Purified antibodies to the thick filament accessory proteins, C-protein, X-protein and H-protein, have been used to label fibres of three rabbit muscles, psoas (containing mainly fast white fibres), soleus (containing mainly slow red fibres) and plantaris (a muscle of mixed fibre type) and their location has been examined by electron microscopy. These accessory proteins are present on one or more of a set of eleven transverse stripes about 43 nm apart that have been observed previously in each half A-band. Each protein has a limited set of characteristic distributions. H-protein is present on stripe 3 (counting from the M-line) in the majority of psoas fibres but is absent in soleus and plantaris muscle. C-protein can occur (1) on stripes 4–11 (the commonest pattern seen in psoas); (2) on stripes 5–11 (in psoas and plantaris); (3) on stripe 3 together with stripes 5–11 (in plantaris); or (4) on none (in red fibres of all three muscles). X-protein can occur (1) on stripes 3–11 in the red fibres of all three muscles; (2) on stripe 4 only (in psoas and plantaris); (3) on stripes 3 and 4 (in psoas and plantaris) or (4) on none. Stripes labelled with anti-X are wider than those labelled with anti-C and consist of a doublet with an internal spacing of 16 nm. The patterns for the three accessory proteins, while overlapping, are in no case identical; this suggests the proteins do not simply substitute for one another. The precise axial positions of the anti-C labelled stripes differ from those of the anti-X stripes; the anti-X stripes lie about 8–9 nm further from the M-line than the corresponding anti-C stripes. This implies that the inner member of an X-protein doublet lies in a very similar position to a C-protein stripe. The anti-H labelled stripe seen in most psoas fibres lies 14 nm nearer the M-line than stripe 3 of the anti-X labelled array in psoas red fibres and is staggered from a continuation of the C-protein array by about 4 nm. The labelling patterns were constant within a fibre and suggest a very precise assembly mechanism. The number of classes of fibre, as defined by the accessory proteins present and their arrangement, exceeds the number of fibre types presently recognized.Keywords
This publication has 31 references indexed in Scilit:
- Novel thick filament protein of chicken pectoralis muscle: the 86 kd proteinJournal of Molecular Biology, 1985
- Novel thick filament protein of chicken pectoralis muscle: the 86 kd proteinJournal of Molecular Biology, 1985
- H-protein and X-proteinJournal of Molecular Biology, 1983
- Structure of A-segments from frog and rabbit skeletal muscleJournal of Molecular Biology, 1977
- Axial arrangement of crossbridges in thick filaments of vertebrate skeletal muscleJournal of Molecular Biology, 1976
- Discrimination between fiber populations in mammalian skeletal muscle by using ultrastructural parametersJournal of Ultrastructure Research, 1976
- A new protein of the thick filaments of vertebrate skeletal myofibrilsJournal of Molecular Biology, 1973
- Polypeptide chains of intermediate molecular weight in myosin preparationsFEBS Letters, 1971
- Structure of the myosin-containing filament assembly (A-segment) separated from frog skeletal muscleJournal of Molecular Biology, 1971
- On the relationship of ultrastructural and cytochemical features to color in mammalian skeletal muscleCell and tissue research, 1969