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Titolo:
Expression and enzymatic activity of human disintegrin and metalloproteinase ADAM19/meltrin beta
Autore:
Wei, P; Zhao, YG; Zhuang, L; Ruben, S; Sang, QXA;
Indirizzi:
Florida State Univ, Dept Chem, Tallahassee, FL 32306 USA Florida State Univ Tallahassee FL USA 32306 em, Tallahassee, FL 32306 USA Florida State Univ, Inst Mol Biophys, Tallahassee, FL 32306 USA Florida State Univ Tallahassee FL USA 32306 ys, Tallahassee, FL 32306 USA Human Genome Sci Inc, Rockville, MD 20850 USA Human Genome Sci Inc Rockville MD USA 20850 Inc, Rockville, MD 20850 USA
Titolo Testata:
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
fascicolo: 3, volume: 280, anno: 2001,
pagine: 744 - 755
SICI:
0006-291X(20010126)280:3<744:EAEAOH>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
MATRIX METALLOPROTEINASES; MELTRIN-ALPHA; CELL-ADHESION; ADAM FAMILY; PROTEIN; DOMAIN; ALPHA(2)-MACROGLOBULIN; METARGIDIN; CLONING; PEPTIDE;
Keywords:
adamalysin; metzincin; metalloproteinase/disintegrin/cysteine-rich (MDC); active enzyme; type 1a; transmembrane protein; gene expression; metalloproteinase inhibitors; alpha-2 macroglobulin;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
30
Recensione:
Indirizzi per estratti:
Indirizzo: Wei, P Florida State Univ, Dept Chem, Tallahassee, FL 32306 USA Florida State Univ Tallahassee FL USA 32306 lahassee, FL 32306 USA
Citazione:
P. Wei et al., "Expression and enzymatic activity of human disintegrin and metalloproteinase ADAM19/meltrin beta", BIOC BIOP R, 280(3), 2001, pp. 744-755

Abstract

The adamalysins are involved in proteolysis, adhesion, fusion, and intracellular signaling. Human ADAM19/adamalysin-19 (A disintegrin and metalloproteinase 19) was identified from primary dendritic cell cDNA libraries. It has a signal sequence, a prodomain with a "cysteine-switch" residue, a metallo proteinase domain with a zinc-binding site, a disintegrin, a cysteine-rich domain, an epidermal-growth-factor-like domain, a transmembrane domain, and a cytoplasmic domain with putative SH3 ligand binding sites. Its mRNA was expressed in the placenta, heart, bladder, lymph nodes, and leukocytes, colorectal ade nocarcinoma SW 480, and other organs/cells. The hADAM19 recombinant protein was expressed in human cells. It formed a complex with and cleaved alpha-a macroglobulin (alpha2-M). Its proteolytic activity was blocked by 1,10-phenanthroline, EDTA, EGTA, and a synthetic matrix metalloproteinase (MMP) inhibitor and not by the tissue inhibitors of metalloproteinasesTIMP-1 and TIMP-2. It did not cleave the MMP substrates tested, e.g., typeI collagen and gelatin, casein, and four peptide substrates. Thus, hADAM19is an active metalloproteinase and may have a specific substrate profile. (C) 2001 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/09/20 alle ore 10:22:53