Inactive Zymogen and Highly Active Proteolytically Processed Membrane-Bound Forms of the Transglutaminase 1 Enzyme in Human Epidermal Keratinocytes
The transglutaminase 1 enzyme is important for the formation of a cornified cell envelope in terminally differentiating keratinocytes. We show here that it is present in low levels in proliferating foreskin or cultured epidermal cells as an inactive zymogen full length form of 106 kDa, of which >...
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Veröffentlicht in: | Biochemical and biophysical research communications 1996-04, Vol.221 (1), p.101-106 |
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creator | Steinert, Peter M. Chung, Soo-Il Kim, Soo-Youl |
description | The transglutaminase 1 enzyme is important for the formation of a cornified cell envelope in terminally differentiating keratinocytes. We show here that it is present in low levels in proliferating foreskin or cultured epidermal cells as an inactive zymogen full length form of 106 kDa, of which >95% is attached to membranes. In terminally differentiating keratinocytes, there is a ≥100-fold induction of mRNA and protein. In addition to some cytosolic protein, most of the newly expressed protein is attached to membranes, of which about half exists in the zymogen form. Other protein consists of a 67/33/10 kDa complex formed by proteolytic processing at specific sites, and is anchored by way of the 10 kDa fragment. This processed form is very highly active and thus accounts for almost all transglutaminase 1 activity in keratinocytes. |
doi_str_mv | 10.1006/bbrc.1996.0552 |
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We show here that it is present in low levels in proliferating foreskin or cultured epidermal cells as an inactive zymogen full length form of 106 kDa, of which >95% is attached to membranes. In terminally differentiating keratinocytes, there is a ≥100-fold induction of mRNA and protein. In addition to some cytosolic protein, most of the newly expressed protein is attached to membranes, of which about half exists in the zymogen form. Other protein consists of a 67/33/10 kDa complex formed by proteolytic processing at specific sites, and is anchored by way of the 10 kDa fragment. This processed form is very highly active and thus accounts for almost all transglutaminase 1 activity in keratinocytes.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1006/bbrc.1996.0552</identifier><identifier>PMID: 8660317</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Base Sequence ; Cell Membrane - metabolism ; Cells, Cultured ; Cytosol - metabolism ; DNA Primers ; Enzyme Precursors - metabolism ; Epidermis - enzymology ; Humans ; Hydrolysis ; Keratinocytes - enzymology ; Molecular Sequence Data ; Protein Processing, Post-Translational ; Transglutaminases - metabolism</subject><ispartof>Biochemical and biophysical research communications, 1996-04, Vol.221 (1), p.101-106</ispartof><rights>1996 Academic Press</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c405t-5560a26d3ad016b22522db484fd77e0739f8c9d3f22fb2a9464634db7be6ecd83</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0006291X96905525$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8660317$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Steinert, Peter M.</creatorcontrib><creatorcontrib>Chung, Soo-Il</creatorcontrib><creatorcontrib>Kim, Soo-Youl</creatorcontrib><title>Inactive Zymogen and Highly Active Proteolytically Processed Membrane-Bound Forms of the Transglutaminase 1 Enzyme in Human Epidermal Keratinocytes</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>The transglutaminase 1 enzyme is important for the formation of a cornified cell envelope in terminally differentiating keratinocytes. We show here that it is present in low levels in proliferating foreskin or cultured epidermal cells as an inactive zymogen full length form of 106 kDa, of which >95% is attached to membranes. In terminally differentiating keratinocytes, there is a ≥100-fold induction of mRNA and protein. In addition to some cytosolic protein, most of the newly expressed protein is attached to membranes, of which about half exists in the zymogen form. Other protein consists of a 67/33/10 kDa complex formed by proteolytic processing at specific sites, and is anchored by way of the 10 kDa fragment. This processed form is very highly active and thus accounts for almost all transglutaminase 1 activity in keratinocytes.</description><subject>Base Sequence</subject><subject>Cell Membrane - metabolism</subject><subject>Cells, Cultured</subject><subject>Cytosol - metabolism</subject><subject>DNA Primers</subject><subject>Enzyme Precursors - metabolism</subject><subject>Epidermis - enzymology</subject><subject>Humans</subject><subject>Hydrolysis</subject><subject>Keratinocytes - enzymology</subject><subject>Molecular Sequence Data</subject><subject>Protein Processing, Post-Translational</subject><subject>Transglutaminases - metabolism</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1UU1v1DAQtRCoLIUrNySfuGWxncSJj6XadiuK2kORql4sx55sjWJ7sZ1K4W_wh_FqV9w4jWbeh_TmIfSRkjUlhH8ZhqjXVAi-Jm3LXqEVJYJUjJLmNVqRwqiYoI9v0buUfhJCacPFGTrrOSc17Vboz41XOtsXwE-LCzvwWHmDt3b3PC344ojcx5AhTEu2Wk3lXHYNKYHB38ENUXmovoa5yK5CdAmHEednwA8FSLtpzspZrxJgijf-9-IAW4-3s1Meb_bWQHRqwt8gqmx90EuG9B69GdWU4MNpnqMfV5uHy211e3d9c3lxW-mGtLlqW04U46ZWhlA-MNYyZoamb0bTdUC6Woy9FqYeGRsHpkTDG143ZugG4KBNX5-jz0fffQy_ZkhZOps0TFNJFOYku560tGaiENdHoo4hpQij3EfrVFwkJfLQgjy0IA8tyEMLRfDp5DwPDsw_-untBe-POJR4LxaiTNqC12BsBJ2lCfZ_1n8BawCZJQ</recordid><startdate>19960405</startdate><enddate>19960405</enddate><creator>Steinert, Peter M.</creator><creator>Chung, Soo-Il</creator><creator>Kim, Soo-Youl</creator><general>Elsevier Inc</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>7X8</scope></search><sort><creationdate>19960405</creationdate><title>Inactive Zymogen and Highly Active Proteolytically Processed Membrane-Bound Forms of the Transglutaminase 1 Enzyme in Human Epidermal Keratinocytes</title><author>Steinert, Peter M. ; Chung, Soo-Il ; Kim, Soo-Youl</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c405t-5560a26d3ad016b22522db484fd77e0739f8c9d3f22fb2a9464634db7be6ecd83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Base Sequence</topic><topic>Cell Membrane - metabolism</topic><topic>Cells, Cultured</topic><topic>Cytosol - metabolism</topic><topic>DNA Primers</topic><topic>Enzyme Precursors - metabolism</topic><topic>Epidermis - enzymology</topic><topic>Humans</topic><topic>Hydrolysis</topic><topic>Keratinocytes - enzymology</topic><topic>Molecular Sequence Data</topic><topic>Protein Processing, Post-Translational</topic><topic>Transglutaminases - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Steinert, Peter M.</creatorcontrib><creatorcontrib>Chung, Soo-Il</creatorcontrib><creatorcontrib>Kim, Soo-Youl</creatorcontrib><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>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Steinert, Peter M.</au><au>Chung, Soo-Il</au><au>Kim, Soo-Youl</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Inactive Zymogen and Highly Active Proteolytically Processed Membrane-Bound Forms of the Transglutaminase 1 Enzyme in Human Epidermal Keratinocytes</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1996-04-05</date><risdate>1996</risdate><volume>221</volume><issue>1</issue><spage>101</spage><epage>106</epage><pages>101-106</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>The transglutaminase 1 enzyme is important for the formation of a cornified cell envelope in terminally differentiating keratinocytes. We show here that it is present in low levels in proliferating foreskin or cultured epidermal cells as an inactive zymogen full length form of 106 kDa, of which >95% is attached to membranes. In terminally differentiating keratinocytes, there is a ≥100-fold induction of mRNA and protein. In addition to some cytosolic protein, most of the newly expressed protein is attached to membranes, of which about half exists in the zymogen form. Other protein consists of a 67/33/10 kDa complex formed by proteolytic processing at specific sites, and is anchored by way of the 10 kDa fragment. This processed form is very highly active and thus accounts for almost all transglutaminase 1 activity in keratinocytes.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>8660317</pmid><doi>10.1006/bbrc.1996.0552</doi><tpages>6</tpages></addata></record> |
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subjects | Base Sequence Cell Membrane - metabolism Cells, Cultured Cytosol - metabolism DNA Primers Enzyme Precursors - metabolism Epidermis - enzymology Humans Hydrolysis Keratinocytes - enzymology Molecular Sequence Data Protein Processing, Post-Translational Transglutaminases - metabolism |
title | Inactive Zymogen and Highly Active Proteolytically Processed Membrane-Bound Forms of the Transglutaminase 1 Enzyme in Human Epidermal Keratinocytes |
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