Novel nonmatrix-metalloproteinase-mediated collagen degradation

F. Song, L. Windsor

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

Matrix metalloproteinases (MMPs) and their inhibitors have long been believed to play a major role in the collagen loss seen in destructive temporomandibular joint (TMJ) disorders. This project was originally designed to examine the expression of MMPs and the tissue inhibitors of MMPs (TIMPs) by diseased human TMJ synovial fibroblasts and to determine their ability to degrade Type I collagen. Reverse transcriptase-PCR indicated that these TMJ synovial fibroblasts expressed mRNA for multiple MMPs and TIMPs. The collagen degradation assay showed that these TMJ synovial fibroblasts at passage 3 to 8 were capable of digesting the collagen underneath them on collagen-coated plates. This degradation was inhibited by GM6001, a synthetic MMP inhibitor. During passage 8 to 13, these TMJ fibroblasts were able to digest all the collagen in the wells. This degradation was completely inhibited by combining GM6001 and soybean trypsin inhibitor (STI), a serine proteinase inhibitor. The collagen cleavage activity of collected conditioned media was dramatically inhibited by STI but not by 1,10-phenanthroline, an MMP inhibitor. The data suggest that these TMJ cells utilize a MMP-dependent pathway and a novel MMP-independent pathway to digest Type I collagen.

Original languageEnglish (US)
Pages (from-to)65-72
Number of pages8
JournalBiochimica et Biophysica Acta - General Subjects
Volume1721
Issue number1-3
DOIs
StatePublished - Jan 19 2005

Fingerprint

Metalloproteases
Matrix Metalloproteinase Inhibitors
Collagen
Temporomandibular Joint
Fibroblasts
Matrix Metalloproteinases
Degradation
Temporomandibular Joint Disorders
Trypsin Inhibitors
Collagen Type I
Soybeans
Tissue
Tissue Inhibitor of Metalloproteinases
Serine Proteinase Inhibitors
RNA-Directed DNA Polymerase
Conditioned Culture Medium
Reverse Transcriptase Polymerase Chain Reaction
Assays
Messenger RNA

Keywords

  • Collagen degradation
  • Destructive temporomandibular joint disorder
  • Fibroblast
  • Matrix metalloproteinase
  • Serine proteinase

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Novel nonmatrix-metalloproteinase-mediated collagen degradation. / Song, F.; Windsor, L.

In: Biochimica et Biophysica Acta - General Subjects, Vol. 1721, No. 1-3, 19.01.2005, p. 65-72.

Research output: Contribution to journalArticle

@article{bb2deaf72ab24a12b59cdc867c34f09b,
title = "Novel nonmatrix-metalloproteinase-mediated collagen degradation",
abstract = "Matrix metalloproteinases (MMPs) and their inhibitors have long been believed to play a major role in the collagen loss seen in destructive temporomandibular joint (TMJ) disorders. This project was originally designed to examine the expression of MMPs and the tissue inhibitors of MMPs (TIMPs) by diseased human TMJ synovial fibroblasts and to determine their ability to degrade Type I collagen. Reverse transcriptase-PCR indicated that these TMJ synovial fibroblasts expressed mRNA for multiple MMPs and TIMPs. The collagen degradation assay showed that these TMJ synovial fibroblasts at passage 3 to 8 were capable of digesting the collagen underneath them on collagen-coated plates. This degradation was inhibited by GM6001, a synthetic MMP inhibitor. During passage 8 to 13, these TMJ fibroblasts were able to digest all the collagen in the wells. This degradation was completely inhibited by combining GM6001 and soybean trypsin inhibitor (STI), a serine proteinase inhibitor. The collagen cleavage activity of collected conditioned media was dramatically inhibited by STI but not by 1,10-phenanthroline, an MMP inhibitor. The data suggest that these TMJ cells utilize a MMP-dependent pathway and a novel MMP-independent pathway to digest Type I collagen.",
keywords = "Collagen degradation, Destructive temporomandibular joint disorder, Fibroblast, Matrix metalloproteinase, Serine proteinase",
author = "F. Song and L. Windsor",
year = "2005",
month = "1",
day = "19",
doi = "10.1016/j.bbagen.2004.10.007",
language = "English (US)",
volume = "1721",
pages = "65--72",
journal = "Biochimica et Biophysica Acta - General Subjects",
issn = "0304-4165",
publisher = "Elsevier",
number = "1-3",

}

TY - JOUR

T1 - Novel nonmatrix-metalloproteinase-mediated collagen degradation

AU - Song, F.

AU - Windsor, L.

PY - 2005/1/19

Y1 - 2005/1/19

N2 - Matrix metalloproteinases (MMPs) and their inhibitors have long been believed to play a major role in the collagen loss seen in destructive temporomandibular joint (TMJ) disorders. This project was originally designed to examine the expression of MMPs and the tissue inhibitors of MMPs (TIMPs) by diseased human TMJ synovial fibroblasts and to determine their ability to degrade Type I collagen. Reverse transcriptase-PCR indicated that these TMJ synovial fibroblasts expressed mRNA for multiple MMPs and TIMPs. The collagen degradation assay showed that these TMJ synovial fibroblasts at passage 3 to 8 were capable of digesting the collagen underneath them on collagen-coated plates. This degradation was inhibited by GM6001, a synthetic MMP inhibitor. During passage 8 to 13, these TMJ fibroblasts were able to digest all the collagen in the wells. This degradation was completely inhibited by combining GM6001 and soybean trypsin inhibitor (STI), a serine proteinase inhibitor. The collagen cleavage activity of collected conditioned media was dramatically inhibited by STI but not by 1,10-phenanthroline, an MMP inhibitor. The data suggest that these TMJ cells utilize a MMP-dependent pathway and a novel MMP-independent pathway to digest Type I collagen.

AB - Matrix metalloproteinases (MMPs) and their inhibitors have long been believed to play a major role in the collagen loss seen in destructive temporomandibular joint (TMJ) disorders. This project was originally designed to examine the expression of MMPs and the tissue inhibitors of MMPs (TIMPs) by diseased human TMJ synovial fibroblasts and to determine their ability to degrade Type I collagen. Reverse transcriptase-PCR indicated that these TMJ synovial fibroblasts expressed mRNA for multiple MMPs and TIMPs. The collagen degradation assay showed that these TMJ synovial fibroblasts at passage 3 to 8 were capable of digesting the collagen underneath them on collagen-coated plates. This degradation was inhibited by GM6001, a synthetic MMP inhibitor. During passage 8 to 13, these TMJ fibroblasts were able to digest all the collagen in the wells. This degradation was completely inhibited by combining GM6001 and soybean trypsin inhibitor (STI), a serine proteinase inhibitor. The collagen cleavage activity of collected conditioned media was dramatically inhibited by STI but not by 1,10-phenanthroline, an MMP inhibitor. The data suggest that these TMJ cells utilize a MMP-dependent pathway and a novel MMP-independent pathway to digest Type I collagen.

KW - Collagen degradation

KW - Destructive temporomandibular joint disorder

KW - Fibroblast

KW - Matrix metalloproteinase

KW - Serine proteinase

UR - http://www.scopus.com/inward/record.url?scp=11844299608&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=11844299608&partnerID=8YFLogxK

U2 - 10.1016/j.bbagen.2004.10.007

DO - 10.1016/j.bbagen.2004.10.007

M3 - Article

VL - 1721

SP - 65

EP - 72

JO - Biochimica et Biophysica Acta - General Subjects

JF - Biochimica et Biophysica Acta - General Subjects

SN - 0304-4165

IS - 1-3

ER -