The evolution of fibrillar collagens: A sea-pen collagen shares common features with vertebrate type V collagen

The extracellular matrix of marine primitive invertebrates (sponges, polyps and jellyfishes) contains collagen fibrils with narrow diameters. From various data, it has been hypothesized that these primitive collagens could represent ancestral forms of the vertebrate minor collagens, i.e. types V or...

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Bibliographic Details
Published in:Comparative Biochemistry and Physiology - Part B: Biochemistry and Molecular Biology 1996-02, Vol.113 (2), p.239-246
Main Authors: Tillet, E., Franc, J.M., Franc, S., Garrone, R.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Anthozoa
Antibodies
biochemistry
Biochemistry, Molecular Biology
cnidaria
coelenterates
collagen
Collagen - chemistry
Collagen - isolation & purification
Collagen - ultrastructure
Decapodiformes - chemistry
electron microscopy
evolution
extracellular matrix
Female
Humans
invertebrates
Life Sciences
Marine
mesoglea
Microscopy, Electron
Microscopy, Immunoelectron
Molecular Sequence Data
Pepsin A
Peptide Fragments - chemistry
Peptide Fragments - isolation & purification
Placenta - chemistry
Pregnancy
Rats
Veretillum cynomorium
Vertebrates
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Summary:The extracellular matrix of marine primitive invertebrates (sponges, polyps and jellyfishes) contains collagen fibrils with narrow diameters. From various data, it has been hypothesized that these primitive collagens could represent ancestral forms of the vertebrate minor collagens, i.e. types V or XI. Recently, we have isolated a primitive collagen from the soft tissues of the sea-pen Veretillum cynomorium(31). This report examines whether the sea-pen collagen shares some features with vertebrate type V collagen. Rotary shadowed images of acid-soluble collagen molecules extracted from β-APN treated animals, positive staining of segmentlong-spacing crystallites precipitated from pepsinized collagen, Western blots of the pepsinized α1 and α2 chains with antibodies to vertebrate types I, III and V collagens, and in situ gold immunolabeling of ECM collagen fibrils were examined. Our results showed that the tissue form of the sea-pen collagen is a 340-nm threadlike molecule, which is close to the vertebrate type V collagen with its voluminous terminal globular domain, the distribution of most of its polar amino-acid residues, and its antigenic properties.
ISSN:1096-4959
0305-0491
1879-1107
DOI:10.1016/0305-0491(95)02014-4