| Processing of rat and human angiotensinogen precursors by microsomal membranes. | |
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MedLine Citation:
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PMID: 3934016 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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We have studied the processing of rat and human angiotensinogen precursors by microsomal membranes as a means of determining the number of asparagine-linked oligosaccharide units per angiotensinogen molecule, and thus the utilization of potential sites of N-glycosylation. Glycosylated, processed forms of angiotensinogen were isolated by chromatography on lentil lectin-Sepharose 4B. 35S-Methionine-labeled precursor and processed forms of angiotensinogen were compared with glycosylated and nonglycosylated 35S-methionine-labeled mature forms of angiotensinogen secreted by hepatoma cells, using immunoprecipitation, sodium dodecyl sulfate-polyacrylamide gel electrophoresis and autoradiography. N-Glycosylation of secreted angiotensinogen was inhibited using tunicamycin. For rat angiotensinogen, only 2 of 3 potential sites of N-glycosylation were utilized; in contrast, all 4 potential sites of N-glycosylation of human angiotensinogen were utilized. For neither rat or human angiotensinogen precursor was there any evidence for a prosequence. |
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Authors:
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D J Campbell; J Bouhnik; E Coezy; J Menard; P Corvol |
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Publication Detail:
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Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Molecular and cellular endocrinology Volume: 43 ISSN: 0303-7207 ISO Abbreviation: Mol. Cell. Endocrinol. Publication Date: 1985 Nov |
Date Detail:
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Created Date: 1986-01-03 Completed Date: 1986-01-03 Revised Date: 2007-11-15 |
Medline Journal Info:
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Nlm Unique ID: 7500844 Medline TA: Mol Cell Endocrinol Country: NETHERLANDS |
Other Details:
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Languages: eng Pagination: 31-40 Citation Subset: IM |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Acetylglucosaminidase Angiotensinogen / genetics* Angiotensins / genetics* Animals Cell Line Cell-Free System Humans Intracellular Membranes / enzymology* Liver Neoplasms, Experimental / enzymology* Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase Microsomes / enzymology* Microsomes, Liver / enzymology* Protein Biosynthesis* Protein Processing, Post-Translational* RNA, Messenger / genetics Rats Species Specificity |
| Chemical | |
Reg. No./Substance:
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0/Angiotensins; 0/RNA, Messenger; 11002-13-4/Angiotensinogen; EC 3.2.1.52/Acetylglucosaminidase; EC 3.2.1.96/Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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