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Journal of Cell Science, Vol 103, 273-285, Copyright © 1992 by Company of Biologists

Submitted on March 12, 1992
Accepted on June 5, 1992

Organization and characterization of fibrillar collagens in fish scales in situ and in vitro

L. ZYLBERBERG 1, J. BONAVENTURE 2, L. COHEN-SOLAL 2, D. J. HARTMANN 3, and J. BEREITERHAHN 4

1 Université Paris 7, Laboratoire d'Anatomie Comparée URA 11 37, 2, place Jussieu, 75251 Paris cedex 05, France
2 Hôpital des Enfants-Malades, Laboratoire de Physiopathologie des Tissus Conjonctifs pendant la Croissance URA 584, 149, rue de Sèvres,75743 Paris cedex 15, France
3 Institut Pasteur de Lyon, Centre de Radioanalyse, 13-15 rue Domer, 69366 Lyon, France
4 Goethe Universität, Arbeitskreis Kinematische Zellforschung, Senckenberganlage 27, 6000 Frankfurt am Main, Germany

The characterization of the fibrillar collagens and the cellular control of their spatial deposition were studied in fish scales using immunofluorescence, electron microscopy, electrophoretic and HPLC analyses, immunoprecipitation and hybridization with cDNA probes. This study was carried out on undisturbed and regenerating scales in situ and in organ and cell cultures from regenerating scales. The hyposquamal scleroblasts forming a pseudoepithelium show an apico-basal polarization and synthesize thick collagen fibrils (100 nm) organized in a plywood pattern as long as the integrity of the cell-cell and cell-collagenous matrix contacts are preserved. In culture, scleroblasts become fibroblastlike and produce an unordered meshwork of thin collagen fibrils (30 nm). Comparison of the synthesized collagens in culture with those extracted from the scales indicates that culture conditions modify fibrillogenesis but do not change the expression of fibrillar collagen genes. Type I collagen, the predominent component, is associated with the minor type V collagen. Type III collagen was not present. In type I collagen, a third chain, {alpha}3 chain, was identified. The ratio between the 3 chains suggests the coexistence of two heterotrimers ({alpha}(I))2 {alpha}2(I) and {alpha}l(I) {alpha}2(I) {alpha}3(I). Analysis by HPLC and electrophoresis of the cyanogen bromide-derived peptides obtained from the purified a3 chain support the hypothesis that {alpha}(I) and {alpha}3(I) chains are encoded by two different genes. The presence of the two types of heterotrimers in vivo as well as in vitro could correspond to an innate property of the goldfish scleroblasts. Despite the fact that teleost cyanogen bromide-derived peptides differ from those of higher vertebrates, homologies with the mammalian collagen genes (human, for example) are sufficient to allow the detection of mRNA transcripts for {alpha}l(I), {alpha}2(I) and {alpha}2(V) from confluent scleroblast cultures with human probes.

Key words: collagens, microtubules, culture, fish scales

Submitted on March 12, 1992
Accepted on June 5, 1992




This article has been cited by other articles:


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J. Histochem. Cytochem.Home page
G. Nicolas, F. Gaill, and L. Zylberberg
In Situ Localization of Two Fibrillar Collagens in Two Compact Connective Tissues by Immunoelectron Microscopy After Cryotechnical Processing
J. Histochem. Cytochem., January 1, 1997; 45(1): 119 - 128.
[Abstract] [Full Text] [PDF]




© The Company of Biologists Ltd 1992