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Deer antler does not represent a typical endochondral growth system: immunoidentification of collagen type X but little collagen type II in growing antler tissue.
Rucklidge, G J; Milne, G; Bos, K J; Farquharson, C; Robins, S P.
Afiliação
  • Rucklidge GJ; Rowett Research Institute, Bucksburn, Aberdeen, U.K. gjr@rri.sari.ac.uk
Article em En | MEDLINE | ID: mdl-9440222
ABSTRACT
The collagen isotypes present at early (6 week) and late (5 month) stages of growing deer antler were isolated and identified. Pepsin-digested collagens were separated by differential salt fractionation, SDS-PAGE and Western blotting and subsequently identified by immunostaining. Cyanogen bromide digestion of antler tissue was used to establish a collagen type-specific pattern of peptides, and these were also identified by immunoblotting. Collagen type I was found to be the major collagen in both early- and late-stage antler. Collagen type II was present in the young antler in small amounts but was not confined to the soft "cartilaginous" tip of the antler. Collagen type XI was found in the pepsin digest of the young antler, but collagen type IX was not present at either stage of antler growth. Collagen type X was found in the young antler in all fractions studied. Microscopic study showed that the deer antler did not possess a discrete growth plate as found in endochondral bone growth. Unequivocal immunolocalization of the different collagen types in the antler were unsuccessful. These results show that, despite the presence in the antler of many cartilage collagens, growth does not occur through a simple endochondral process.
Assuntos
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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Chifres de Veado / Cervos / Colágeno Limite: Animals Idioma: En Revista: Comp Biochem Physiol B Biochem Mol Biol Assunto da revista: BIOLOGIA MOLECULAR / BIOQUIMICA Ano de publicação: 1997 Tipo de documento: Article País de afiliação: Reino Unido
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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Chifres de Veado / Cervos / Colágeno Limite: Animals Idioma: En Revista: Comp Biochem Physiol B Biochem Mol Biol Assunto da revista: BIOLOGIA MOLECULAR / BIOQUIMICA Ano de publicação: 1997 Tipo de documento: Article País de afiliação: Reino Unido