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Titolo:
Characterization of C-terminally truncated human tissue inhibitor of metalloproteinases-4 expressed in Pichia pastoris
Autore:
Stratmann, B; Farr, M; Tschesche, H;
Indirizzi:
Univ Bielefeld, Fac Chem, D-33615 Bielefeld, Germany Univ Bielefeld Bielefeld Germany D-33615 hem, D-33615 Bielefeld, Germany
Titolo Testata:
BIOLOGICAL CHEMISTRY
fascicolo: 6, volume: 382, anno: 2001,
pagine: 987 - 991
SICI:
1431-6730(200106)382:6<987:COCTHT>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
RECOMBINANT CATALYTIC DOMAIN; MATRIX METALLOPROTEINASES; PROGELATINASE-A; COLLAGENASE; TIMP-1; SPECIFICITY; ACTIVATION; MECHANISM; AFFINITY; REGION;
Keywords:
matrix metalloproteinase (MMP); Pichia pastoris; tissue inhibitor of metalloproteinases (TIMP);
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
26
Recensione:
Indirizzi per estratti:
Indirizzo: Tschesche, H Univ Bielefeld, Fac Chem, D-33615 Bielefeld, Germany Univ Bielefeld Bielefeld Germany D-33615 Bielefeld, Germany
Citazione:
B. Stratmann et al., "Characterization of C-terminally truncated human tissue inhibitor of metalloproteinases-4 expressed in Pichia pastoris", BIOL CHEM, 382(6), 2001, pp. 987-991

Abstract

The tight regulation of extracellular matrix remodeling and degradation isof great importance in physiological processes like development and morphogenesis, as well as in pathological situations like tumor invasion and metastasis. Tissue inhibitors of metalloproteinases (TIMPs) are the naturally occuring inhibitors of matrix metalloproteinases, which are involved in matrix turnover. In this report we describe the cloning of human TIMP-4 from a human adenocarcinoma and an osteosarcoma cell line and the expression of the inhibitorydomain in the methylotrophic yeast Pichia pastoris. The inhibition of MMP-8, -9, -12, -13 and -14 by the N-terminal domain of TIMP-4 was analysed. Using a fluorescent MCA-peptide, K-i values for each subclass of MMPs were determined. With dissociation constants in the nanomolar range, TIMP-4 seems to be a good inhibitor for all classes of MMPs without remarkable preference for special MMPs.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/03/20 alle ore 08:02:49