Document Detail


Proprotein convertase activity contributes to the processing of the Alzheimer's beta-amyloid precursor protein in human cells: evidence for a role of the prohormone convertase PC7 in the constitutive alpha-secretase pathway.
MedLine Citation:
PMID:  10537065     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The physiological maturation of the beta-amyloid precursor protein (betaAPP) leads to the secretion of a fragment termed APPalpha, after cleavage by a proteolytic enzyme called-secretase. In Alzheimer's disease, betaAPP undergoes exacerbated proteolytic attacks by beta- and gamma-secretases, which liberate a readily aggregatable 40-42-amino acid peptide called AP. We show here that overexpression of the prohormone convertase PC7 triggers increased secretion of APPalpha and lowers both Abeta40 and Abeta42 recoveries. Overexpression of alpha1-antitrypsin Portland (alpha1-PDX), which blocks mammalian precursor convertases of the constitutive secretory pathway, reverses the PC7-induced APPalpha increase as well as the decrease of Abeta40/42 in HEK293 cells. It is interesting that alpha1-PDX also lowers the level of APPalpha endogenously produced by mock-transfected HEK293 cells. Finally, a Jurkat clone stably expressing alpha1-PDX produces noticeably lower amounts of APPalpha. Therefore, this serpin affects endogenous a-secretase activity/pathway in distinct cell types. By contrast, alpha1-PDX does not alter the processing of presenilin 1 or its mutated congeners linked to some familial forms of Alzheimer's disease. Altogether, we demonstrate that a prohormone convertase participates in the alpha-secretase pathway of betaAPP maturation in human cells and concomitantly contributes to slowing the pathogenic route leading to the formation of Abeta. Our data strongly suggest that PC7 could fulfill such a role.
Authors:
E Lopez-Perez; N G Seidah; F Checler
Related Documents :
18924105 - Proteomic analysis of conditioned media from glucose responsive and glucose non-respons...
3697345 - Porphyrin-induced photodamage to isolated epidermal cells from hairless mice.
8452925 - Isolation of ovine luteal cell subpopulations by flow cytometry.
1330935 - Transforming growth factor beta 1 (tgf-beta 1) inhibits growth of a human ovarian carci...
2707955 - Gonadoblastoma. immunohistochemical and ultrastructural observations.
6539665 - An ultra-pure in vitro phase synchrony method employing centrifugal elutriation and via...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of neurochemistry     Volume:  73     ISSN:  0022-3042     ISO Abbreviation:  J. Neurochem.     Publication Date:  1999 Nov 
Date Detail:
Created Date:  1999-11-05     Completed Date:  1999-11-05     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  2985190R     Medline TA:  J Neurochem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  2056-62     Citation Subset:  IM    
Affiliation:
IPMC du CNRS, UPR 411, Sophia Antipolis, Valbonne, France.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Alzheimer Disease / metabolism*
Amyloid Precursor Protein Secretases
Amyloid beta-Protein / metabolism
Amyloid beta-Protein Precursor / metabolism*
Animals
Aspartic Acid Endopeptidases
Cell Line
Endopeptidases / metabolism*
Enzyme Inhibitors / pharmacology
Furin
Gene Deletion
Gene Expression
Humans
Jurkat Cells
Kinetics
Membrane Proteins / genetics
Mutation
Peptide Fragments / metabolism
Presenilin-1
Rats
Subtilisins / antagonists & inhibitors,  genetics,  metabolism*
Transfection
alpha 1-Antitrypsin / genetics,  pharmacology
Chemical
Reg. No./Substance:
0/Amyloid beta-Protein; 0/Amyloid beta-Protein Precursor; 0/Enzyme Inhibitors; 0/Membrane Proteins; 0/PSEN1 protein, human; 0/Peptide Fragments; 0/Presenilin-1; 0/alpha 1-Antitrypsin; 0/alpha 1-antitrypsin Portland; EC 3.4.-/Amyloid Precursor Protein Secretases; EC 3.4.-/Endopeptidases; EC 3.4.21.-/Subtilisins; EC 3.4.21.75/Furin; EC 3.4.23.-/Aspartic Acid Endopeptidases; EC 3.4.23.46/BACE1 protein, human

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Kinetic modeling of 52Fe/52mMn-citrate at the blood-brain barrier by positron emission tomography.
Next Document:  Effects of aging on the interaction between glutamate, dopamine, and GABA in striatum and nucleus ac...