A 92 kDa Gelatinase (MMP-9) cleavage site in native Type V collagen

Christopher Niyibizi, Roger Chan, Jiann Jiu Wu, David Eyre

Research output: Contribution to journalArticle

46 Citations (Scopus)

Abstract

Native type V collagen molecules resist mammalian collagenase but are cleaved by certain gelatinases. We report a prominent site of cleavage within the collagen type V molecules by 92 kDa gelatinase (MMP-9). The enzyme was purified from conditioned medium of a rabbit synovial cell line (HIG-82). It cleaved native type V collagen from bovine bone in solution at two molecular sites, one near the amino-terminus, the other producing a 3/5 C-terminal fragment. Amino-terminal sequence analysis of the individual α chains from this latter fragment showed that MMP-9 had cleaved between residues Gly439-Val in both α 1(V) and α(XI) and between residues Gly445-Leu in the α2(V) chain. These sites are close to the previously reported trypsin-cleavage site. The findings imply that gelatinases may be necessary for initiating or completing degradation of type I/type V copolymeric fibrils for growth and remodeling of extracellular collagen.

Original languageEnglish (US)
Pages (from-to)328-333
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume202
Issue number1
DOIs
StatePublished - Jul 15 1994

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Collagen Type V
Matrix Metalloproteinase 9
Matrix Metalloproteinases
Gelatinases
Molecules
Collagenases
Conditioned Culture Medium
Trypsin
Sequence Analysis
Bone
Collagen
Cells
Rabbits
Bone and Bones
Cell Line
Degradation
Enzymes
Growth

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

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abstract = "Native type V collagen molecules resist mammalian collagenase but are cleaved by certain gelatinases. We report a prominent site of cleavage within the collagen type V molecules by 92 kDa gelatinase (MMP-9). The enzyme was purified from conditioned medium of a rabbit synovial cell line (HIG-82). It cleaved native type V collagen from bovine bone in solution at two molecular sites, one near the amino-terminus, the other producing a 3/5 C-terminal fragment. Amino-terminal sequence analysis of the individual α chains from this latter fragment showed that MMP-9 had cleaved between residues Gly439-Val in both α 1(V) and α(XI) and between residues Gly445-Leu in the α2(V) chain. These sites are close to the previously reported trypsin-cleavage site. The findings imply that gelatinases may be necessary for initiating or completing degradation of type I/type V copolymeric fibrils for growth and remodeling of extracellular collagen.",
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A 92 kDa Gelatinase (MMP-9) cleavage site in native Type V collagen. / Niyibizi, Christopher; Chan, Roger; Wu, Jiann Jiu; Eyre, David.

In: Biochemical and Biophysical Research Communications, Vol. 202, No. 1, 15.07.1994, p. 328-333.

Research output: Contribution to journalArticle

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AB - Native type V collagen molecules resist mammalian collagenase but are cleaved by certain gelatinases. We report a prominent site of cleavage within the collagen type V molecules by 92 kDa gelatinase (MMP-9). The enzyme was purified from conditioned medium of a rabbit synovial cell line (HIG-82). It cleaved native type V collagen from bovine bone in solution at two molecular sites, one near the amino-terminus, the other producing a 3/5 C-terminal fragment. Amino-terminal sequence analysis of the individual α chains from this latter fragment showed that MMP-9 had cleaved between residues Gly439-Val in both α 1(V) and α(XI) and between residues Gly445-Leu in the α2(V) chain. These sites are close to the previously reported trypsin-cleavage site. The findings imply that gelatinases may be necessary for initiating or completing degradation of type I/type V copolymeric fibrils for growth and remodeling of extracellular collagen.

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