sPLA2-X Stimulates Cutaneous Melanocyte Dendricity and Pigmentation Through a Lysophosphatidylcholine-Dependent Mechanism
Photoprotection of the skin is provided by melanocytes, neural crest derived cells that synthesize melanin in specialized organelles that are transferred to keratinocytes. Secretory phospholipases comprise a large family of Ca2+-dependent enzymes that liberate arachidonic acid (AA), a precursor of p...
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description | Photoprotection of the skin is provided by melanocytes, neural crest derived cells that synthesize melanin in specialized organelles that are transferred to keratinocytes. Secretory phospholipases comprise a large family of Ca2+-dependent enzymes that liberate arachidonic acid (AA), a precursor of prostaglandins, as well as lysophospholipids. The predominant secretory phospholipase expressed by keratinocytes is group X secretory phospholipase A2 (sPLA2), which liberates large amounts of AA and the lysophospholipid lysophosphatidylcholine (LPC), from membrane preparations. Recent work by our laboratory has shown that melanocytes express receptors for prostaglandins that upon activation stimulate melanocyte dendricity and activity of tyrosinase, a key enzyme in melanin biosynthesis. In the present study, we have treated human melanocytes with recombinant sPLA2-X and show that low levels of sPLA2-X stimulate both tyrosinase activity and melanocyte dendricity. We found that the effects of sPLA2-X are mediated predominantly by LPC, not AA, and we have demonstrated expression of the phospholipase A2 receptor and two G-protein-coupled receptors for LPC (G2A and GPR119) in human melanocytes. Because secretory phospholipases are released during inflammation and are regulated by UV irradiation, our data suggest an important role for sPLA2-X in cutaneous pigmentation through the release of LPC. |
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Secretory phospholipases comprise a large family of Ca2+-dependent enzymes that liberate arachidonic acid (AA), a precursor of prostaglandins, as well as lysophospholipids. The predominant secretory phospholipase expressed by keratinocytes is group X secretory phospholipase A2 (sPLA2), which liberates large amounts of AA and the lysophospholipid lysophosphatidylcholine (LPC), from membrane preparations. Recent work by our laboratory has shown that melanocytes express receptors for prostaglandins that upon activation stimulate melanocyte dendricity and activity of tyrosinase, a key enzyme in melanin biosynthesis. In the present study, we have treated human melanocytes with recombinant sPLA2-X and show that low levels of sPLA2-X stimulate both tyrosinase activity and melanocyte dendricity. We found that the effects of sPLA2-X are mediated predominantly by LPC, not AA, and we have demonstrated expression of the phospholipase A2 receptor and two G-protein-coupled receptors for LPC (G2A and GPR119) in human melanocytes. Because secretory phospholipases are released during inflammation and are regulated by UV irradiation, our data suggest an important role for sPLA2-X in cutaneous pigmentation through the release of LPC.</description><identifier>ISSN: 0022-202X</identifier><identifier>EISSN: 1523-1747</identifier><identifier>DOI: 10.1038/sj.jid.5700180</identifier><identifier>PMID: 16456529</identifier><identifier>CODEN: JIDEAE</identifier><language>eng</language><publisher>Danvers, MA: Elsevier Inc</publisher><subject>Arachidonic Acid - metabolism ; Biological and medical sciences ; Cell Cycle Proteins - metabolism ; Cell Proliferation ; Dermatology ; Group X Phospholipases A2 ; Humans ; Lysophosphatidylcholines - metabolism ; Medical sciences ; Melanocytes - cytology ; Melanocytes - drug effects ; Melanocytes - metabolism ; Monophenol Monooxygenase - metabolism ; Phospholipases A - pharmacology ; Phospholipases A2 ; Receptors, Cell Surface - genetics ; Receptors, Cell Surface - metabolism ; Receptors, G-Protein-Coupled - metabolism ; Receptors, Phospholipase A2 ; Skin - cytology ; Skin - drug effects ; Skin Pigmentation</subject><ispartof>Journal of investigative dermatology, 2006-04, Vol.126 (4), p.855-861</ispartof><rights>2006 The Society for Investigative Dermatology, Inc</rights><rights>2006 INIST-CNRS</rights><rights>Copyright Nature Publishing Group Apr 2006</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.proquest.com/docview/210375242?pq-origsite=primo$$EHTML$$P50$$Gproquest$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,64385,64387,64389,72469</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=17692081$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16456529$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Scott, Glynis A.</creatorcontrib><creatorcontrib>Jacobs, Stacey E.</creatorcontrib><creatorcontrib>Pentland, Alice P.</creatorcontrib><title>sPLA2-X Stimulates Cutaneous Melanocyte Dendricity and Pigmentation Through a Lysophosphatidylcholine-Dependent Mechanism</title><title>Journal of investigative dermatology</title><addtitle>J Invest Dermatol</addtitle><description>Photoprotection of the skin is provided by melanocytes, neural crest derived cells that synthesize melanin in specialized organelles that are transferred to keratinocytes. Secretory phospholipases comprise a large family of Ca2+-dependent enzymes that liberate arachidonic acid (AA), a precursor of prostaglandins, as well as lysophospholipids. The predominant secretory phospholipase expressed by keratinocytes is group X secretory phospholipase A2 (sPLA2), which liberates large amounts of AA and the lysophospholipid lysophosphatidylcholine (LPC), from membrane preparations. Recent work by our laboratory has shown that melanocytes express receptors for prostaglandins that upon activation stimulate melanocyte dendricity and activity of tyrosinase, a key enzyme in melanin biosynthesis. In the present study, we have treated human melanocytes with recombinant sPLA2-X and show that low levels of sPLA2-X stimulate both tyrosinase activity and melanocyte dendricity. We found that the effects of sPLA2-X are mediated predominantly by LPC, not AA, and we have demonstrated expression of the phospholipase A2 receptor and two G-protein-coupled receptors for LPC (G2A and GPR119) in human melanocytes. Because secretory phospholipases are released during inflammation and are regulated by UV irradiation, our data suggest an important role for sPLA2-X in cutaneous pigmentation through the release of LPC.</description><subject>Arachidonic Acid - metabolism</subject><subject>Biological and medical sciences</subject><subject>Cell Cycle Proteins - metabolism</subject><subject>Cell Proliferation</subject><subject>Dermatology</subject><subject>Group X Phospholipases A2</subject><subject>Humans</subject><subject>Lysophosphatidylcholines - metabolism</subject><subject>Medical sciences</subject><subject>Melanocytes - cytology</subject><subject>Melanocytes - drug effects</subject><subject>Melanocytes - metabolism</subject><subject>Monophenol Monooxygenase - metabolism</subject><subject>Phospholipases A - pharmacology</subject><subject>Phospholipases A2</subject><subject>Receptors, Cell Surface - genetics</subject><subject>Receptors, Cell Surface - metabolism</subject><subject>Receptors, G-Protein-Coupled - metabolism</subject><subject>Receptors, Phospholipase A2</subject><subject>Skin - cytology</subject><subject>Skin - drug effects</subject><subject>Skin Pigmentation</subject><issn>0022-202X</issn><issn>1523-1747</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><recordid>eNpd0U1r3DAQBmBRGppN2muPxRTam7f6sCT7GDZtGtjSQFPITWjlcSxjS64kF_zvo7BbCjnNQc-MNHoRek_wlmBWf4nDdrDtlkuMSY1foQ3hlJVEVvI12mBMaUkxfThHFzEOmYiK12_Q-XMVnDYbtMa7_RUtH4pfyU7LqBPEYrck7cAvsfgBo3berAmKa3BtsMamtdCuLe7s4wQu6WS9K-774JfHvtDFfo1-7n2c-3zSrqPp_WgdlNcw5_7ckEeaXjsbp7forNNjhHeneol-f_t6v_te7n_e3O6u9iVQhlMpuGwx7RogBFeUEixNQwUzwCtKaEWqpuKd4Ieu4UZoAW1tjGgkOWBGGCeGXaLPx7lz8H8WiElNNhoYx-OOSkjJRVOLDD--gINfgstvU_laJjmtaEYfTmg5TNCqOdhJh1X9-9EMPp2AjkaPXdDO2PjfSdFQXJPs6qODvPtfC0FFY8EZaG0Ak1TrrSJYPYes4qByyOoUMnsCUtiY1A</recordid><startdate>200604</startdate><enddate>200604</enddate><creator>Scott, Glynis A.</creator><creator>Jacobs, Stacey E.</creator><creator>Pentland, Alice P.</creator><general>Elsevier Inc</general><general>Nature Publishing</general><general>Elsevier Limited</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>3V.</scope><scope>7T5</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>BENPR</scope><scope>CCPQU</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>H94</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>200604</creationdate><title>sPLA2-X Stimulates Cutaneous Melanocyte Dendricity and Pigmentation Through a Lysophosphatidylcholine-Dependent Mechanism</title><author>Scott, Glynis A. ; Jacobs, Stacey E. ; Pentland, Alice P.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-e230t-657d02f9e110422107c9263ce54212414945f65bf95c6a6ed8cc6971b031351c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Arachidonic Acid - metabolism</topic><topic>Biological and medical sciences</topic><topic>Cell Cycle Proteins - metabolism</topic><topic>Cell Proliferation</topic><topic>Dermatology</topic><topic>Group X Phospholipases A2</topic><topic>Humans</topic><topic>Lysophosphatidylcholines - metabolism</topic><topic>Medical sciences</topic><topic>Melanocytes - cytology</topic><topic>Melanocytes - drug effects</topic><topic>Melanocytes - metabolism</topic><topic>Monophenol Monooxygenase - metabolism</topic><topic>Phospholipases A - pharmacology</topic><topic>Phospholipases A2</topic><topic>Receptors, Cell Surface - genetics</topic><topic>Receptors, Cell Surface - metabolism</topic><topic>Receptors, G-Protein-Coupled - metabolism</topic><topic>Receptors, Phospholipase A2</topic><topic>Skin - cytology</topic><topic>Skin - drug effects</topic><topic>Skin Pigmentation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Scott, Glynis A.</creatorcontrib><creatorcontrib>Jacobs, Stacey E.</creatorcontrib><creatorcontrib>Pentland, Alice P.</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>ProQuest Central (Corporate)</collection><collection>Immunology Abstracts</collection><collection>ProQuest Health and Medical</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</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 Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central</collection><collection>ProQuest One Community College</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical 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 China</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of investigative dermatology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Scott, Glynis A.</au><au>Jacobs, Stacey E.</au><au>Pentland, Alice P.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>sPLA2-X Stimulates Cutaneous Melanocyte Dendricity and Pigmentation Through a Lysophosphatidylcholine-Dependent Mechanism</atitle><jtitle>Journal of investigative dermatology</jtitle><addtitle>J Invest Dermatol</addtitle><date>2006-04</date><risdate>2006</risdate><volume>126</volume><issue>4</issue><spage>855</spage><epage>861</epage><pages>855-861</pages><issn>0022-202X</issn><eissn>1523-1747</eissn><coden>JIDEAE</coden><abstract>Photoprotection of the skin is provided by melanocytes, neural crest derived cells that synthesize melanin in specialized organelles that are transferred to keratinocytes. Secretory phospholipases comprise a large family of Ca2+-dependent enzymes that liberate arachidonic acid (AA), a precursor of prostaglandins, as well as lysophospholipids. The predominant secretory phospholipase expressed by keratinocytes is group X secretory phospholipase A2 (sPLA2), which liberates large amounts of AA and the lysophospholipid lysophosphatidylcholine (LPC), from membrane preparations. Recent work by our laboratory has shown that melanocytes express receptors for prostaglandins that upon activation stimulate melanocyte dendricity and activity of tyrosinase, a key enzyme in melanin biosynthesis. In the present study, we have treated human melanocytes with recombinant sPLA2-X and show that low levels of sPLA2-X stimulate both tyrosinase activity and melanocyte dendricity. We found that the effects of sPLA2-X are mediated predominantly by LPC, not AA, and we have demonstrated expression of the phospholipase A2 receptor and two G-protein-coupled receptors for LPC (G2A and GPR119) in human melanocytes. Because secretory phospholipases are released during inflammation and are regulated by UV irradiation, our data suggest an important role for sPLA2-X in cutaneous pigmentation through the release of LPC.</abstract><cop>Danvers, MA</cop><pub>Elsevier Inc</pub><pmid>16456529</pmid><doi>10.1038/sj.jid.5700180</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Arachidonic Acid - metabolism Biological and medical sciences Cell Cycle Proteins - metabolism Cell Proliferation Dermatology Group X Phospholipases A2 Humans Lysophosphatidylcholines - metabolism Medical sciences Melanocytes - cytology Melanocytes - drug effects Melanocytes - metabolism Monophenol Monooxygenase - metabolism Phospholipases A - pharmacology Phospholipases A2 Receptors, Cell Surface - genetics Receptors, Cell Surface - metabolism Receptors, G-Protein-Coupled - metabolism Receptors, Phospholipase A2 Skin - cytology Skin - drug effects Skin Pigmentation |
title | sPLA2-X Stimulates Cutaneous Melanocyte Dendricity and Pigmentation Through a Lysophosphatidylcholine-Dependent Mechanism |
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