| Role of lysophosphatidylcholine in brush-border intestinal alkaline phosphatase release and restoration. | |
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MedLine Citation:
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PMID: 19407215 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Intestinal alkaline phosphatase (IAP) is a brush-border membrane ectoenzyme (BBM-IAP) that is released into the lumen (L-IAP) after a high-fat diet. We examined the effects of oil feeding and the addition of mixed-lipid micelles on the formation of L-IAP in oil-fed rat intestine, Caco-2 cell monolayers, and mouse intestinal loops. We localized IAP in the duodenum of rats fed corn oil using fluorescence microscopy with enzyme-labeled fluorescence-97 as substrate. Four hours after oil feeding, L-IAP increased approximately 10-fold accompanied by the loss of BBM-IAP, consistent with BBM-IAP release. Rat IAP isozyme mRNAs progressively increased 4-6 h after oil feeding, followed by the increase of IAP activity in the subapical location at 6 h, consistent with the restoration of IAP protein. Postprandial lipid-micelle components, sodium taurocholate with or without oleic acid, mono-oleylglycerol, cholesterol, or lysophosphatidylcholine (lysoPC) were applied singly or as mixed-lipid micelles to the apical surface of polarized Caco-2 cell monolayers. LysoPC increased L-IAP >10-fold over basal release. LysoPC released IAP into the apical medium more than other intestinal brush-border enzymes, 5'-nucleotidase, sucrase, aminopeptidase N, and lactase, without comparable lactate dehydrogenase release or cell injury. LysoPC increased human IAP mRNA levels by 1.5-fold in Caco-2 cells. Luminally applied lysoPC also increased release of IAP preferentially in mouse intestinal loops. These data show that lysoPC accelerates the formation of L-IAP from BBM-IAP, followed by enhanced IAP synthesis, suggesting the role that lysoPC might play in the turnover of brush-border proteins. |
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Authors:
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Takanari Nakano; Ikuo Inoue; David H Alpers; Yasutada Akiba; Shigehiro Katayama; Rina Shinozaki; Jonathan D Kaunitz; Susumu Ohshima; Masumi Akita; Seiichiro Takahashi; Iwao Koyama; Makoto Matsushita; Tsugikazu Komoda |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't Date: 2009-04-30 |
Journal Detail:
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Title: American journal of physiology. Gastrointestinal and liver physiology Volume: 297 ISSN: 1522-1547 ISO Abbreviation: Am. J. Physiol. Gastrointest. Liver Physiol. Publication Date: 2009 Jul |
Date Detail:
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Created Date: 2009-06-29 Completed Date: 2009-08-04 Revised Date: 2011-02-21 |
Medline Journal Info:
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Nlm Unique ID: 100901227 Medline TA: Am J Physiol Gastrointest Liver Physiol Country: United States |
Other Details:
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Languages: eng Pagination: G207-14 Citation Subset: IM |
Affiliation:
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Department of Biochemistry, Biomedical Research Center, Saitama Medical University, Saitama, Japan. nk.takanari@gmail.com |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Alkaline Phosphatase
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genetics,
metabolism* Animals Antigens, Neoplasm / metabolism Caco-2 Cells Corn Oil / administration & dosage* Duodenum / enzymology Epithelial Cells / enzymology GPI-Linked Proteins Humans Intestines / enzymology* Isoenzymes Lysophosphatidylcholines / metabolism* Male Mice Mice, Inbred C57BL Micelles Microvilli / enzymology Postprandial Period Protein Transport RNA, Messenger / metabolism Rats Rats, Wistar Time Factors |
| Grant Support | |
ID/Acronym/Agency:
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DK56341/DK/NIDDK NIH HHS; P30 DK056341-08/DK/NIDDK NIH HHS; R01 DK54221/DK/NIDDK NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Antigens, Neoplasm; 0/GPI-Linked Proteins; 0/Isoenzymes; 0/Lysophosphatidylcholines; 0/Micelles; 0/RNA, Messenger; 8001-30-7/Corn Oil; EC 3.1.3.1/ALPI protein, human; EC 3.1.3.1/Alkaline Phosphatase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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