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Titolo:
Protein kinase C regulation of intracellular and cell surface amyloid precursor protein (APP) cleavage in CHO695 cells
Autore:
Jolly-Tornetta, C; Wolf, BA;
Indirizzi:
Univ Penn, Sch Med, Dept Pathol & Lab Med, Philadelphia, PA 19104 USA UnivPenn Philadelphia PA USA 19104 & Lab Med, Philadelphia, PA 19104 USA
Titolo Testata:
BIOCHEMISTRY
fascicolo: 49, volume: 39, anno: 2000,
pagine: 15282 - 15290
SICI:
0006-2960(200012)39:49<15282:PKCROI>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
FAMILIAL ALZHEIMERS-DISEASE; ALPHA-SECRETASE CLEAVAGE; TRANS-GOLGI NETWORK; GROWTH-FACTOR-ALPHA; BETA-PROTEIN; ENDOPLASMIC-RETICULUM; BREFELDIN-A; HUMAN NEURONS; NT2N CELLS; RELEASE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
61
Recensione:
Indirizzi per estratti:
Indirizzo: Wolf, BA Univ Penn, Sch Med, Dept Pathol & Lab Med, 230 John Morgan Bldg,3620 Hamilton Walk, Philadelphia, PA 19104 USA Univ Penn 230 John Morgan Bldg,3620 Hamilton Walk Philadelphia PA USA 19104
Citazione:
C. Jolly-Tornetta e B.A. Wolf, "Protein kinase C regulation of intracellular and cell surface amyloid precursor protein (APP) cleavage in CHO695 cells", BIOCHEM, 39(49), 2000, pp. 15282-15290

Abstract

Cleavage of amyloid precursor protein (APP) by beta -secretase generates beta -amyloid (A beta), the major component of senile plaques in Alzheimer'sdisease. Cleavage of APP by alpha -secretase prevents A beta formation, producing nonamyloidogenic secreted APPs products. PKC-regulated API, alpha -secretase cleavage has been shown to involve tumor necrosis factor alpha (TNF-alpha) converting enzyme (TACE). To determine the location of APP cleavage, we examined PKC-regulated APPs secretion by examining cell surface versus intracellular APP in CHO cells stably expressing APP(695) (CH0695). We demonstrate that PKC regulates cell surface and intracellular APP cleavage. The majority of secreted APPs originates from the intracellular compartment, and PKC does not cause an increase in APP trafficking to the cell surfacefor cleavage. Therefore, intracellular APP regulated by PKC must be cleaved at an intracellular site. Experiments utilizing Brefeldin A suggest APP cleavage occurs at the Golgi or late in the secretory pathway. Experiments using TAPI, an inhibitor of TACE, demonstrate PKC-regulated APPs secretion from the cell surface is inhibited after pretreatment with TAPI, and APPs secretion from the intracellular pool is partially inhibited after pretreatment with TAPI. These findings suggest PKC-regulated APP cleavage occurs at multiple locations within the cell and both events appear to involve TACE.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/03/20 alle ore 13:11:39