Intracellular lipid binding proteins of the small intestine

The small intestine contains three distinct proteins belonging to the intracellular lipid binding protein family: the liver-type fatty acid binding protein (L-FABP), the intestinal fatty acid binding protein (I-FABP) and the ileal lipid binding protein (ilbp). The function of these proteins in the s...

Full description

Saved in:
Bibliographic Details
Published in:Molecular and cellular biochemistry 2002-10, Vol.239 (1-2), p.79-82
Main Authors: Agellon, Luis B, Toth, Matthew J, Thomson, Alan B R
Format: Article
Language:English
Subjects:
Animals
Carrier Proteins - genetics
Carrier Proteins - metabolism
Dietary Fats - metabolism
Fatty Acid-Binding Protein 7
Fatty Acid-Binding Proteins
Fatty acids
Intestinal Absorption - physiology
Intestine, Small - metabolism
Lipids
Mice
Mice, Knockout
Neoplasm Proteins
Nerve Tissue Proteins
Proteins
Small intestine
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-c280t-32bc12b5444f6b16c420929bb864b97d361373fbccc631b34c11577526766edc3
cites
container_end_page 82
container_issue 1-2
container_start_page 79
container_title Molecular and cellular biochemistry
container_volume 239
creator Agellon, Luis B
Toth, Matthew J
Thomson, Alan B R
description The small intestine contains three distinct proteins belonging to the intracellular lipid binding protein family: the liver-type fatty acid binding protein (L-FABP), the intestinal fatty acid binding protein (I-FABP) and the ileal lipid binding protein (ilbp). The function of these proteins in the small intestine has remained enigmatic. Targeted gene disruption studies may shed insights into the physiological importance of these proteins. In the case of I-FABP, this approach has demonstrated that the complete elimination of this protein in murine intestine does not compromise dietary fat absorption in vivo but is associated with the development of insulin resistance.
doi_str_mv 10.1023/A:1020520521025
format article
fullrecord <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_proquest_miscellaneous_72759002</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2153373541</sourcerecordid><originalsourceid>FETCH-LOGICAL-c280t-32bc12b5444f6b16c420929bb864b97d361373fbccc631b34c11577526766edc3</originalsourceid><addsrcrecordid>eNpdkL1PwzAQxS0EoqUwsyGLgS3g82cMU1XxUakSC8xR7DjgynFKnAz897iiLEhPejf8dPfuIXQJ5BYIZXfL-2xE7JUHcYTmIBQruAZ9jOaEEVKUoNQMnaW0JQSy4BTNgHKlhYI5eljHcaitC2EK9YCD3_kGGx8bHz_wbuhH52PCfYvHT4dTV4eAfRxdGn105-ikrUNyFwdfoPenx7fVS7F5fV6vlpvC0pKMBaPGAjWCc95KA9JySjTVxpSSG60aJoEp1hprrWRgGLeQn1CCSiWlayxboJvfvTnP15RvV51P-8h1dP2UKkWV0CTXsUDX_8BtPw0xZ6uUkJQzWqoMXR2gyXSuqXaD7-rhu_rrhP0AVQZhIg</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>756243287</pqid></control><display><type>article</type><title>Intracellular lipid binding proteins of the small intestine</title><source>Springer Link</source><creator>Agellon, Luis B ; Toth, Matthew J ; Thomson, Alan B R</creator><creatorcontrib>Agellon, Luis B ; Toth, Matthew J ; Thomson, Alan B R</creatorcontrib><description>The small intestine contains three distinct proteins belonging to the intracellular lipid binding protein family: the liver-type fatty acid binding protein (L-FABP), the intestinal fatty acid binding protein (I-FABP) and the ileal lipid binding protein (ilbp). The function of these proteins in the small intestine has remained enigmatic. Targeted gene disruption studies may shed insights into the physiological importance of these proteins. In the case of I-FABP, this approach has demonstrated that the complete elimination of this protein in murine intestine does not compromise dietary fat absorption in vivo but is associated with the development of insulin resistance.</description><identifier>ISSN: 0300-8177</identifier><identifier>EISSN: 1573-4919</identifier><identifier>DOI: 10.1023/A:1020520521025</identifier><identifier>PMID: 12479571</identifier><language>eng</language><publisher>Netherlands: Springer Nature B.V</publisher><subject>Animals ; Carrier Proteins - genetics ; Carrier Proteins - metabolism ; Dietary Fats - metabolism ; Fatty Acid-Binding Protein 7 ; Fatty Acid-Binding Proteins ; Fatty acids ; Intestinal Absorption - physiology ; Intestine, Small - metabolism ; Lipids ; Mice ; Mice, Knockout ; Neoplasm Proteins ; Nerve Tissue Proteins ; Proteins ; Small intestine</subject><ispartof>Molecular and cellular biochemistry, 2002-10, Vol.239 (1-2), p.79-82</ispartof><rights>Kluwer Academic Publishers 2002</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c280t-32bc12b5444f6b16c420929bb864b97d361373fbccc631b34c11577526766edc3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12479571$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Agellon, Luis B</creatorcontrib><creatorcontrib>Toth, Matthew J</creatorcontrib><creatorcontrib>Thomson, Alan B R</creatorcontrib><title>Intracellular lipid binding proteins of the small intestine</title><title>Molecular and cellular biochemistry</title><addtitle>Mol Cell Biochem</addtitle><description>The small intestine contains three distinct proteins belonging to the intracellular lipid binding protein family: the liver-type fatty acid binding protein (L-FABP), the intestinal fatty acid binding protein (I-FABP) and the ileal lipid binding protein (ilbp). The function of these proteins in the small intestine has remained enigmatic. Targeted gene disruption studies may shed insights into the physiological importance of these proteins. In the case of I-FABP, this approach has demonstrated that the complete elimination of this protein in murine intestine does not compromise dietary fat absorption in vivo but is associated with the development of insulin resistance.</description><subject>Animals</subject><subject>Carrier Proteins - genetics</subject><subject>Carrier Proteins - metabolism</subject><subject>Dietary Fats - metabolism</subject><subject>Fatty Acid-Binding Protein 7</subject><subject>Fatty Acid-Binding Proteins</subject><subject>Fatty acids</subject><subject>Intestinal Absorption - physiology</subject><subject>Intestine, Small - metabolism</subject><subject>Lipids</subject><subject>Mice</subject><subject>Mice, Knockout</subject><subject>Neoplasm Proteins</subject><subject>Nerve Tissue Proteins</subject><subject>Proteins</subject><subject>Small intestine</subject><issn>0300-8177</issn><issn>1573-4919</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><recordid>eNpdkL1PwzAQxS0EoqUwsyGLgS3g82cMU1XxUakSC8xR7DjgynFKnAz897iiLEhPejf8dPfuIXQJ5BYIZXfL-2xE7JUHcYTmIBQruAZ9jOaEEVKUoNQMnaW0JQSy4BTNgHKlhYI5eljHcaitC2EK9YCD3_kGGx8bHz_wbuhH52PCfYvHT4dTV4eAfRxdGn105-ikrUNyFwdfoPenx7fVS7F5fV6vlpvC0pKMBaPGAjWCc95KA9JySjTVxpSSG60aJoEp1hprrWRgGLeQn1CCSiWlayxboJvfvTnP15RvV51P-8h1dP2UKkWV0CTXsUDX_8BtPw0xZ6uUkJQzWqoMXR2gyXSuqXaD7-rhu_rrhP0AVQZhIg</recordid><startdate>200210</startdate><enddate>200210</enddate><creator>Agellon, Luis B</creator><creator>Toth, Matthew J</creator><creator>Thomson, Alan B R</creator><general>Springer Nature B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>3V.</scope><scope>7QL</scope><scope>7QP</scope><scope>7T5</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>200210</creationdate><title>Intracellular lipid binding proteins of the small intestine</title><author>Agellon, Luis B ; Toth, Matthew J ; Thomson, Alan B R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c280t-32bc12b5444f6b16c420929bb864b97d361373fbccc631b34c11577526766edc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Animals</topic><topic>Carrier Proteins - genetics</topic><topic>Carrier Proteins - metabolism</topic><topic>Dietary Fats - metabolism</topic><topic>Fatty Acid-Binding Protein 7</topic><topic>Fatty Acid-Binding Proteins</topic><topic>Fatty acids</topic><topic>Intestinal Absorption - physiology</topic><topic>Intestine, Small - metabolism</topic><topic>Lipids</topic><topic>Mice</topic><topic>Mice, Knockout</topic><topic>Neoplasm Proteins</topic><topic>Nerve Tissue Proteins</topic><topic>Proteins</topic><topic>Small intestine</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Agellon, Luis B</creatorcontrib><creatorcontrib>Toth, Matthew J</creatorcontrib><creatorcontrib>Thomson, Alan B R</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium &amp; Calcified Tissue Abstracts</collection><collection>Immunology Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health &amp; Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>ProQuest Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health &amp; Medical Complete (Alumni)</collection><collection>Biological Sciences</collection><collection>Health &amp; Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular and cellular biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Agellon, Luis B</au><au>Toth, Matthew J</au><au>Thomson, Alan B R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Intracellular lipid binding proteins of the small intestine</atitle><jtitle>Molecular and cellular biochemistry</jtitle><addtitle>Mol Cell Biochem</addtitle><date>2002-10</date><risdate>2002</risdate><volume>239</volume><issue>1-2</issue><spage>79</spage><epage>82</epage><pages>79-82</pages><issn>0300-8177</issn><eissn>1573-4919</eissn><abstract>The small intestine contains three distinct proteins belonging to the intracellular lipid binding protein family: the liver-type fatty acid binding protein (L-FABP), the intestinal fatty acid binding protein (I-FABP) and the ileal lipid binding protein (ilbp). The function of these proteins in the small intestine has remained enigmatic. Targeted gene disruption studies may shed insights into the physiological importance of these proteins. In the case of I-FABP, this approach has demonstrated that the complete elimination of this protein in murine intestine does not compromise dietary fat absorption in vivo but is associated with the development of insulin resistance.</abstract><cop>Netherlands</cop><pub>Springer Nature B.V</pub><pmid>12479571</pmid><doi>10.1023/A:1020520521025</doi><tpages>4</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0300-8177
ispartof Molecular and cellular biochemistry, 2002-10, Vol.239 (1-2), p.79-82
issn 0300-8177
1573-4919
language eng
recordid cdi_proquest_miscellaneous_72759002
source Springer Link
subjects Animals
Carrier Proteins - genetics
Carrier Proteins - metabolism
Dietary Fats - metabolism
Fatty Acid-Binding Protein 7
Fatty Acid-Binding Proteins
Fatty acids
Intestinal Absorption - physiology
Intestine, Small - metabolism
Lipids
Mice
Mice, Knockout
Neoplasm Proteins
Nerve Tissue Proteins
Proteins
Small intestine
title Intracellular lipid binding proteins of the small intestine
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-26T02%3A59%3A01IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Intracellular%20lipid%20binding%20proteins%20of%20the%20small%20intestine&rft.jtitle=Molecular%20and%20cellular%20biochemistry&rft.au=Agellon,%20Luis%20B&rft.date=2002-10&rft.volume=239&rft.issue=1-2&rft.spage=79&rft.epage=82&rft.pages=79-82&rft.issn=0300-8177&rft.eissn=1573-4919&rft_id=info:doi/10.1023/A:1020520521025&rft_dat=%3Cproquest_pubme%3E2153373541%3C/proquest_pubme%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c280t-32bc12b5444f6b16c420929bb864b97d361373fbccc631b34c11577526766edc3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=756243287&rft_id=info:pmid/12479571&rfr_iscdi=true