| Cellular distributions of the prohormone processing enzymes PC1 and PC2. | |
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MedLine Citation:
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PMID: 7704436 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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I Lindberg; S C Ahn; M B Breslin |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: Molecular and cellular neurosciences Volume: 5 ISSN: 1044-7431 ISO Abbreviation: Mol. Cell. Neurosci. Publication Date: 1994 Dec |
Date Detail:
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Created Date: 1995-05-09 Completed Date: 1995-05-09 Revised Date: 2009-11-19 |
Medline Journal Info:
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Nlm Unique ID: 9100095 Medline TA: Mol Cell Neurosci Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 614-22 Citation Subset: IM |
Affiliation:
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Department of Biochemistry and Molecular Biology, Louisiana State University Medical Center, New Orleans 70112. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Aspartic Acid Endopeptidases / metabolism* Centrifugation, Density Gradient Insulinoma / enzymology, pathology Mice PC12 Cells Proprotein Convertase 1* Proprotein Convertase 2 Proprotein Convertases Rats Subcellular Fractions / metabolism* Subtilisins / metabolism* Tissue Distribution Tumor Cells, Cultured |
| Grant Support | |
ID/Acronym/Agency:
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NIDA 05084/DA/NIDA NIH HHS |
| Chemical | |
Reg. No./Substance:
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EC 3.4.-/Proprotein Convertases; EC 3.4.21.-/Subtilisins; EC 3.4.21.93/Pcsk1 protein, mouse; EC 3.4.21.93/Proprotein Convertase 1; EC 3.4.21.94/Proprotein Convertase 2; EC 3.4.23.-/Aspartic Acid Endopeptidases |
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