Activation of human progelatinase A by collagenase and matrilysin

Activation of procollagenase by matrilysin

Qingxiang Amy Sang, M. Kirby Bodden, L. Jack Windsor

Research output: Contribution to journalArticle

36 Citations (Scopus)

Abstract

Proteolytic and nonproteolytic methods were used to investigate the mechanism(s) by which human fibroblast progelatinase A and fibroblast-type procollagenase can be activated. Both collagenase and matrilysin were able to activate progelatinase A, resulting in an amino terminus in gelatinase A of Tyr.81 The cleavage occurred distal to Cys73 within the sequence of PRCGNPDVAN80-Y81NFFPRKP. While several nonproteolytic reagents were tested, only the heavy metal Hg(Π) and p-chloromercuribenzoate (PCMB) were able to induce activation of progelatinase A and resulted in the conversion of the latent 72-kDa gelatinase A to an active form of about 64.5 kDa. Matrilysin was also able to activate procollagenase and resulted in an amino terminus in collagenase of Phe.81 These results suggest that fibroblast-type collagenase and matrilysin may be physiologically relevant activators of progelatinase A; the maintenance of latency and the process of activation for progelatinase A may occur through the cysteine-switch mechanism, and the proteolytic activation of procollagenase by matrilysin resulted in the same amino terminus as produced by stromelysin-1.

Original languageEnglish (US)
Pages (from-to)243-253
Number of pages11
JournalProtein Journal
Volume15
Issue number3
StatePublished - 1996
Externally publishedYes

Fingerprint

Matrix Metalloproteinase 7
Collagenases
Fibroblasts
Chemical activation
Matrix Metalloproteinase 2
Heavy metals
Matrix Metalloproteinase 8
Chloromercuribenzoates
Matrix Metalloproteinase 3
Switches
Heavy Metals
Cysteine
Maintenance
progelatinase
procollagenase

Keywords

  • Collagenase
  • Gelatinase A
  • Matrilysin
  • Matrix metalloproteinases
  • Zymogen activation

ASJC Scopus subject areas

  • Biochemistry
  • Analytical Chemistry
  • Organic Chemistry
  • Bioengineering

Cite this

Activation of human progelatinase A by collagenase and matrilysin : Activation of procollagenase by matrilysin. / Sang, Qingxiang Amy; Bodden, M. Kirby; Windsor, L. Jack.

In: Protein Journal, Vol. 15, No. 3, 1996, p. 243-253.

Research output: Contribution to journalArticle

@article{918cffc491e549ae91f98897fd743374,
title = "Activation of human progelatinase A by collagenase and matrilysin: Activation of procollagenase by matrilysin",
abstract = "Proteolytic and nonproteolytic methods were used to investigate the mechanism(s) by which human fibroblast progelatinase A and fibroblast-type procollagenase can be activated. Both collagenase and matrilysin were able to activate progelatinase A, resulting in an amino terminus in gelatinase A of Tyr.81 The cleavage occurred distal to Cys73 within the sequence of PRCGNPDVAN80-Y81NFFPRKP. While several nonproteolytic reagents were tested, only the heavy metal Hg(Π) and p-chloromercuribenzoate (PCMB) were able to induce activation of progelatinase A and resulted in the conversion of the latent 72-kDa gelatinase A to an active form of about 64.5 kDa. Matrilysin was also able to activate procollagenase and resulted in an amino terminus in collagenase of Phe.81 These results suggest that fibroblast-type collagenase and matrilysin may be physiologically relevant activators of progelatinase A; the maintenance of latency and the process of activation for progelatinase A may occur through the cysteine-switch mechanism, and the proteolytic activation of procollagenase by matrilysin resulted in the same amino terminus as produced by stromelysin-1.",
keywords = "Collagenase, Gelatinase A, Matrilysin, Matrix metalloproteinases, Zymogen activation",
author = "Sang, {Qingxiang Amy} and Bodden, {M. Kirby} and Windsor, {L. Jack}",
year = "1996",
language = "English (US)",
volume = "15",
pages = "243--253",
journal = "Protein Journal",
issn = "1572-3887",
publisher = "Springer New York",
number = "3",

}

TY - JOUR

T1 - Activation of human progelatinase A by collagenase and matrilysin

T2 - Activation of procollagenase by matrilysin

AU - Sang, Qingxiang Amy

AU - Bodden, M. Kirby

AU - Windsor, L. Jack

PY - 1996

Y1 - 1996

N2 - Proteolytic and nonproteolytic methods were used to investigate the mechanism(s) by which human fibroblast progelatinase A and fibroblast-type procollagenase can be activated. Both collagenase and matrilysin were able to activate progelatinase A, resulting in an amino terminus in gelatinase A of Tyr.81 The cleavage occurred distal to Cys73 within the sequence of PRCGNPDVAN80-Y81NFFPRKP. While several nonproteolytic reagents were tested, only the heavy metal Hg(Π) and p-chloromercuribenzoate (PCMB) were able to induce activation of progelatinase A and resulted in the conversion of the latent 72-kDa gelatinase A to an active form of about 64.5 kDa. Matrilysin was also able to activate procollagenase and resulted in an amino terminus in collagenase of Phe.81 These results suggest that fibroblast-type collagenase and matrilysin may be physiologically relevant activators of progelatinase A; the maintenance of latency and the process of activation for progelatinase A may occur through the cysteine-switch mechanism, and the proteolytic activation of procollagenase by matrilysin resulted in the same amino terminus as produced by stromelysin-1.

AB - Proteolytic and nonproteolytic methods were used to investigate the mechanism(s) by which human fibroblast progelatinase A and fibroblast-type procollagenase can be activated. Both collagenase and matrilysin were able to activate progelatinase A, resulting in an amino terminus in gelatinase A of Tyr.81 The cleavage occurred distal to Cys73 within the sequence of PRCGNPDVAN80-Y81NFFPRKP. While several nonproteolytic reagents were tested, only the heavy metal Hg(Π) and p-chloromercuribenzoate (PCMB) were able to induce activation of progelatinase A and resulted in the conversion of the latent 72-kDa gelatinase A to an active form of about 64.5 kDa. Matrilysin was also able to activate procollagenase and resulted in an amino terminus in collagenase of Phe.81 These results suggest that fibroblast-type collagenase and matrilysin may be physiologically relevant activators of progelatinase A; the maintenance of latency and the process of activation for progelatinase A may occur through the cysteine-switch mechanism, and the proteolytic activation of procollagenase by matrilysin resulted in the same amino terminus as produced by stromelysin-1.

KW - Collagenase

KW - Gelatinase A

KW - Matrilysin

KW - Matrix metalloproteinases

KW - Zymogen activation

UR - http://www.scopus.com/inward/record.url?scp=53349171709&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=53349171709&partnerID=8YFLogxK

M3 - Article

VL - 15

SP - 243

EP - 253

JO - Protein Journal

JF - Protein Journal

SN - 1572-3887

IS - 3

ER -