| Structure, glycosylation, and localization of rat intestinal guanylyl cyclase C: modulation by fasting. | |
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MedLine Citation:
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PMID: 8997239 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Guanylyl cyclase C (GC-C), an intestinal receptor guanylyl cyclase, binds diarrhea-producing bacterial ligands such as the Escherichia coli heat stable enterotoxin. We examined the regulatory influence of feeding and fasting on the expression, structure, and biochemical properties of GC-C. When solubilized at 4 degrees C under nonreducing conditions, GC-C from both fed and fasted rats migrated on 7% sodium dodecyl sulfate-polyacrylamide electrophoretic gels as two extremely large aggregates that barely penetrated the stacking and resolving gels. Chemical reduction of disulfide linkages disaggregated GC-C in fed but not fasted rat samples, causing it to migrate as smaller forms (approximately 220 and 240 kDa). Although GC-C aggregates from fasted rats resisted this disaggregating effect of chemical reduction, they rapidly acquired it within 90 min of refeeding. When solubilized at denaturing temperatures (95 degrees C) under reducing conditions, GC-C aggregates largely disassembled into four smaller proteins (relative molecular weight approximately 140,000, 131,000, 85,000, and 65,000). However, the 131-kDa glycoprotein was disproportionately increased in fasted rat membranes. This unit and the 220-kDa unit were sensitive to endoglycosidase H. Subcellular fractionation and immunohistochemical studies revealed a major redistribution of GC-C from surface to intracellular enterocyte sites during fasting. |
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Authors:
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L A Scheving; W E Russell; K M Chong |
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Publication Detail:
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Type: Journal Article; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: The American journal of physiology Volume: 271 ISSN: 0002-9513 ISO Abbreviation: Am. J. Physiol. Publication Date: 1996 Dec |
Date Detail:
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Created Date: 1997-02-12 Completed Date: 1997-02-12 Revised Date: 2007-11-14 |
Medline Journal Info:
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Nlm Unique ID: 0370511 Medline TA: Am J Physiol Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: G959-68 Citation Subset: IM |
Affiliation:
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Department of Pathology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-2576, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Fasting Glycosylation Guanylate Cyclase / analysis, genetics, metabolism* Immunohistochemistry Intestines / enzymology* Male Rats Rats, Sprague-Dawley Receptors, Peptide / analysis, genetics, metabolism* |
| Grant Support | |
ID/Acronym/Agency:
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DK-26657-15/DK/NIDDK NIH HHS; DK-44557/DK/NIDDK NIH HHS; DK-45925/DK/NIDDK NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Receptors, Peptide; EC 4.6.1.2/Guanylate Cyclase; EC 4.6.1.2/enterotoxin receptor |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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