Characterization of a Non-fibrillar-Related Collagen in the Mollusc Haliotis tuberculata and its Biological Activity on Human Dermal Fibroblasts

In invertebrates, members of the collagen family have been found in various phyla. Surprisingly, in mollusc, little is known about such molecules. In this study, we characterize the full-length abalone type IV collagen and we analysed its biological effects on human fibroblast in order to gain insig...

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Veröffentlicht in:Marine biotechnology (New York, N.Y.) N.Y.), 2011-10, Vol.13 (5), p.1003-1016
Hauptverfasser: Fleury, Christophe, Serpentini, Antoine, Kypriotou, Magdalini, Renard, Emmanuelle, Galéra, Philippe, Lebel, Jean-Marc
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container_issue 5
container_start_page 1003
container_title Marine biotechnology (New York, N.Y.)
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creator Fleury, Christophe
Serpentini, Antoine
Kypriotou, Magdalini
Renard, Emmanuelle
Galéra, Philippe
Lebel, Jean-Marc
description In invertebrates, members of the collagen family have been found in various phyla. Surprisingly, in mollusc, little is known about such molecules. In this study, we characterize the full-length abalone type IV collagen and we analysed its biological effects on human fibroblast in order to gain insights about this molecule in molluscs and particularly clues about its roles. We screened a cDNA library of Haliotis tuberculata hemocytes. The expression pattern of the transcript is determined using real-time polymerase chain reaction and in situ hybridization. The close identity between α1(IV) C-terminal domain and the vertebrate homologue led us to produce, purify and test in vitro a recombinant protein corresponding to this region using human dermal fibroblasts cell culture. The biological effects were evaluated on proliferation and on differentiation. We found that the 5,334-bp open reading frame transcript encodes a protein of 1,777 amino acids, including an interrupted 1,502-residue collagenous domain and a 232-residue C-terminal non-collagenous domain. The expression pattern of this transcript is mainly found in the mantle and hemocytes. The recombinant protein corresponding α1(IV) C-terminal domain increased fibroblast proliferation by 69% and doubled collagen synthesis produced in primary cultures. This work provides the first complete primary structure of a mollusc non-fibrillar collagen chain and the biological effects of its C-terminal domain on human cells. In this study, we prove that the NC1 domain from a molluscan collagen can improve human fibroblast proliferation as well as differentiation.
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issn 1436-2228
1436-2236
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source MEDLINE; SpringerLink (Online service)
subjects abalone
Amino Acid Sequence
Amino acids
Analysis
Animal biology
Animals
bioactive properties
Biological activity
Biological effects
Biomedical and Life Sciences
Biotechnology
cDNA libraries
cell culture
Cell division
Cells, Cultured
Collagen
Collagen - chemistry
Collagen - metabolism
Collagen - pharmacology
complementary DNA
Engineering
Fibroblasts
Fibroblasts - drug effects
Freshwater & Marine Ecology
Gene expression
Gene Expression Regulation - physiology
Genetic recombination
Haliotis
Haliotis tuberculata
hemocytes
Humans
in situ hybridization
Invertebrate Zoology
Invertebrates
Life Sciences
Marine
Microbiology
Molecular Sequence Data
Mollusca - metabolism
Mollusks
open reading frames
Original Article
Polymerase Chain Reaction
Protein Structure, Tertiary
Proteins
quantitative polymerase chain reaction
RNA, Messenger - genetics
RNA, Messenger - metabolism
Studies
Zoology
title Characterization of a Non-fibrillar-Related Collagen in the Mollusc Haliotis tuberculata and its Biological Activity on Human Dermal Fibroblasts
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