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Titolo:
EVIDENCE AGAINST A ROLE FOR THE KUNITZ DOMAIN IN AMYLOIDOGENIC AND SECRETORY PROCESSING OF THE AMYLOID PRECURSOR PROTEIN
Autore:
LADROR US; KOHNKEN RE; WANG GT; MANELLI AM; FRAIL DE; KLEIN WL; HOLZMAN TF; KRAFFT GA;
Indirizzi:
ABBOTT LABS,DIV PHARMACEUT PROD,D-46Y,AP-10 ABBOTT PK IL 60064 ABBOTT LABS,DIV PHARMACEUT PROD ABBOTT PK IL 60064 NORTHWESTERN UNIV,DEPT NEUROBIOL EVANSTON IL 00000
Titolo Testata:
Journal of neurochemistry
fascicolo: 6, volume: 63, anno: 1994,
pagine: 2225 - 2230
SICI:
0022-3042(1994)63:6<2225:EAARFT>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
ALZHEIMERS-DISEASE; MESSENGER-RNA; BETA-PROTEIN; HUMAN-BRAIN; SOLUBLE DERIVATIVES; MAMMALIAN-CELLS; CLEAVAGE SITE; ALPHA-1-ANTICHYMOTRYPSIN; DEPOSITS; PEPTIDE;
Keywords:
BETA-AMYLOID PRECURSOR PROTEIN; KUNITZ PROTEINASE INHIBITOR; ALZHEIMERS DISEASE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
38
Recensione:
Indirizzi per estratti:
Citazione:
U.S. Ladror et al., "EVIDENCE AGAINST A ROLE FOR THE KUNITZ DOMAIN IN AMYLOIDOGENIC AND SECRETORY PROCESSING OF THE AMYLOID PRECURSOR PROTEIN", Journal of neurochemistry, 63(6), 1994, pp. 2225-2230

Abstract

The effect of the Kunitz proteinase inhibitor (KPI) on potential beta-amyloid precursor protein (beta PP)-processing activities from control and Alzheimer's disease (AD) brains was examined using fluorogenic substrates designed to mimic the secretory and amyloidogenic cleavages in beta PP. In addition, the level of secretion of KPI-containing betaPP751 and KPI-lacking beta PP695 from transfected cells was examined to assess the effect of the KPI on beta PP secretion. beta PP751 and beta PP695, obtained from conditioned media of transfected cells, had no effect on proteinase activities against the secretory and amyloidogenic substrates in extracts from control and AD brains. At similar concentrations beta PP751, but not beta PP695, completely inhibited the activity of trypsin against these substrates. Serine proteinase inhibitors had only modest effects on activities from brain, whereas cysteine modification completely inhibited them, indicating that these proteinase activities were not of the serine type. Thus, the results do not support a role for the KPI in the secretion of beta PP or in the amyloidogenic cleavage of beta PP. The amounts of beta PP695 and beta PP751 collected from the media of transfected cells after 48 h of growth weresimilar, indicating an equal rate of secretion. This result suggests that the KPI domain in beta PP751 did not inhibit the secretory cleavage in transfected cells.

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Documento generato il 01/12/20 alle ore 07:24:06