DEGRADATION OF KININS, ANGIOTENSINS AND SUBSTANCE-P BY POLYMORPHONUCLEAR MATRIX METALLOPROTEINASES MMP-8 AND MMP-9

DIEKMANN O, Tschesche H (1994)
In: BRAZILIAN JOURNAL OF MEDICAL AND BIOLOGICAL RESEARCH. 27. ASSOC BRAS DIVULG CIENTIFICA: 1865-1876.

Conference Paper | Published | English

No fulltext has been uploaded

Author
;
Abstract
1. The kinetics of the degradation of the kinins bradykinin and Met-Lys-bradykinin, angiotensins I and II and the tachykinin substance P by PMNL-collagenase (MMP 8), PMNL-gelatinase (MMP 9) and by the recombinant catalytic domain of MMP 8 (rcd-PMNL-c) was examined by RP-HPLC. The resulting fragments were identified by automated Edman degradation or by amino acid analysis. 2. The initial degradation rates of substance P at a substrate concentration of 25 mu M were 5 min(-1) for MMP 9 and 150 min(-1) for MMP 8. The kinetic constants K-M and k(cat) were determined by concentration-dependent measurements. For MMP 8/substance P the constants were K-M = 78 +/- 14 mu M and k(cat) = 412 +/- 67 min(-1). For MMP 9/substance P the constants were K-M = 91 +/- 15 mu M and k(cat) = 25 +/- 4 min(-1). Both enzymes cleaved substance P between Gln(6) and Phe(7) and between Gly(9) and Leu(10). 3. Under the same conditions, MMP 8 degraded angiotensin I at an initial rate of 20 h(-1) resulting mainly in the vasoactive fragments angiotensin II and angiotensin(1-7). At a substrate concentration of 25 mu M and an enzyme/substrate ratio of 1:100, angiotensin II was degraded very slowly (19% in 24 h) by MMP 8. Under these conditions, MMP 9 degraded angiotensin I to a lesser extent than MMP 8 (25% in 24 h) and was unable to cleave angiotensin II. 4. Under the same conditions, bradykinin and Met-Lys-bradykinin were cleaved by PMNL-collagenase at a rate of 20% in 24 h, producing BK(1-7) and BK(1-8). PMNL-gelatinase was unable to cleave the kinins under these conditions. 5. In all cases, rcd-PMNL-c produced the same fragments as wild type PMNL-collagenase, but at a significantly lower rate.
Publishing Year
ISSN
PUB-ID

Cite this

DIEKMANN O, Tschesche H. DEGRADATION OF KININS, ANGIOTENSINS AND SUBSTANCE-P BY POLYMORPHONUCLEAR MATRIX METALLOPROTEINASES MMP-8 AND MMP-9. In: BRAZILIAN JOURNAL OF MEDICAL AND BIOLOGICAL RESEARCH. Vol 27. ASSOC BRAS DIVULG CIENTIFICA; 1994: 1865-1876.
DIEKMANN, O., & Tschesche, H. (1994). DEGRADATION OF KININS, ANGIOTENSINS AND SUBSTANCE-P BY POLYMORPHONUCLEAR MATRIX METALLOPROTEINASES MMP-8 AND MMP-9. BRAZILIAN JOURNAL OF MEDICAL AND BIOLOGICAL RESEARCH, 27(8), 1865-1876.
DIEKMANN, O., and Tschesche, H. (1994). “DEGRADATION OF KININS, ANGIOTENSINS AND SUBSTANCE-P BY POLYMORPHONUCLEAR MATRIX METALLOPROTEINASES MMP-8 AND MMP-9” in BRAZILIAN JOURNAL OF MEDICAL AND BIOLOGICAL RESEARCH, vol. 27, (ASSOC BRAS DIVULG CIENTIFICA), 1865-1876.
DIEKMANN, O., & Tschesche, H., 1994. DEGRADATION OF KININS, ANGIOTENSINS AND SUBSTANCE-P BY POLYMORPHONUCLEAR MATRIX METALLOPROTEINASES MMP-8 AND MMP-9. In BRAZILIAN JOURNAL OF MEDICAL AND BIOLOGICAL RESEARCH. no.27 ASSOC BRAS DIVULG CIENTIFICA, pp. 1865-1876.
O. DIEKMANN and H. Tschesche, “DEGRADATION OF KININS, ANGIOTENSINS AND SUBSTANCE-P BY POLYMORPHONUCLEAR MATRIX METALLOPROTEINASES MMP-8 AND MMP-9”, BRAZILIAN JOURNAL OF MEDICAL AND BIOLOGICAL RESEARCH, vol. 27, ASSOC BRAS DIVULG CIENTIFICA, 1994, pp.1865-1876.
DIEKMANN, O., Tschesche, H.: DEGRADATION OF KININS, ANGIOTENSINS AND SUBSTANCE-P BY POLYMORPHONUCLEAR MATRIX METALLOPROTEINASES MMP-8 AND MMP-9. BRAZILIAN JOURNAL OF MEDICAL AND BIOLOGICAL RESEARCH. 27, p. 1865-1876. ASSOC BRAS DIVULG CIENTIFICA (1994).
DIEKMANN, O, and Tschesche, Harald. “DEGRADATION OF KININS, ANGIOTENSINS AND SUBSTANCE-P BY POLYMORPHONUCLEAR MATRIX METALLOPROTEINASES MMP-8 AND MMP-9”. BRAZILIAN JOURNAL OF MEDICAL AND BIOLOGICAL RESEARCH. ASSOC BRAS DIVULG CIENTIFICA, 1994.Vol. 27. 1865-1876.
This data publication is cited in the following publications:
This publication cites the following data publications:

12 Citations in Europe PMC

Data provided by Europe PubMed Central.

Substance P and Acute Pain in Patients Undergoing Orthopedic Surgery.
Lisowska B, Siewruk K, Lisowski A., PLoS ONE 11(1), 2016
PMID: 26731421
Matrix metalloproteinase-13 predominates over matrix metalloproteinase-8 as the functional interstitial collagenase in mouse atheromata.
Quillard T, Araujo HA, Franck G, Tesmenitsky Y, Libby P., Arterioscler. Thromb. Vasc. Biol. 34(6), 2014
PMID: 24723558
Topically applied substance P enhanced healing of open excision wound in rats.
Kant V, Gopal A, Kumar D, Bag S, Kurade NP, Kumar A, Tandan SK, Kumar D., Eur. J. Pharmacol. 715(1-3), 2013
PMID: 23684543
An important role of matrix metalloproteinase-8 in angiogenesis in vitro and in vivo.
Fang C, Wen G, Zhang L, Lin L, Moore A, Wu S, Ye S, Xiao Q., Cardiovasc. Res. 99(1), 2013
PMID: 23512982
MMP-8 promotes polymorphonuclear cell migration through collagen barriers in obliterative bronchiolitis.
Khatwa UA, Kleibrink BE, Shapiro SD, Subramaniam M., J. Leukoc. Biol. 87(1), 2010
PMID: 19801498
A role of matrix metalloproteinase-8 in atherosclerosis.
Laxton RC, Hu Y, Duchene J, Zhang F, Zhang Z, Leung KY, Xiao Q, Scotland RS, Hodgkinson CP, Smith K, Willeit J, Lopez-Otin C, Simpson IA, Kiechl S, Ahluwalia A, Xu Q, Ye S., Circ. Res. 105(9), 2009
PMID: 19745165
ACE inhibitors to block MMP-9 activity: new functions for old inhibitors.
Jin Y, Han HC, Lindsey ML., J. Mol. Cell. Cardiol. 43(6), 2007
PMID: 17949743
Inflammation, proteases and cancer.
van Kempen LC, de Visser KE, Coussens LM., Eur. J. Cancer 42(6), 2006
PMID: 16524717
Matrix metalloproteinases and their tissue inhibitors in endocrinology.
Salamonsen LA., Trends Endocrinol. Metab. 7(1), 1996
PMID: 18406722
Kininase of the Latrodectus tredecimguttatus venom: a study of its enzyme substrate specificity.
Akhunov AA, Makevnina LG, Golubenko Z, Paskhina TS., Immunopharmacology 32(1-3), 1996
PMID: 8796297
X-ray structures of human neutrophil collagenase complexed with peptide hydroxamate and peptide thiol inhibitors. Implications for substrate binding and rational drug design.
Grams F, Reinemer P, Powers JC, Kleine T, Pieper M, Tschesche H, Huber R, Bode W., Eur. J. Biochem. 228(3), 1995
PMID: 7737183

Export

0 Marked Publications

Open Data PUB

Web of Science

View record in Web of Science®

Sources

PMID: 7538373
PubMed | Europe PMC

Search this title in

Google Scholar