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Titolo:
Regulation of membrane metalloproteolytic cleavage of L-selectin (CD62L) by the epidermal growth factor domain
Autore:
Zhao, LC; Shey, M; Farnsworth, M; Dailey, MO;
Indirizzi:
Univ Iowa, Coll Med, Dept Pathol, Iowa City, IA 52242 USA Univ Iowa Iowa City IA USA 52242 ed, Dept Pathol, Iowa City, IA 52242 USA Univ Iowa, Coll Med, Dept Microbiol, Iowa City, IA 52242 USA Univ Iowa Iowa City IA USA 52242 Dept Microbiol, Iowa City, IA 52242 USA Univ Iowa, Coll Med, Interdisciplinary Grad Program, Iowa City, IA 52242 USA Univ Iowa Iowa City IA USA 52242 ry Grad Program, Iowa City, IA 52242 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 33, volume: 276, anno: 2001,
pagine: 30631 - 30640
SICI:
0021-9258(20010817)276:33<30631:ROMMCO>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
NECROSIS-FACTOR-ALPHA; AMYLOID PRECURSOR PROTEIN; NODE HOMING RECEPTOR; CONVERTING ENZYME SECRETASE; CELL-SURFACE; TNF RECEPTOR; HUMAN NEUTROPHILS; KINASE-C; DISINTEGRIN-METALLOPROTEASE; STRUCTURAL REQUIREMENTS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
83
Recensione:
Indirizzi per estratti:
Indirizzo: Dailey, MO Univ Iowa, Coll Med, Dept Pathol, Iowa City, IA 52242 USA Univ Iowa Iowa City IA USA 52242 thol, Iowa City, IA 52242 USA
Citazione:
L.C. Zhao et al., "Regulation of membrane metalloproteolytic cleavage of L-selectin (CD62L) by the epidermal growth factor domain", J BIOL CHEM, 276(33), 2001, pp. 30631-30640

Abstract

The adhesion molecule L-selectin is cleaved rapidly from the surface of activated leukocytes by tumor necrosis factor-a converting enzyme, a cell surface metalloprotease, and also undergoes slower constitutive shedding in unactivated cells. The structural features that render it susceptible to shedding are poorly understood. We therefore analyzed the shedding of a series of mutant and chimeric L-selectin molecules. Although murine L-selectin is cleaved at a specific location in the juxtamembrane region 11 amino acids distal to the cell membrane, this cleavage has little sequence specificity. However, proline substitution at the P2 ' or P3 ' position or deletion of the epidermal growth factor (EGF) domain completely blocks the rapid phorbolester-induced cleavage, but does not affect the slower basal proteolytic shedding. Insertion of the 15-residue membrane-proximal region (MPR) of L-selectin into the heterologous protein B7.2 results in a molecule that undergoes constitutive proteolytic turnover. In contrast, insertion of both the EGF domain and the MPR confers susceptibility to both slow constitutive shedding and the rapid proteolytic cleavage induced by phorbol 12-myristate 13-acetate. These results demonstrate that constitutive and induced L-selectincleavage are separable processes and that the rapid phorbol ester-induced shedding requires the presence of the EGF domain, a sequence that is remotefrom the cleavage site.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/09/20 alle ore 09:03:00