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Titolo:
The in vitro activity of ADAM-10 is inhibited by TIMP-1 and TIMP-3
Autore:
Amour, A; Knight, CG; Webster, A; Slocombe, PM; Stephens, PE; Knauper, V; Docherty, AJP; Murphy, G;
Indirizzi:
Univ E Anglia, Sch Biol Sci, Norwich NR4 7TJ, Norfolk, England Univ E Anglia Norwich Norfolk England NR4 7TJ h NR4 7TJ, Norfolk, England Celltech Grp PLC, Slough SL1 4EN, Berks, England Celltech Grp PLC Slough Berks England SL1 4EN ugh SL1 4EN, Berks, England Univ Cambridge, Dept Biochem, Cambridge CB2 1QW, England Univ Cambridge Cambridge England CB2 1QW hem, Cambridge CB2 1QW, England
Titolo Testata:
FEBS LETTERS
fascicolo: 3, volume: 473, anno: 2000,
pagine: 275 - 279
SICI:
0014-5793(20000519)473:3<275:TIVAOA>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
NECROSIS-FACTOR-ALPHA; TISSUE INHIBITOR; TNF-ALPHA; DISINTEGRIN-METALLOPROTEASE; CONVERTING-ENZYME; CLEAVAGE; PROTEIN; CLONING; DOMAIN; CELLS;
Keywords:
metalloproteinase; disintegrin metalloproteinase; tissue inhibitor of metalloproteinase;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
27
Recensione:
Indirizzi per estratti:
Indirizzo: Murphy, G Univ E Anglia, Sch Biol Sci, Norwich NR4 7TJ, Norfolk, England Univ E Anglia Norwich Norfolk England NR4 7TJ Norfolk, England
Citazione:
A. Amour et al., "The in vitro activity of ADAM-10 is inhibited by TIMP-1 and TIMP-3", FEBS LETTER, 473(3), 2000, pp. 275-279

Abstract

A recombinant soluble form of the catalytic domain of human ADAM-10 was expressed as an Fc fusion protein from myeloma cells. The ADAM-10,vas catalytically active, cleaving myelin basic protein and peptides based on the previously described 'metallosheddase' cleavage sites of tumour necrosis factoralpha, CD40 ligand and amyloid precursor protein. The myelin basic proteindegradation assay mas used to demonstrate that hydroxamate inhibitors of matrix metalloproteinases (MMPs) were also inhibitors of ADAM-10. The natural MMP inhibitors, TIMP-2 and TIMP-4 were unable to inhibit ADAM-10, but TIMP-1 and TIMP-3 were inhibitory. Using a quenched fluorescent substrate assay and ADAM-10 Ne obtained approximate apparent inhibition constants of 0.1 nM (TIMP-1) and 0.9 nM (TIMP-3). The TIMP-1 inhibition of ADAM-10 could therefore prove useful in distinguishing its activity from that of TACE, whichis only inhibited by TIMP-3, in cell based assays. (C) 2000 Federation of European Biochemical Societies.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 21/09/20 alle ore 06:34:03