The pro α2(V) collagen gene is evolutionarily related to the major fibrillar-forming collagens

Dominique Weil; Michael Bernard; Silvana Gargano; Francesco Ramirez

doi:10.1093/nar/15.1.181

The pro α2(V) collagen gene is evolutionarily related to the major fibrillar-forming collagens

Dominique Weil
, Michael Bernard
, Silvana Gargano
, Francesco Ramirez

Research output: Contribution to journal › Article › peer-review

75 Scopus citations

Abstract

A number of overlapping cDNA clones, covering 5.2 kb of sequences which code for the human pro α2(V) collagen chain, have been isolated. Analysis of the structural data have indicated a close evolutionary kinship between the pro α2(V) chain and the major fibrillar collagen types. Isolation and analysis of an 8 kb genomic fragment has further supported this notion by revealing a homologous arrangement of nine triple-helical domain exons. These studies have therefore provided conclusive evidence which categorizes the Type V collagen as a member of the Group 1 molecules, or fibrillar-forming collagens.

Original language	English
Pages (from-to)	181-198
Number of pages	18
Journal	Nucleic Acids Research
Volume	15
Issue number	1
DOIs	https://doi.org/10.1093/nar/15.1.181
State	Published - 12 Jan 1987
Externally published	Yes

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title = "The pro α2(V) collagen gene is evolutionarily related to the major fibrillar-forming collagens",

abstract = "A number of overlapping cDNA clones, covering 5.2 kb of sequences which code for the human pro α2(V) collagen chain, have been isolated. Analysis of the structural data have indicated a close evolutionary kinship between the pro α2(V) chain and the major fibrillar collagen types. Isolation and analysis of an 8 kb genomic fragment has further supported this notion by revealing a homologous arrangement of nine triple-helical domain exons. These studies have therefore provided conclusive evidence which categorizes the Type V collagen as a member of the Group 1 molecules, or fibrillar-forming collagens.",

author = "Dominique Weil and Michael Bernard and Silvana Gargano and Francesco Ramirez",

note = "Funding Information: ACKNOWLEDGEMENTS The authors wish to thank Drs. P. Berg, M.L. Chu, H. Okayama and G. Todaro for providing us with some of the materials used in these studies and Drs. B. Brodsky, W. deWet , P. Little and M. van der Rest for many helpful discussions and suggestions. We are also very much in debt to V. Benson-Chanda, D. Leviant, M. Leong and S. Salkeld for their help during the course of this work and Ms. M. Schneider for typing the manuscript. This work was supported by grants from the National Institute of Health (AR 386U8) and the March of Dimes, Birth Defect Foundation (1-10142) .",

year = "1987",

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doi = "10.1093/nar/15.1.181",

language = "English",

volume = "15",

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journal = "Nucleic Acids Research",

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T1 - The pro α2(V) collagen gene is evolutionarily related to the major fibrillar-forming collagens

AU - Weil, Dominique

AU - Bernard, Michael

AU - Gargano, Silvana

AU - Ramirez, Francesco

N1 - Funding Information: ACKNOWLEDGEMENTS The authors wish to thank Drs. P. Berg, M.L. Chu, H. Okayama and G. Todaro for providing us with some of the materials used in these studies and Drs. B. Brodsky, W. deWet , P. Little and M. van der Rest for many helpful discussions and suggestions. We are also very much in debt to V. Benson-Chanda, D. Leviant, M. Leong and S. Salkeld for their help during the course of this work and Ms. M. Schneider for typing the manuscript. This work was supported by grants from the National Institute of Health (AR 386U8) and the March of Dimes, Birth Defect Foundation (1-10142) .

PY - 1987/1/12

Y1 - 1987/1/12

N2 - A number of overlapping cDNA clones, covering 5.2 kb of sequences which code for the human pro α2(V) collagen chain, have been isolated. Analysis of the structural data have indicated a close evolutionary kinship between the pro α2(V) chain and the major fibrillar collagen types. Isolation and analysis of an 8 kb genomic fragment has further supported this notion by revealing a homologous arrangement of nine triple-helical domain exons. These studies have therefore provided conclusive evidence which categorizes the Type V collagen as a member of the Group 1 molecules, or fibrillar-forming collagens.

AB - A number of overlapping cDNA clones, covering 5.2 kb of sequences which code for the human pro α2(V) collagen chain, have been isolated. Analysis of the structural data have indicated a close evolutionary kinship between the pro α2(V) chain and the major fibrillar collagen types. Isolation and analysis of an 8 kb genomic fragment has further supported this notion by revealing a homologous arrangement of nine triple-helical domain exons. These studies have therefore provided conclusive evidence which categorizes the Type V collagen as a member of the Group 1 molecules, or fibrillar-forming collagens.

UR - https://www.scopus.com/pages/publications/0023108277

U2 - 10.1093/nar/15.1.181

DO - 10.1093/nar/15.1.181

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AN - SCOPUS:0023108277

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EP - 198

JO - Nucleic Acids Research

JF - Nucleic Acids Research

IS - 1

ER -

The pro α2(V) collagen gene is evolutionarily related to the major fibrillar-forming collagens

Abstract

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