Submucosal connective tissue-type mast cells contribute to the production of lysophosphatidic acid (LPA) in the gastrointestinal tract through the secretion of autotaxin (ATX)/lysophospholipase D (lysoPLD)

Lysophosphatidic acid (LPA) is involved in a broad spectrum of biological activities, including wound healing and cancer metastasis. Autotaxin (ATX), originally isolated from a melanoma supernatant as a tumor cell motility-stimulating factor, has been shown to be molecularly identical to lysophospho...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Virchows Archiv : an international journal of pathology 2007-07, Vol.451 (1), p.47-56
Hauptverfasser: MORI, Ken, KITAYAMA, Joji, AOKI, Junken, KISHI, Yasuhiro, SHIDA, Dai, YAMASHITA, Hiroharu, ARAI, Hiroyuki, NAGAWA, Hirokazu
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 56
container_issue 1
container_start_page 47
container_title Virchows Archiv : an international journal of pathology
container_volume 451
creator MORI, Ken
KITAYAMA, Joji
AOKI, Junken
KISHI, Yasuhiro
SHIDA, Dai
YAMASHITA, Hiroharu
ARAI, Hiroyuki
NAGAWA, Hirokazu
description Lysophosphatidic acid (LPA) is involved in a broad spectrum of biological activities, including wound healing and cancer metastasis. Autotaxin (ATX), originally isolated from a melanoma supernatant as a tumor cell motility-stimulating factor, has been shown to be molecularly identical to lysophospholipase D (lysoPLD), which is the main enzyme in the production of LPA. Although ATX/lysoPLD is known to be widely expressed in normal human tissues, the exact distribution of ATX-producing cells has not been fully investigated. In this study, we evaluated ATX/lysoPLD expression by immunohistochemical staining using a rat anti-ATX mAb in the human gastrointestinal tract and found that submucosal mast cells (MC) highly expressed this enzyme. This was confirmed by immunofluorescent double staining using mAbs to tryptase and chymase. Then, we isolated MC from human gastric tissue by an immunomagnetic method using CD117-microbeads and showed that a subpopulation of CD203c-positive MC showed positive staining for intracellular ATX/lysoPLD on flowcytometry. This was confirmed by Western blotting of the isolated cells. Moreover, a significant level of ATX/lysoPLD release could be detected in the culture supernatants of human MC by Western blot analysis. Our data suggest that submucosal MC play significant roles in various aspects of pathophysiology in the gastrointestinal tract by locally providing bioactive LPA through the production of ATX/lysoPLD.
doi_str_mv 10.1007/s00428-007-0425-4
format Article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_68253489</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2220030731</sourcerecordid><originalsourceid>FETCH-LOGICAL-c422t-3abdacf57413af40aac971bd0c9fdd7ab22427b70146511f924841ff8cda42143</originalsourceid><addsrcrecordid>eNpdkd1qGzEQhUVpaZy0D9CbIgot9sU2klb7d2mS_oGhgabQu2VWK8UK69VGI5X6IfNO1cYuhl5pkL5zRjOHkDecfeSMVZfImBR1lsosFUUmn5EFl7nIRM6q52TBGllkZc6rM3KOeM-Y4DUvX5IzXhWFLIpmQR5_xG4XlUMYqHLjqFWwvzUNFjHqLOwnTXeAgSo9DDgTwdsuhkQ4GraaTt71MWncSJ2hwx7dtHU4bSHY3ioKyvZ0ublZr6gdnwR3yc07OwaNwY6pa_CgQnryLt5tnxDUyut_lhCDC_AnqZfr21-ry1MLN9gJUNNrupwvbzbXq1fkhYEB9evjeUF-fv50e_U123z_8u1qvcmUFCJkOXQ9KFNUkudgJANQTcW7nqnG9H0FnRBSVF3FuCwLzk0jZC25MbXqQYq04Qvy4eCbxn-IaZJ2Z3FeEYzaRWzLWhS5rJsEvvsPvHfRp7GxrQUrmyZRCeIHSHmH6LVpJ2934PctZ-0cdHsIup3LOeh2_sHbo3HKT_cnxTHZBLw_AoAKBuNhVBZPXN0Ilpd1_hdUwrUj</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>820699348</pqid></control><display><type>article</type><title>Submucosal connective tissue-type mast cells contribute to the production of lysophosphatidic acid (LPA) in the gastrointestinal tract through the secretion of autotaxin (ATX)/lysophospholipase D (lysoPLD)</title><source>MEDLINE</source><source>Springer Nature - Complete Springer Journals</source><creator>MORI, Ken ; KITAYAMA, Joji ; AOKI, Junken ; KISHI, Yasuhiro ; SHIDA, Dai ; YAMASHITA, Hiroharu ; ARAI, Hiroyuki ; NAGAWA, Hirokazu</creator><creatorcontrib>MORI, Ken ; KITAYAMA, Joji ; AOKI, Junken ; KISHI, Yasuhiro ; SHIDA, Dai ; YAMASHITA, Hiroharu ; ARAI, Hiroyuki ; NAGAWA, Hirokazu</creatorcontrib><description>Lysophosphatidic acid (LPA) is involved in a broad spectrum of biological activities, including wound healing and cancer metastasis. Autotaxin (ATX), originally isolated from a melanoma supernatant as a tumor cell motility-stimulating factor, has been shown to be molecularly identical to lysophospholipase D (lysoPLD), which is the main enzyme in the production of LPA. Although ATX/lysoPLD is known to be widely expressed in normal human tissues, the exact distribution of ATX-producing cells has not been fully investigated. In this study, we evaluated ATX/lysoPLD expression by immunohistochemical staining using a rat anti-ATX mAb in the human gastrointestinal tract and found that submucosal mast cells (MC) highly expressed this enzyme. This was confirmed by immunofluorescent double staining using mAbs to tryptase and chymase. Then, we isolated MC from human gastric tissue by an immunomagnetic method using CD117-microbeads and showed that a subpopulation of CD203c-positive MC showed positive staining for intracellular ATX/lysoPLD on flowcytometry. This was confirmed by Western blotting of the isolated cells. Moreover, a significant level of ATX/lysoPLD release could be detected in the culture supernatants of human MC by Western blot analysis. Our data suggest that submucosal MC play significant roles in various aspects of pathophysiology in the gastrointestinal tract by locally providing bioactive LPA through the production of ATX/lysoPLD.</description><identifier>ISSN: 0945-6317</identifier><identifier>EISSN: 1432-2307</identifier><identifier>DOI: 10.1007/s00428-007-0425-4</identifier><identifier>PMID: 17554559</identifier><language>eng</language><publisher>Berlin: Springer</publisher><subject>Biological and medical sciences ; Chymases - analysis ; Gastrointestinal tract ; Gastrointestinal Tract - cytology ; Gastrointestinal Tract - metabolism ; Humans ; Investigative techniques, diagnostic techniques (general aspects) ; Lysophospholipids - biosynthesis ; Mast Cells - classification ; Mast Cells - metabolism ; Medical research ; Medical sciences ; Melanoma ; Multienzyme Complexes - analysis ; Multienzyme Complexes - physiology ; Multienzyme Complexes - secretion ; Pathology. Cytology. Biochemistry. Spectrometry. Miscellaneous investigative techniques ; Phosphodiesterase I - analysis ; Phosphodiesterase I - physiology ; Phosphodiesterase I - secretion ; Phosphoric Diester Hydrolases - analysis ; Phosphoric Diester Hydrolases - physiology ; Phosphoric Diester Hydrolases - secretion ; Proteins ; Pyrophosphatases - analysis ; Pyrophosphatases - physiology ; Pyrophosphatases - secretion ; Tryptases - analysis ; Wound Healing</subject><ispartof>Virchows Archiv : an international journal of pathology, 2007-07, Vol.451 (1), p.47-56</ispartof><rights>2007 INIST-CNRS</rights><rights>Springer-Verlag 2007</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c422t-3abdacf57413af40aac971bd0c9fdd7ab22427b70146511f924841ff8cda42143</citedby><cites>FETCH-LOGICAL-c422t-3abdacf57413af40aac971bd0c9fdd7ab22427b70146511f924841ff8cda42143</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&amp;idt=18920368$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17554559$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>MORI, Ken</creatorcontrib><creatorcontrib>KITAYAMA, Joji</creatorcontrib><creatorcontrib>AOKI, Junken</creatorcontrib><creatorcontrib>KISHI, Yasuhiro</creatorcontrib><creatorcontrib>SHIDA, Dai</creatorcontrib><creatorcontrib>YAMASHITA, Hiroharu</creatorcontrib><creatorcontrib>ARAI, Hiroyuki</creatorcontrib><creatorcontrib>NAGAWA, Hirokazu</creatorcontrib><title>Submucosal connective tissue-type mast cells contribute to the production of lysophosphatidic acid (LPA) in the gastrointestinal tract through the secretion of autotaxin (ATX)/lysophospholipase D (lysoPLD)</title><title>Virchows Archiv : an international journal of pathology</title><addtitle>Virchows Arch</addtitle><description>Lysophosphatidic acid (LPA) is involved in a broad spectrum of biological activities, including wound healing and cancer metastasis. Autotaxin (ATX), originally isolated from a melanoma supernatant as a tumor cell motility-stimulating factor, has been shown to be molecularly identical to lysophospholipase D (lysoPLD), which is the main enzyme in the production of LPA. Although ATX/lysoPLD is known to be widely expressed in normal human tissues, the exact distribution of ATX-producing cells has not been fully investigated. In this study, we evaluated ATX/lysoPLD expression by immunohistochemical staining using a rat anti-ATX mAb in the human gastrointestinal tract and found that submucosal mast cells (MC) highly expressed this enzyme. This was confirmed by immunofluorescent double staining using mAbs to tryptase and chymase. Then, we isolated MC from human gastric tissue by an immunomagnetic method using CD117-microbeads and showed that a subpopulation of CD203c-positive MC showed positive staining for intracellular ATX/lysoPLD on flowcytometry. This was confirmed by Western blotting of the isolated cells. Moreover, a significant level of ATX/lysoPLD release could be detected in the culture supernatants of human MC by Western blot analysis. Our data suggest that submucosal MC play significant roles in various aspects of pathophysiology in the gastrointestinal tract by locally providing bioactive LPA through the production of ATX/lysoPLD.</description><subject>Biological and medical sciences</subject><subject>Chymases - analysis</subject><subject>Gastrointestinal tract</subject><subject>Gastrointestinal Tract - cytology</subject><subject>Gastrointestinal Tract - metabolism</subject><subject>Humans</subject><subject>Investigative techniques, diagnostic techniques (general aspects)</subject><subject>Lysophospholipids - biosynthesis</subject><subject>Mast Cells - classification</subject><subject>Mast Cells - metabolism</subject><subject>Medical research</subject><subject>Medical sciences</subject><subject>Melanoma</subject><subject>Multienzyme Complexes - analysis</subject><subject>Multienzyme Complexes - physiology</subject><subject>Multienzyme Complexes - secretion</subject><subject>Pathology. Cytology. Biochemistry. Spectrometry. Miscellaneous investigative techniques</subject><subject>Phosphodiesterase I - analysis</subject><subject>Phosphodiesterase I - physiology</subject><subject>Phosphodiesterase I - secretion</subject><subject>Phosphoric Diester Hydrolases - analysis</subject><subject>Phosphoric Diester Hydrolases - physiology</subject><subject>Phosphoric Diester Hydrolases - secretion</subject><subject>Proteins</subject><subject>Pyrophosphatases - analysis</subject><subject>Pyrophosphatases - physiology</subject><subject>Pyrophosphatases - secretion</subject><subject>Tryptases - analysis</subject><subject>Wound Healing</subject><issn>0945-6317</issn><issn>1432-2307</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNpdkd1qGzEQhUVpaZy0D9CbIgot9sU2klb7d2mS_oGhgabQu2VWK8UK69VGI5X6IfNO1cYuhl5pkL5zRjOHkDecfeSMVZfImBR1lsosFUUmn5EFl7nIRM6q52TBGllkZc6rM3KOeM-Y4DUvX5IzXhWFLIpmQR5_xG4XlUMYqHLjqFWwvzUNFjHqLOwnTXeAgSo9DDgTwdsuhkQ4GraaTt71MWncSJ2hwx7dtHU4bSHY3ioKyvZ0ublZr6gdnwR3yc07OwaNwY6pa_CgQnryLt5tnxDUyut_lhCDC_AnqZfr21-ry1MLN9gJUNNrupwvbzbXq1fkhYEB9evjeUF-fv50e_U123z_8u1qvcmUFCJkOXQ9KFNUkudgJANQTcW7nqnG9H0FnRBSVF3FuCwLzk0jZC25MbXqQYq04Qvy4eCbxn-IaZJ2Z3FeEYzaRWzLWhS5rJsEvvsPvHfRp7GxrQUrmyZRCeIHSHmH6LVpJ2934PctZ-0cdHsIup3LOeh2_sHbo3HKT_cnxTHZBLw_AoAKBuNhVBZPXN0Ilpd1_hdUwrUj</recordid><startdate>20070701</startdate><enddate>20070701</enddate><creator>MORI, Ken</creator><creator>KITAYAMA, Joji</creator><creator>AOKI, Junken</creator><creator>KISHI, Yasuhiro</creator><creator>SHIDA, Dai</creator><creator>YAMASHITA, Hiroharu</creator><creator>ARAI, Hiroyuki</creator><creator>NAGAWA, Hirokazu</creator><general>Springer</general><general>Springer Nature B.V</general><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>3V.</scope><scope>7RV</scope><scope>7T5</scope><scope>7T7</scope><scope>7TM</scope><scope>7TO</scope><scope>7U7</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</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>KB0</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>NAPCQ</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>7X8</scope></search><sort><creationdate>20070701</creationdate><title>Submucosal connective tissue-type mast cells contribute to the production of lysophosphatidic acid (LPA) in the gastrointestinal tract through the secretion of autotaxin (ATX)/lysophospholipase D (lysoPLD)</title><author>MORI, Ken ; KITAYAMA, Joji ; AOKI, Junken ; KISHI, Yasuhiro ; SHIDA, Dai ; YAMASHITA, Hiroharu ; ARAI, Hiroyuki ; NAGAWA, Hirokazu</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c422t-3abdacf57413af40aac971bd0c9fdd7ab22427b70146511f924841ff8cda42143</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Biological and medical sciences</topic><topic>Chymases - analysis</topic><topic>Gastrointestinal tract</topic><topic>Gastrointestinal Tract - cytology</topic><topic>Gastrointestinal Tract - metabolism</topic><topic>Humans</topic><topic>Investigative techniques, diagnostic techniques (general aspects)</topic><topic>Lysophospholipids - biosynthesis</topic><topic>Mast Cells - classification</topic><topic>Mast Cells - metabolism</topic><topic>Medical research</topic><topic>Medical sciences</topic><topic>Melanoma</topic><topic>Multienzyme Complexes - analysis</topic><topic>Multienzyme Complexes - physiology</topic><topic>Multienzyme Complexes - secretion</topic><topic>Pathology. Cytology. Biochemistry. Spectrometry. Miscellaneous investigative techniques</topic><topic>Phosphodiesterase I - analysis</topic><topic>Phosphodiesterase I - physiology</topic><topic>Phosphodiesterase I - secretion</topic><topic>Phosphoric Diester Hydrolases - analysis</topic><topic>Phosphoric Diester Hydrolases - physiology</topic><topic>Phosphoric Diester Hydrolases - secretion</topic><topic>Proteins</topic><topic>Pyrophosphatases - analysis</topic><topic>Pyrophosphatases - physiology</topic><topic>Pyrophosphatases - secretion</topic><topic>Tryptases - analysis</topic><topic>Wound Healing</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>MORI, Ken</creatorcontrib><creatorcontrib>KITAYAMA, Joji</creatorcontrib><creatorcontrib>AOKI, Junken</creatorcontrib><creatorcontrib>KISHI, Yasuhiro</creatorcontrib><creatorcontrib>SHIDA, Dai</creatorcontrib><creatorcontrib>YAMASHITA, Hiroharu</creatorcontrib><creatorcontrib>ARAI, Hiroyuki</creatorcontrib><creatorcontrib>NAGAWA, Hirokazu</creatorcontrib><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>ProQuest Central (Corporate)</collection><collection>Nursing &amp; Allied Health Database</collection><collection>Immunology Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Toxicology 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>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 Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</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>Nursing &amp; Allied Health Database (Alumni Edition)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health &amp; Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>Nursing &amp; Allied Health Premium</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>MEDLINE - Academic</collection><jtitle>Virchows Archiv : an international journal of pathology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>MORI, Ken</au><au>KITAYAMA, Joji</au><au>AOKI, Junken</au><au>KISHI, Yasuhiro</au><au>SHIDA, Dai</au><au>YAMASHITA, Hiroharu</au><au>ARAI, Hiroyuki</au><au>NAGAWA, Hirokazu</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Submucosal connective tissue-type mast cells contribute to the production of lysophosphatidic acid (LPA) in the gastrointestinal tract through the secretion of autotaxin (ATX)/lysophospholipase D (lysoPLD)</atitle><jtitle>Virchows Archiv : an international journal of pathology</jtitle><addtitle>Virchows Arch</addtitle><date>2007-07-01</date><risdate>2007</risdate><volume>451</volume><issue>1</issue><spage>47</spage><epage>56</epage><pages>47-56</pages><issn>0945-6317</issn><eissn>1432-2307</eissn><abstract>Lysophosphatidic acid (LPA) is involved in a broad spectrum of biological activities, including wound healing and cancer metastasis. Autotaxin (ATX), originally isolated from a melanoma supernatant as a tumor cell motility-stimulating factor, has been shown to be molecularly identical to lysophospholipase D (lysoPLD), which is the main enzyme in the production of LPA. Although ATX/lysoPLD is known to be widely expressed in normal human tissues, the exact distribution of ATX-producing cells has not been fully investigated. In this study, we evaluated ATX/lysoPLD expression by immunohistochemical staining using a rat anti-ATX mAb in the human gastrointestinal tract and found that submucosal mast cells (MC) highly expressed this enzyme. This was confirmed by immunofluorescent double staining using mAbs to tryptase and chymase. Then, we isolated MC from human gastric tissue by an immunomagnetic method using CD117-microbeads and showed that a subpopulation of CD203c-positive MC showed positive staining for intracellular ATX/lysoPLD on flowcytometry. This was confirmed by Western blotting of the isolated cells. Moreover, a significant level of ATX/lysoPLD release could be detected in the culture supernatants of human MC by Western blot analysis. Our data suggest that submucosal MC play significant roles in various aspects of pathophysiology in the gastrointestinal tract by locally providing bioactive LPA through the production of ATX/lysoPLD.</abstract><cop>Berlin</cop><pub>Springer</pub><pmid>17554559</pmid><doi>10.1007/s00428-007-0425-4</doi><tpages>10</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0945-6317
ispartof Virchows Archiv : an international journal of pathology, 2007-07, Vol.451 (1), p.47-56
issn 0945-6317
1432-2307
language eng
recordid cdi_proquest_miscellaneous_68253489
source MEDLINE; Springer Nature - Complete Springer Journals
subjects Biological and medical sciences
Chymases - analysis
Gastrointestinal tract
Gastrointestinal Tract - cytology
Gastrointestinal Tract - metabolism
Humans
Investigative techniques, diagnostic techniques (general aspects)
Lysophospholipids - biosynthesis
Mast Cells - classification
Mast Cells - metabolism
Medical research
Medical sciences
Melanoma
Multienzyme Complexes - analysis
Multienzyme Complexes - physiology
Multienzyme Complexes - secretion
Pathology. Cytology. Biochemistry. Spectrometry. Miscellaneous investigative techniques
Phosphodiesterase I - analysis
Phosphodiesterase I - physiology
Phosphodiesterase I - secretion
Phosphoric Diester Hydrolases - analysis
Phosphoric Diester Hydrolases - physiology
Phosphoric Diester Hydrolases - secretion
Proteins
Pyrophosphatases - analysis
Pyrophosphatases - physiology
Pyrophosphatases - secretion
Tryptases - analysis
Wound Healing
title Submucosal connective tissue-type mast cells contribute to the production of lysophosphatidic acid (LPA) in the gastrointestinal tract through the secretion of autotaxin (ATX)/lysophospholipase D (lysoPLD)
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-13T11%3A29%3A35IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Submucosal%20connective%20tissue-type%20mast%20cells%20contribute%20to%20the%20production%20of%20lysophosphatidic%20acid%20(LPA)%20in%20the%20gastrointestinal%20tract%20through%20the%20secretion%20of%20autotaxin%20(ATX)/lysophospholipase%20D%20(lysoPLD)&rft.jtitle=Virchows%20Archiv%20:%20an%20international%20journal%20of%20pathology&rft.au=MORI,%20Ken&rft.date=2007-07-01&rft.volume=451&rft.issue=1&rft.spage=47&rft.epage=56&rft.pages=47-56&rft.issn=0945-6317&rft.eissn=1432-2307&rft_id=info:doi/10.1007/s00428-007-0425-4&rft_dat=%3Cproquest_cross%3E2220030731%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=820699348&rft_id=info:pmid/17554559&rfr_iscdi=true