Age-related changes and location of types I, III, XII and XIV collagen during development of skeletal muscles from genetically different animals

• Published in: Journal of molecular histology Vol. 32; no. 6; pp. 349 - 356
• Main Authors: Listrat, A, Lethias, C, Hocquette, J F, Renand, G, Ménissier, F, Geay, Y, Picard, B
• Format: Journal Article
• Language: English
• Published: Netherlands Springer Nature B.V 01.06.2000
• Subjects: Age Factors; Animals; Cattle - genetics; Collagen; Collagen - analysis; Embryonic and Fetal Development; Hydroxyproline - metabolism; Immunohistochemistry - methods; Muscle Development; Muscle, Skeletal - chemistry; Muscle, Skeletal - embryology; Muscle, Skeletal - growth & development; Studies
• ISSN: 0018-2214; 1567-2379; 1567-2387; 1573-6865
• DOI: 10.1023/A:1004013613793

The ontogenesis of total collagen and of different collagen types was studied in four muscle types from genetically different cattle. Hydroxyproline content was 1.2-fold higher in muscles from cross-bred foetuses with normal muscle growth compared to those of the other genetic types (pure bred with different growth rates, double-muscled breed). A similar tendency was observed for type III collagen content. In all muscles of each animal studied, type XII and XIV collagens were colocated in perimysium. Immunolabelling obtained for type XII collagen was higher during foetal life than after birth, while for type XIV collagen, the opposite result was obtained. Whatever the muscle studied, but especially in semitendinosus muscle, during the foetal and the post-natal period until 15 months of age, immunolabelling with antibody anti-type XIV collagen tended to be more intense in muscles of animals from fathers selected for a low muscle growth capacity compared to those from fathers selected for a high muscle growth capacity. In conclusion, this study shows, that during foetal life, selection according to muscle growth capacity has no significant effect on the contents of total hydroxyproline or type III collagen, but minor effects on collagen localization.