Document Detail

Cellular distributions of the prohormone processing enzymes PC1 and PC2.
MedLine Citation:
PMID:  7704436     Owner:  NLM     Status:  MEDLINE    
The prohormone convertases PC1 (also known as sPC3) and PC2 are known to mediate the proteolytic conversion of inactive neuropeptide and hormone precursors to bioactive peptide products. In this study we have used sucrose density centrifugation to determine the subcellular distributions of the various forms of PC1 and PC2 in three different cell types, AtT-20, beta TC3, and PC12 cells. The former two cell lines naturally express PC enzymes, while PC12 cell clones expressing PCs were obtained by stable transfection. Our data show considerable cell-line specific variation in PC processing, with PC12 cells exhibiting the most complete processing of both enzyme precursors. While in all cell lines mature forms of both enzymes were stored within particles having the same buoyant density as secretory granule markers, in some cell lines substantial amounts of mature PC1 and PC2 were also associated with the Golgi marker. Processing of the two PC precursors was not interdependent since PC12 cells expressing only one of the two PCs were fully capable of enzyme maturation. Interestingly, analysis of intracellular processing of an endogenous peptide precursor, proneurotensin, revealed that transfected PC1, but not PC2, showed enzymatic activity against this precursor.
I Lindberg; S C Ahn; M B Breslin
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Molecular and cellular neurosciences     Volume:  5     ISSN:  1044-7431     ISO Abbreviation:  Mol. Cell. Neurosci.     Publication Date:  1994 Dec 
Date Detail:
Created Date:  1995-05-09     Completed Date:  1995-05-09     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  9100095     Medline TA:  Mol Cell Neurosci     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  614-22     Citation Subset:  IM    
Department of Biochemistry and Molecular Biology, Louisiana State University Medical Center, New Orleans 70112.
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MeSH Terms
Aspartic Acid Endopeptidases / metabolism*
Centrifugation, Density Gradient
Insulinoma / enzymology,  pathology
PC12 Cells
Proprotein Convertase 1*
Proprotein Convertase 2
Proprotein Convertases
Subcellular Fractions / metabolism*
Subtilisins / metabolism*
Tissue Distribution
Tumor Cells, Cultured
Grant Support
Reg. No./Substance:
EC 3.4.-/Proprotein Convertases; EC 3.4.21.-/Subtilisins; EC protein, mouse; EC Convertase 1; EC Convertase 2; EC 3.4.23.-/Aspartic Acid Endopeptidases

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