Loading…

Identification of human salivary transglutaminases

Transglutaminases (TGs) expression and enzymatic activities in human saliva were investigated. Specific antibodies showed the co-existence of TG1, TG2, TG3 and TG4. TG2 and TG3 were found in native and multiple proteolytic forms. Our data indicate that TG1 and TG2 isoenzymes are highly active with t...

Full description

Saved in:
Bibliographic Details
Published in:Amino acids 2013, Vol.44 (1), p.245-250
Main Authors: Perez Alea, Mileidys, Thomas, Vincent, Martin, Guillaume, El Alaoui, Saïd
Format: Article
Language:English
Subjects:
Citations: Items that this one cites
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-c405t-89d9efd25f9cabf320e2662d3e62c1f02fa1993bd5cf3a4e7bb93977e6da79483
cites cdi_FETCH-LOGICAL-c405t-89d9efd25f9cabf320e2662d3e62c1f02fa1993bd5cf3a4e7bb93977e6da79483
container_end_page 250
container_issue 1
container_start_page 245
container_title Amino acids
container_volume 44
creator Perez Alea, Mileidys
Thomas, Vincent
Martin, Guillaume
El Alaoui, Saïd
description Transglutaminases (TGs) expression and enzymatic activities in human saliva were investigated. Specific antibodies showed the co-existence of TG1, TG2, TG3 and TG4. TG2 and TG3 were found in native and multiple proteolytic forms. Our data indicate that TG1 and TG2 isoenzymes are highly active with the major activity attributed to TG1. These findings pave the way for future studies on the physiological role of TG in the oral cavity and the potential impact of their deregulation in TG-associated oral diseases.
doi_str_mv 10.1007/s00726-011-1142-5
format article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_1816001408</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>4033723511</sourcerecordid><originalsourceid>FETCH-LOGICAL-c405t-89d9efd25f9cabf320e2662d3e62c1f02fa1993bd5cf3a4e7bb93977e6da79483</originalsourceid><addsrcrecordid>eNqNkMtKAzEUhoMotlYfwI0U3LgZPeckc8lSipdCwY2uQ2YmqVPmUpMZwbc3ZaqIILhJFvnOn_N_jJ0jXCNAeuPDQUkEiBGioCg-YFMUPIsIpTxkU5BcRkLEOGEn3m8AkDJMjtmECDIgkFNGy9K0fWWrQvdV1847O38dGt3Ova6rd-0-5r3TrV_XQ6-bqtXe-FN2ZHXtzdn-nrGX-7vnxWO0enpYLm5XUSEg7qNMltLYkmIrC51bTmAoSajkJqECLZDVYUuel3FhuRYmzfOwbpqapNSpFBmfsasxd-u6t8H4XjWVL0xd69Z0g1cYuoRKAv6BUsoxzjKAgF7-Qjfd4NpQRGGaccmJkjhQOFKF67x3xqqtq5qgQyGonXs1ulfBvdq5V7uZi33ykDem_J74kh0AGgEfntq1cT--_jP1E9dvjVA</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1783932265</pqid></control><display><type>article</type><title>Identification of human salivary transglutaminases</title><source>Springer Link</source><creator>Perez Alea, Mileidys ; Thomas, Vincent ; Martin, Guillaume ; El Alaoui, Saïd</creator><creatorcontrib>Perez Alea, Mileidys ; Thomas, Vincent ; Martin, Guillaume ; El Alaoui, Saïd</creatorcontrib><description>Transglutaminases (TGs) expression and enzymatic activities in human saliva were investigated. Specific antibodies showed the co-existence of TG1, TG2, TG3 and TG4. TG2 and TG3 were found in native and multiple proteolytic forms. Our data indicate that TG1 and TG2 isoenzymes are highly active with the major activity attributed to TG1. These findings pave the way for future studies on the physiological role of TG in the oral cavity and the potential impact of their deregulation in TG-associated oral diseases.</description><identifier>ISSN: 0939-4451</identifier><identifier>EISSN: 1438-2199</identifier><identifier>DOI: 10.1007/s00726-011-1142-5</identifier><identifier>PMID: 22080209</identifier><language>eng</language><publisher>Vienna: Springer Vienna</publisher><subject>Amino acids ; Analytical Chemistry ; Antibodies ; Biochemical Engineering ; Biochemistry ; Biomedical and Life Sciences ; Deregulation ; Diseases ; Enzyme Inhibitors - chemistry ; Female ; GTP-Binding Proteins ; Holes ; Human ; Humans ; Isoenzymes - antagonists &amp; inhibitors ; Isoenzymes - chemistry ; Isoenzymes - metabolism ; Life Sciences ; Male ; Neurobiology ; Original Article ; Peptide Fragments - chemistry ; Proteomics ; Saliva ; Saliva - enzymology ; Transglutaminases - antagonists &amp; inhibitors ; Transglutaminases - chemistry ; Transglutaminases - metabolism</subject><ispartof>Amino acids, 2013, Vol.44 (1), p.245-250</ispartof><rights>Springer-Verlag 2011</rights><rights>Springer-Verlag Wien 2013</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c405t-89d9efd25f9cabf320e2662d3e62c1f02fa1993bd5cf3a4e7bb93977e6da79483</citedby><cites>FETCH-LOGICAL-c405t-89d9efd25f9cabf320e2662d3e62c1f02fa1993bd5cf3a4e7bb93977e6da79483</cites></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/22080209$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Perez Alea, Mileidys</creatorcontrib><creatorcontrib>Thomas, Vincent</creatorcontrib><creatorcontrib>Martin, Guillaume</creatorcontrib><creatorcontrib>El Alaoui, Saïd</creatorcontrib><title>Identification of human salivary transglutaminases</title><title>Amino acids</title><addtitle>Amino Acids</addtitle><addtitle>Amino Acids</addtitle><description>Transglutaminases (TGs) expression and enzymatic activities in human saliva were investigated. Specific antibodies showed the co-existence of TG1, TG2, TG3 and TG4. TG2 and TG3 were found in native and multiple proteolytic forms. Our data indicate that TG1 and TG2 isoenzymes are highly active with the major activity attributed to TG1. These findings pave the way for future studies on the physiological role of TG in the oral cavity and the potential impact of their deregulation in TG-associated oral diseases.</description><subject>Amino acids</subject><subject>Analytical Chemistry</subject><subject>Antibodies</subject><subject>Biochemical Engineering</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Deregulation</subject><subject>Diseases</subject><subject>Enzyme Inhibitors - chemistry</subject><subject>Female</subject><subject>GTP-Binding Proteins</subject><subject>Holes</subject><subject>Human</subject><subject>Humans</subject><subject>Isoenzymes - antagonists &amp; inhibitors</subject><subject>Isoenzymes - chemistry</subject><subject>Isoenzymes - metabolism</subject><subject>Life Sciences</subject><subject>Male</subject><subject>Neurobiology</subject><subject>Original Article</subject><subject>Peptide Fragments - chemistry</subject><subject>Proteomics</subject><subject>Saliva</subject><subject>Saliva - enzymology</subject><subject>Transglutaminases - antagonists &amp; inhibitors</subject><subject>Transglutaminases - chemistry</subject><subject>Transglutaminases - metabolism</subject><issn>0939-4451</issn><issn>1438-2199</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><recordid>eNqNkMtKAzEUhoMotlYfwI0U3LgZPeckc8lSipdCwY2uQ2YmqVPmUpMZwbc3ZaqIILhJFvnOn_N_jJ0jXCNAeuPDQUkEiBGioCg-YFMUPIsIpTxkU5BcRkLEOGEn3m8AkDJMjtmECDIgkFNGy9K0fWWrQvdV1847O38dGt3Ova6rd-0-5r3TrV_XQ6-bqtXe-FN2ZHXtzdn-nrGX-7vnxWO0enpYLm5XUSEg7qNMltLYkmIrC51bTmAoSajkJqECLZDVYUuel3FhuRYmzfOwbpqapNSpFBmfsasxd-u6t8H4XjWVL0xd69Z0g1cYuoRKAv6BUsoxzjKAgF7-Qjfd4NpQRGGaccmJkjhQOFKF67x3xqqtq5qgQyGonXs1ulfBvdq5V7uZi33ykDem_J74kh0AGgEfntq1cT--_jP1E9dvjVA</recordid><startdate>2013</startdate><enddate>2013</enddate><creator>Perez Alea, Mileidys</creator><creator>Thomas, Vincent</creator><creator>Martin, Guillaume</creator><creator>El Alaoui, Saïd</creator><general>Springer Vienna</general><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>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7TK</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>PDBOC</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7X8</scope><scope>7U5</scope><scope>8FD</scope><scope>L7M</scope></search><sort><creationdate>2013</creationdate><title>Identification of human salivary transglutaminases</title><author>Perez Alea, Mileidys ; Thomas, Vincent ; Martin, Guillaume ; El Alaoui, Saïd</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c405t-89d9efd25f9cabf320e2662d3e62c1f02fa1993bd5cf3a4e7bb93977e6da79483</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Amino acids</topic><topic>Analytical Chemistry</topic><topic>Antibodies</topic><topic>Biochemical Engineering</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Deregulation</topic><topic>Diseases</topic><topic>Enzyme Inhibitors - chemistry</topic><topic>Female</topic><topic>GTP-Binding Proteins</topic><topic>Holes</topic><topic>Human</topic><topic>Humans</topic><topic>Isoenzymes - antagonists &amp; inhibitors</topic><topic>Isoenzymes - chemistry</topic><topic>Isoenzymes - metabolism</topic><topic>Life Sciences</topic><topic>Male</topic><topic>Neurobiology</topic><topic>Original Article</topic><topic>Peptide Fragments - chemistry</topic><topic>Proteomics</topic><topic>Saliva</topic><topic>Saliva - enzymology</topic><topic>Transglutaminases - antagonists &amp; inhibitors</topic><topic>Transglutaminases - chemistry</topic><topic>Transglutaminases - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Perez Alea, Mileidys</creatorcontrib><creatorcontrib>Thomas, Vincent</creatorcontrib><creatorcontrib>Martin, Guillaume</creatorcontrib><creatorcontrib>El Alaoui, Saïd</creatorcontrib><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>Neurosciences Abstracts</collection><collection>Health &amp; Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology 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>Materials Science &amp; Engineering Collection</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health &amp; Medical Complete (Alumni)</collection><collection>Materials Science Database</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>Materials Science Collection</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>MEDLINE - Academic</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Technology Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><jtitle>Amino acids</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Perez Alea, Mileidys</au><au>Thomas, Vincent</au><au>Martin, Guillaume</au><au>El Alaoui, Saïd</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification of human salivary transglutaminases</atitle><jtitle>Amino acids</jtitle><stitle>Amino Acids</stitle><addtitle>Amino Acids</addtitle><date>2013</date><risdate>2013</risdate><volume>44</volume><issue>1</issue><spage>245</spage><epage>250</epage><pages>245-250</pages><issn>0939-4451</issn><eissn>1438-2199</eissn><abstract>Transglutaminases (TGs) expression and enzymatic activities in human saliva were investigated. Specific antibodies showed the co-existence of TG1, TG2, TG3 and TG4. TG2 and TG3 were found in native and multiple proteolytic forms. Our data indicate that TG1 and TG2 isoenzymes are highly active with the major activity attributed to TG1. These findings pave the way for future studies on the physiological role of TG in the oral cavity and the potential impact of their deregulation in TG-associated oral diseases.</abstract><cop>Vienna</cop><pub>Springer Vienna</pub><pmid>22080209</pmid><doi>10.1007/s00726-011-1142-5</doi><tpages>6</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0939-4451
ispartof Amino acids, 2013, Vol.44 (1), p.245-250
issn 0939-4451
1438-2199
language eng
recordid cdi_proquest_miscellaneous_1816001408
source Springer Link
subjects Amino acids
Analytical Chemistry
Antibodies
Biochemical Engineering
Biochemistry
Biomedical and Life Sciences
Deregulation
Diseases
Enzyme Inhibitors - chemistry
Female
GTP-Binding Proteins
Holes
Human
Humans
Isoenzymes - antagonists & inhibitors
Isoenzymes - chemistry
Isoenzymes - metabolism
Life Sciences
Male
Neurobiology
Original Article
Peptide Fragments - chemistry
Proteomics
Saliva
Saliva - enzymology
Transglutaminases - antagonists & inhibitors
Transglutaminases - chemistry
Transglutaminases - metabolism
title Identification of human salivary transglutaminases
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-26T21%3A19%3A50IST&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=Identification%20of%20human%20salivary%20transglutaminases&rft.jtitle=Amino%20acids&rft.au=Perez%20Alea,%20Mileidys&rft.date=2013&rft.volume=44&rft.issue=1&rft.spage=245&rft.epage=250&rft.pages=245-250&rft.issn=0939-4451&rft.eissn=1438-2199&rft_id=info:doi/10.1007/s00726-011-1142-5&rft_dat=%3Cproquest_cross%3E4033723511%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c405t-89d9efd25f9cabf320e2662d3e62c1f02fa1993bd5cf3a4e7bb93977e6da79483%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=1783932265&rft_id=info:pmid/22080209&rfr_iscdi=true