Isolation and partial characterization of a new human collagen with an extended triple-helical structural domain

H. Bentz, N. P. Morris, L. W. Murray, Lynn Sakai, D. W. Hollister, R. E. Burgeson

Research output: Contribution to journalArticle

85 Citations (Scopus)

Abstract

The collagens are a family of major connective tissue proteins that are known to be the products of at least 11 distinct genes. Primary structural differences between the individual collagen types are thought to reflect functional diversity. We have isolated a previously unknown collagen gene product, termed 'long-chain' (LC) collagen, from human chorioamniotic membranes by limited pepsin digestion. Comparison of the isolated α-chain subunit to the α chains of other collagen types by amino acid composition, peptide mapping with either cyanogen bromide fragmentation or staphylococcal V8 protease digestion, chromatographic elution position, and relative molecular weight indicates that this protein is a product of a previously unrecognized gene. We report structural studies indicating that this molecule contains three identical α-chain subunits that are each approximately molecular weight 170,000. The amino acid composition of LC α chains suggests that they are about 90% triple helical. Comparisons of the length of segment-long-spacing (SLS) crystallites made from LC molecules with those from types I and V collagens indicate that the LC molecule is substantially longer than these collagens and somewhat longer than the reported length of type IV collagen. This finding suggests that LC collagen represents an additional class of collagen molecules. We suggest that these molecules be referred to as type VII collagen.

Original languageEnglish (US)
Pages (from-to)3168-3172
Number of pages5
JournalUnknown Journal
Volume80
Issue number11 I
DOIs
StatePublished - Jan 1 1983
Externally publishedYes

Fingerprint

Collagen
Digestion
Molecular Weight
Collagen Type VII
Collagen Type V
Genes
Amino Acids
Cyanogen Bromide
Peptide Mapping
Collagen Type IV
Pepsin A
Collagen Type I
Individuality
Connective Tissue
Proteins
Membranes

ASJC Scopus subject areas

  • General

Cite this

Isolation and partial characterization of a new human collagen with an extended triple-helical structural domain. / Bentz, H.; Morris, N. P.; Murray, L. W.; Sakai, Lynn; Hollister, D. W.; Burgeson, R. E.

In: Unknown Journal, Vol. 80, No. 11 I, 01.01.1983, p. 3168-3172.

Research output: Contribution to journalArticle

Bentz, H. ; Morris, N. P. ; Murray, L. W. ; Sakai, Lynn ; Hollister, D. W. ; Burgeson, R. E. / Isolation and partial characterization of a new human collagen with an extended triple-helical structural domain. In: Unknown Journal. 1983 ; Vol. 80, No. 11 I. pp. 3168-3172.
@article{d1d81298c5dc4eb2b1abb28a3b6045ab,
title = "Isolation and partial characterization of a new human collagen with an extended triple-helical structural domain",
abstract = "The collagens are a family of major connective tissue proteins that are known to be the products of at least 11 distinct genes. Primary structural differences between the individual collagen types are thought to reflect functional diversity. We have isolated a previously unknown collagen gene product, termed 'long-chain' (LC) collagen, from human chorioamniotic membranes by limited pepsin digestion. Comparison of the isolated α-chain subunit to the α chains of other collagen types by amino acid composition, peptide mapping with either cyanogen bromide fragmentation or staphylococcal V8 protease digestion, chromatographic elution position, and relative molecular weight indicates that this protein is a product of a previously unrecognized gene. We report structural studies indicating that this molecule contains three identical α-chain subunits that are each approximately molecular weight 170,000. The amino acid composition of LC α chains suggests that they are about 90{\%} triple helical. Comparisons of the length of segment-long-spacing (SLS) crystallites made from LC molecules with those from types I and V collagens indicate that the LC molecule is substantially longer than these collagens and somewhat longer than the reported length of type IV collagen. This finding suggests that LC collagen represents an additional class of collagen molecules. We suggest that these molecules be referred to as type VII collagen.",
author = "H. Bentz and Morris, {N. P.} and Murray, {L. W.} and Lynn Sakai and Hollister, {D. W.} and Burgeson, {R. E.}",
year = "1983",
month = "1",
day = "1",
doi = "10.1073/pnas.80.11.3168",
language = "English (US)",
volume = "80",
pages = "3168--3172",
journal = "Indian Journal of Rheumatology",
issn = "0973-3698",
publisher = "Elsevier (Singapore) Pte Ltd",
number = "11 I",

}

TY - JOUR

T1 - Isolation and partial characterization of a new human collagen with an extended triple-helical structural domain

AU - Bentz, H.

AU - Morris, N. P.

AU - Murray, L. W.

AU - Sakai, Lynn

AU - Hollister, D. W.

AU - Burgeson, R. E.

PY - 1983/1/1

Y1 - 1983/1/1

N2 - The collagens are a family of major connective tissue proteins that are known to be the products of at least 11 distinct genes. Primary structural differences between the individual collagen types are thought to reflect functional diversity. We have isolated a previously unknown collagen gene product, termed 'long-chain' (LC) collagen, from human chorioamniotic membranes by limited pepsin digestion. Comparison of the isolated α-chain subunit to the α chains of other collagen types by amino acid composition, peptide mapping with either cyanogen bromide fragmentation or staphylococcal V8 protease digestion, chromatographic elution position, and relative molecular weight indicates that this protein is a product of a previously unrecognized gene. We report structural studies indicating that this molecule contains three identical α-chain subunits that are each approximately molecular weight 170,000. The amino acid composition of LC α chains suggests that they are about 90% triple helical. Comparisons of the length of segment-long-spacing (SLS) crystallites made from LC molecules with those from types I and V collagens indicate that the LC molecule is substantially longer than these collagens and somewhat longer than the reported length of type IV collagen. This finding suggests that LC collagen represents an additional class of collagen molecules. We suggest that these molecules be referred to as type VII collagen.

AB - The collagens are a family of major connective tissue proteins that are known to be the products of at least 11 distinct genes. Primary structural differences between the individual collagen types are thought to reflect functional diversity. We have isolated a previously unknown collagen gene product, termed 'long-chain' (LC) collagen, from human chorioamniotic membranes by limited pepsin digestion. Comparison of the isolated α-chain subunit to the α chains of other collagen types by amino acid composition, peptide mapping with either cyanogen bromide fragmentation or staphylococcal V8 protease digestion, chromatographic elution position, and relative molecular weight indicates that this protein is a product of a previously unrecognized gene. We report structural studies indicating that this molecule contains three identical α-chain subunits that are each approximately molecular weight 170,000. The amino acid composition of LC α chains suggests that they are about 90% triple helical. Comparisons of the length of segment-long-spacing (SLS) crystallites made from LC molecules with those from types I and V collagens indicate that the LC molecule is substantially longer than these collagens and somewhat longer than the reported length of type IV collagen. This finding suggests that LC collagen represents an additional class of collagen molecules. We suggest that these molecules be referred to as type VII collagen.

UR - http://www.scopus.com/inward/record.url?scp=0038793126&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0038793126&partnerID=8YFLogxK

U2 - 10.1073/pnas.80.11.3168

DO - 10.1073/pnas.80.11.3168

M3 - Article

C2 - 6574478

AN - SCOPUS:0038793126

VL - 80

SP - 3168

EP - 3172

JO - Indian Journal of Rheumatology

JF - Indian Journal of Rheumatology

SN - 0973-3698

IS - 11 I

ER -