Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
PROTEOLYTIC RELEASE OF MEMBRANE-PROTEINS - STUDIES ON A MEMBRANE-PROTEIN-SOLUBILIZING ACTIVITY IN CHO CELLS
Autore:
EHLERS MRW; SCHWAGER SLU; CHUBB AJ; SCHOLLE RR; BRANDT WF; RIORDAN JF;
Indirizzi:
UNIV CAPE TOWN,SCH MED,DEPT BIOCHEM MED ZA-7925 OBSERVATORY SOUTH AFRICA UNIV CAPE TOWN,DEPT BIOCHEM ZA-7700 RONDEBOSCH SOUTH AFRICA HARVARD UNIV,SCH MED,CTR BIOCHEM & BIOPHYS SCI & MED BOSTON MA 02115
Titolo Testata:
Immunopharmacology
fascicolo: 2-3, volume: 36, anno: 1997,
pagine: 271 - 278
SICI:
0162-3109(1997)36:2-3<271:PROM-S>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
ANGIOTENSIN-CONVERTING ENZYME; AMYLOID PRECURSOR PROTEIN; HAMSTER OVARY CELLS; GROWTH-FACTOR-ALPHA; CLEAVAGE SITE; PROXIMAL CLEAVAGE; L-SELECTIN; RECEPTOR; IDENTIFICATION; PEPTIDE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
23
Recensione:
Indirizzi per estratti:
Citazione:
M.R.W. Ehlers et al., "PROTEOLYTIC RELEASE OF MEMBRANE-PROTEINS - STUDIES ON A MEMBRANE-PROTEIN-SOLUBILIZING ACTIVITY IN CHO CELLS", Immunopharmacology, 36(2-3), 1997, pp. 271-278

Abstract

Diverse membrane proteins are solubilized by a specific proteolytic cleavage in the stalk sequence adjacent to the membrane anchor, with release of the extracellular domain. Examples are the amyloid precursor protein, membrane-bound growth factors and angiotensin-converting enzyme (ACE). The identities and characteristics of the responsible proteases remain elusive. We have studied this process in Chinese hamster ovary (CHO) cells stably expressing wild-type ACE (WT-ACE) or juxtamembrane (stalk) deletion or chimaera mutants. Determination of the C termini (i.e. the cleavage sites) of released, soluble wild-type and mutantACE by MALDI-TOF mass spectrometry indicated that the membrane-protein-solubilizing protease (MPSP) in CHO cells is not constrained by a particular cleavage site motif or by a specific distance from the membrane, but instead may position itself with respect to the putative proximal, folded extracellular domain adjacent to the stalk. Nevertheless, kinetic analyses of release rates indicated that a minimum distance from the membrane must be preserved. Interestingly, soluble full-length (anchor-plus) WT-ACE incubated with fractions of, or intact, CHO cellswas not cleaved. In all cases, release was stimulated by a media change or by the addition of phorbol ester, with rate enhancements of 5- and 50-fold, respectively, for WT-ACE. The phorbol ester effect was abolished by staurosporine, a protein kinase C (PKC) inhibitor. We propose that the CHO cell MPSP that solubilizes ACE: (1) only cleaves proteins embedded in a membrane; (2) requires an accessible stalk and cleaves at a minimum distance from both the membrane and proximal extracellular domain; (3) positions itself primarily with respect to the proximal extracellular domain and (4) is regulated in part by a PKC-dependentmechanism.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 21/09/20 alle ore 06:21:13