Fine structure and histochemistry of the tail fin ray in teleosts
Identifieur interne : 000A05 ( Main/Exploration ); précédent : 000A04; suivant : 000A06Fine structure and histochemistry of the tail fin ray in teleosts
Auteurs : S. Montes [Brésil] ; J. Becerra [Espagne] ; S. Toledo [Brésil] ; A. Gordilho [Brésil] ; U. Junqueira [Brésil]Source :
- Histochemistry [ 0301-5564 ] ; 1982-09-01.
Abstract
Summary: Ultrastructural and histochemical studies performed on the skeletal elements of the tail fins of six representative species of teleosts enabled the following observations to be made. The electron microscopic pattern of amorphous substance deposition, and the diameter of the collagen fibrils, in lepidotrichia closely resemble those which are typical of cartilage. In addition, lepidotrichia contain chondroitin sulfate AC as the only sulfated glycosaminoglycan, and this glycosaminoglycan shows high levels of interaction with collagen, both features being characteristic of cartilage. Furthermore, the histochemical data presented in this paper suggest that not all of the glycosaminoglycans present in lepidotrichia are bound to protein cores to form proteoglycans. Each actinotrichium consists of a single ultrastructural entity of remarkable width and, thus, is not composed of a bundle of discretely separated collagen fibrils but rather of hyperpolymerized collagen molecules. This aspect differs from the arrangement pattern of all the other interstitial collagens, suggesting that actinotrichia may contain a new type of collagen.
Url:
DOI: 10.1007/BF00496739
Affiliations:
- Brésil, Espagne
- Andalousie, État de São Paulo
- Malaga, São Paulo
- Université de Malaga, Université de São Paulo
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The electron microscopic pattern of amorphous substance deposition, and the diameter of the collagen fibrils, in lepidotrichia closely resemble those which are typical of cartilage. In addition, lepidotrichia contain chondroitin sulfate AC as the only sulfated glycosaminoglycan, and this glycosaminoglycan shows high levels of interaction with collagen, both features being characteristic of cartilage. Furthermore, the histochemical data presented in this paper suggest that not all of the glycosaminoglycans present in lepidotrichia are bound to protein cores to form proteoglycans. Each actinotrichium consists of a single ultrastructural entity of remarkable width and, thus, is not composed of a bundle of discretely separated collagen fibrils but rather of hyperpolymerized collagen molecules. 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