Expression and Regulation of mRNA for Putative Fatty Acid Transport Related Proteins and Fatty Acyl CoA Synthase in Murine Epidermis and Cultured Human Keratinocytes
The epidermis has a requirement for fatty acids in order to synthesize cellular membranes and the extracellular lipid lamellar membranes in the stratum corneum. Despite high endogenous production of fatty acids the transport of exogenous essential fatty acids into the epidermis is an absolute requir...
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Veröffentlicht in: | Journal of investigative dermatology 1998-11, Vol.111 (5), p.722-726 |
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description | The epidermis has a requirement for fatty acids in order to synthesize cellular membranes and the extracellular lipid lamellar membranes in the stratum corneum. Despite high endogenous production of fatty acids the transport of exogenous essential fatty acids into the epidermis is an absolute requirement. Fatty acid uptake by keratinocytes has been shown to be mediated by a transport system. In this study we determined in murine epidermis and human cultured keratinocytes the expression of three putative fatty acid transport related proteins and fatty acyl CoA synthase, an enzyme that facilitates the uptake of fatty acids by promoting their metabolism. In cultured human keratinocytes, mRNA for fatty acid transport protein (FATP), plasma membrane fatty acid binding protein (FABP-pm), and fatty acyl CoA synthase (FACS) were detectable. Differentiation, induced by high calcium, did not affect FATP mRNA levels, but resulted in an ≈50% increase in FACS mRNA, while decreasing FABP-pm mRNA by 50%. Fatty acid translocase (FAT) mRNA was not detected in cultured human keratinocytes. In murine epidermis, FATP, FABP-pm, FACS, and FAT mRNA were all present. Barrier disruption by either tape stripping or acetone treatment increased FAT mRNA levels by ≈2-fold without affecting FATP, FABP-pm, or FACS. Occlusion with an impermeable membrane immediately after barrier disruption completely blocked the increase in FAT mRNA levels, indicating that this increase is related to barrier disruption rather than a nonspecific injury effect. In summary, this study demonstrates that several putative fatty acid transport related proteins as well as fatty acyl CoA synthase are expressed in keratinocytes and epidermis, and that the expression of these proteins may be regulated by differentiation and/or barrier disruption. |
doi_str_mv | 10.1046/j.1523-1747.1998.00383.x |
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Despite high endogenous production of fatty acids the transport of exogenous essential fatty acids into the epidermis is an absolute requirement. Fatty acid uptake by keratinocytes has been shown to be mediated by a transport system. In this study we determined in murine epidermis and human cultured keratinocytes the expression of three putative fatty acid transport related proteins and fatty acyl CoA synthase, an enzyme that facilitates the uptake of fatty acids by promoting their metabolism. In cultured human keratinocytes, mRNA for fatty acid transport protein (FATP), plasma membrane fatty acid binding protein (FABP-pm), and fatty acyl CoA synthase (FACS) were detectable. Differentiation, induced by high calcium, did not affect FATP mRNA levels, but resulted in an ≈50% increase in FACS mRNA, while decreasing FABP-pm mRNA by 50%. Fatty acid translocase (FAT) mRNA was not detected in cultured human keratinocytes. In murine epidermis, FATP, FABP-pm, FACS, and FAT mRNA were all present. Barrier disruption by either tape stripping or acetone treatment increased FAT mRNA levels by ≈2-fold without affecting FATP, FABP-pm, or FACS. Occlusion with an impermeable membrane immediately after barrier disruption completely blocked the increase in FAT mRNA levels, indicating that this increase is related to barrier disruption rather than a nonspecific injury effect. In summary, this study demonstrates that several putative fatty acid transport related proteins as well as fatty acyl CoA synthase are expressed in keratinocytes and epidermis, and that the expression of these proteins may be regulated by differentiation and/or barrier disruption.</description><identifier>ISSN: 0022-202X</identifier><identifier>EISSN: 1523-1747</identifier><identifier>DOI: 10.1046/j.1523-1747.1998.00383.x</identifier><identifier>PMID: 9804328</identifier><identifier>CODEN: JIDEAE</identifier><language>eng</language><publisher>Danvers, MA: Elsevier Inc</publisher><subject>Animals ; Biological and medical sciences ; Carrier Proteins - genetics ; CD36 ; CD36 Antigens ; Cell Differentiation ; Cell Membrane Permeability ; Cells, Cultured ; Coenzyme A Ligases - genetics ; FABP-pm ; FAT ; FATP ; Fatty Acid Transport Proteins ; fatty acid uptake ; Fundamental and applied biological sciences. Psychology ; Humans ; Keratinocytes - chemistry ; Keratinocytes - cytology ; Keratinocytes - metabolism ; Male ; Membrane Glycoproteins - metabolism ; Membrane Proteins - genetics ; Membrane Transport Proteins ; Mice ; Mice, Hairless ; Organic Anion Transporters ; Repressor Proteins ; RNA, Messenger - metabolism ; Saccharomyces cerevisiae Proteins ; Skin - cytology ; Skin - metabolism ; Vertebrates: skin, associated glands, phaneres, light organs, various exocrine glands (salt gland, uropygial gland...), adipose tissue, connective tissue</subject><ispartof>Journal of investigative dermatology, 1998-11, Vol.111 (5), p.722-726</ispartof><rights>1998 The Society for Investigative Dermatology, Inc</rights><rights>1999 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c536t-7acd2b154fd7f1bb5fb160a1c43e2f7f86089709063b35f66ea7ef6faf32b0383</citedby><cites>FETCH-LOGICAL-c536t-7acd2b154fd7f1bb5fb160a1c43e2f7f86089709063b35f66ea7ef6faf32b0383</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27922,27923</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1592281$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9804328$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Harris, Ian R.</creatorcontrib><creatorcontrib>Farrell, Angela M.</creatorcontrib><creatorcontrib>Memon, Riaz A.</creatorcontrib><creatorcontrib>Grunfeld, Carl</creatorcontrib><creatorcontrib>Elias, Peter M.</creatorcontrib><creatorcontrib>Feingold, Kenneth R.</creatorcontrib><title>Expression and Regulation of mRNA for Putative Fatty Acid Transport Related Proteins and Fatty Acyl CoA Synthase in Murine Epidermis and Cultured Human Keratinocytes</title><title>Journal of investigative dermatology</title><addtitle>J Invest Dermatol</addtitle><description>The epidermis has a requirement for fatty acids in order to synthesize cellular membranes and the extracellular lipid lamellar membranes in the stratum corneum. Despite high endogenous production of fatty acids the transport of exogenous essential fatty acids into the epidermis is an absolute requirement. Fatty acid uptake by keratinocytes has been shown to be mediated by a transport system. In this study we determined in murine epidermis and human cultured keratinocytes the expression of three putative fatty acid transport related proteins and fatty acyl CoA synthase, an enzyme that facilitates the uptake of fatty acids by promoting their metabolism. In cultured human keratinocytes, mRNA for fatty acid transport protein (FATP), plasma membrane fatty acid binding protein (FABP-pm), and fatty acyl CoA synthase (FACS) were detectable. Differentiation, induced by high calcium, did not affect FATP mRNA levels, but resulted in an ≈50% increase in FACS mRNA, while decreasing FABP-pm mRNA by 50%. Fatty acid translocase (FAT) mRNA was not detected in cultured human keratinocytes. In murine epidermis, FATP, FABP-pm, FACS, and FAT mRNA were all present. Barrier disruption by either tape stripping or acetone treatment increased FAT mRNA levels by ≈2-fold without affecting FATP, FABP-pm, or FACS. Occlusion with an impermeable membrane immediately after barrier disruption completely blocked the increase in FAT mRNA levels, indicating that this increase is related to barrier disruption rather than a nonspecific injury effect. In summary, this study demonstrates that several putative fatty acid transport related proteins as well as fatty acyl CoA synthase are expressed in keratinocytes and epidermis, and that the expression of these proteins may be regulated by differentiation and/or barrier disruption.</description><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Carrier Proteins - genetics</subject><subject>CD36</subject><subject>CD36 Antigens</subject><subject>Cell Differentiation</subject><subject>Cell Membrane Permeability</subject><subject>Cells, Cultured</subject><subject>Coenzyme A Ligases - genetics</subject><subject>FABP-pm</subject><subject>FAT</subject><subject>FATP</subject><subject>Fatty Acid Transport Proteins</subject><subject>fatty acid uptake</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humans</subject><subject>Keratinocytes - chemistry</subject><subject>Keratinocytes - cytology</subject><subject>Keratinocytes - metabolism</subject><subject>Male</subject><subject>Membrane Glycoproteins - metabolism</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Transport Proteins</subject><subject>Mice</subject><subject>Mice, Hairless</subject><subject>Organic Anion Transporters</subject><subject>Repressor Proteins</subject><subject>RNA, Messenger - metabolism</subject><subject>Saccharomyces cerevisiae Proteins</subject><subject>Skin - cytology</subject><subject>Skin - metabolism</subject><subject>Vertebrates: skin, associated glands, phaneres, light organs, various exocrine glands (salt gland, uropygial gland...), adipose tissue, connective tissue</subject><issn>0022-202X</issn><issn>1523-1747</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUctu1DAUtRCoDIVPQPICsUuwnfdyGE1pRYGqFImd5TjX4FFiB9upJh_Ef9bpDNMlK-v6PO7VOQhhSlJK8vLDLqUFyxJa5VVKm6ZOCcnqLN0_Q6sT8BytCGEsYYT9fIleeb8jhJZ5UZ-hs6YmecbqFfq73Y8OvNfWYGE6fAu_pl6EZbQKD7df11hZh2-mED_vAV-IEGa8lrrDd04YP1oXoihKoMM3zgbQxj86_WPOPd7YNf4-m_BbeMDa4C-T0wbwdtQduEEf-JupD5OLLpfTIAz-DC5uNFbOAfxr9EKJ3sOb43uOflxs7zaXyfW3T1eb9XUii6wMSSVkx1pa5KqrFG3bQrW0JILKPAOmKlWXpG4q0pAya7NClSWIClSphMpYuwR4jt4ffEdn_0zgA4_XSeh7YcBOnlcx0JwSFon1gSid9d6B4qPTg3Azp4QvDfEdX4rgSxF8aYg_NsT3Ufr2uGNqB-hOwmMlEX93xIWXolcxZan9k3_RMFbTJxsjlthOeFEuLS82Hw84xLzuNTjupQYjodMOZOCd1f-_9QHd3ruU</recordid><startdate>19981101</startdate><enddate>19981101</enddate><creator>Harris, Ian R.</creator><creator>Farrell, Angela M.</creator><creator>Memon, Riaz A.</creator><creator>Grunfeld, Carl</creator><creator>Elias, Peter M.</creator><creator>Feingold, Kenneth R.</creator><general>Elsevier Inc</general><general>Nature Publishing</general><scope>6I.</scope><scope>AAFTH</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19981101</creationdate><title>Expression and Regulation of mRNA for Putative Fatty Acid Transport Related Proteins and Fatty Acyl CoA Synthase in Murine Epidermis and Cultured Human Keratinocytes</title><author>Harris, Ian R. ; Farrell, Angela M. ; Memon, Riaz A. ; Grunfeld, Carl ; Elias, Peter M. ; Feingold, Kenneth R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c536t-7acd2b154fd7f1bb5fb160a1c43e2f7f86089709063b35f66ea7ef6faf32b0383</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Carrier Proteins - genetics</topic><topic>CD36</topic><topic>CD36 Antigens</topic><topic>Cell Differentiation</topic><topic>Cell Membrane Permeability</topic><topic>Cells, Cultured</topic><topic>Coenzyme A Ligases - genetics</topic><topic>FABP-pm</topic><topic>FAT</topic><topic>FATP</topic><topic>Fatty Acid Transport Proteins</topic><topic>fatty acid uptake</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Humans</topic><topic>Keratinocytes - chemistry</topic><topic>Keratinocytes - cytology</topic><topic>Keratinocytes - metabolism</topic><topic>Male</topic><topic>Membrane Glycoproteins - metabolism</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Transport Proteins</topic><topic>Mice</topic><topic>Mice, Hairless</topic><topic>Organic Anion Transporters</topic><topic>Repressor Proteins</topic><topic>RNA, Messenger - metabolism</topic><topic>Saccharomyces cerevisiae Proteins</topic><topic>Skin - cytology</topic><topic>Skin - metabolism</topic><topic>Vertebrates: skin, associated glands, phaneres, light organs, various exocrine glands (salt gland, uropygial gland...), adipose tissue, connective tissue</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Harris, Ian R.</creatorcontrib><creatorcontrib>Farrell, Angela M.</creatorcontrib><creatorcontrib>Memon, Riaz A.</creatorcontrib><creatorcontrib>Grunfeld, Carl</creatorcontrib><creatorcontrib>Elias, Peter M.</creatorcontrib><creatorcontrib>Feingold, Kenneth R.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of investigative dermatology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Harris, Ian R.</au><au>Farrell, Angela M.</au><au>Memon, Riaz A.</au><au>Grunfeld, Carl</au><au>Elias, Peter M.</au><au>Feingold, Kenneth R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Expression and Regulation of mRNA for Putative Fatty Acid Transport Related Proteins and Fatty Acyl CoA Synthase in Murine Epidermis and Cultured Human Keratinocytes</atitle><jtitle>Journal of investigative dermatology</jtitle><addtitle>J Invest Dermatol</addtitle><date>1998-11-01</date><risdate>1998</risdate><volume>111</volume><issue>5</issue><spage>722</spage><epage>726</epage><pages>722-726</pages><issn>0022-202X</issn><eissn>1523-1747</eissn><coden>JIDEAE</coden><abstract>The epidermis has a requirement for fatty acids in order to synthesize cellular membranes and the extracellular lipid lamellar membranes in the stratum corneum. Despite high endogenous production of fatty acids the transport of exogenous essential fatty acids into the epidermis is an absolute requirement. Fatty acid uptake by keratinocytes has been shown to be mediated by a transport system. In this study we determined in murine epidermis and human cultured keratinocytes the expression of three putative fatty acid transport related proteins and fatty acyl CoA synthase, an enzyme that facilitates the uptake of fatty acids by promoting their metabolism. In cultured human keratinocytes, mRNA for fatty acid transport protein (FATP), plasma membrane fatty acid binding protein (FABP-pm), and fatty acyl CoA synthase (FACS) were detectable. Differentiation, induced by high calcium, did not affect FATP mRNA levels, but resulted in an ≈50% increase in FACS mRNA, while decreasing FABP-pm mRNA by 50%. Fatty acid translocase (FAT) mRNA was not detected in cultured human keratinocytes. In murine epidermis, FATP, FABP-pm, FACS, and FAT mRNA were all present. Barrier disruption by either tape stripping or acetone treatment increased FAT mRNA levels by ≈2-fold without affecting FATP, FABP-pm, or FACS. Occlusion with an impermeable membrane immediately after barrier disruption completely blocked the increase in FAT mRNA levels, indicating that this increase is related to barrier disruption rather than a nonspecific injury effect. In summary, this study demonstrates that several putative fatty acid transport related proteins as well as fatty acyl CoA synthase are expressed in keratinocytes and epidermis, and that the expression of these proteins may be regulated by differentiation and/or barrier disruption.</abstract><cop>Danvers, MA</cop><pub>Elsevier Inc</pub><pmid>9804328</pmid><doi>10.1046/j.1523-1747.1998.00383.x</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
subjects | Animals Biological and medical sciences Carrier Proteins - genetics CD36 CD36 Antigens Cell Differentiation Cell Membrane Permeability Cells, Cultured Coenzyme A Ligases - genetics FABP-pm FAT FATP Fatty Acid Transport Proteins fatty acid uptake Fundamental and applied biological sciences. Psychology Humans Keratinocytes - chemistry Keratinocytes - cytology Keratinocytes - metabolism Male Membrane Glycoproteins - metabolism Membrane Proteins - genetics Membrane Transport Proteins Mice Mice, Hairless Organic Anion Transporters Repressor Proteins RNA, Messenger - metabolism Saccharomyces cerevisiae Proteins Skin - cytology Skin - metabolism Vertebrates: skin, associated glands, phaneres, light organs, various exocrine glands (salt gland, uropygial gland...), adipose tissue, connective tissue |
title | Expression and Regulation of mRNA for Putative Fatty Acid Transport Related Proteins and Fatty Acyl CoA Synthase in Murine Epidermis and Cultured Human Keratinocytes |
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