Enzymatic Activity of Desquamin
We have previously described the properties of desquamin, a cell adhesion molecule in the stratum corneum with lectin-like properties specific for amine sugars. We report here that desquamin is also a trypsin-like serine proteinase. It degrades several chromogenic peptides with arginine in the P1 po...
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| Veröffentlicht in: | Experimental cell research 1994-09, Vol.214 (1), p.22-26 |
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| container_title | Experimental cell research |
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| creator | Brysk, Miriam M. Bell, Trace Brysk, Henry Selvanayagam, Peter Rajaraman, Srinivasan |
| description | We have previously described the properties of desquamin, a cell adhesion molecule in the stratum corneum with lectin-like properties specific for amine sugars. We report here that desquamin is also a trypsin-like serine proteinase. It degrades several chromogenic peptides with arginine in the P1 position, with greatest activity for the tissue plasminogen activator peptide; it has no chymotrypsin-like activity. The enzymatic activity of desquamin is inhibited by aprotinin, leupeptin, and soybean trypsin inhibitor. The Km for all active substrates is in the millimole range and the pH for optimal activity is near 10. The enzymatic activity is stable in the temperature range from 37 to 80°C, peaking near the upper end; it is only partially inhibited at 100°C. Using zymogels with immobilized substrates, we show that desquamin degrades both casein and human keratins. Because desquamin is localized to the lipid envelopes of the stratum corneum and can function as an enzyme (and is extremely resistant to chemical and thermal degradation), it is in a position to play a crucial role in desquamation. |
| doi_str_mv | 10.1006/excr.1994.1229 |
| format | Article |
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We report here that desquamin is also a trypsin-like serine proteinase. It degrades several chromogenic peptides with arginine in the P1 position, with greatest activity for the tissue plasminogen activator peptide; it has no chymotrypsin-like activity. The enzymatic activity of desquamin is inhibited by aprotinin, leupeptin, and soybean trypsin inhibitor. The Km for all active substrates is in the millimole range and the pH for optimal activity is near 10. The enzymatic activity is stable in the temperature range from 37 to 80°C, peaking near the upper end; it is only partially inhibited at 100°C. Using zymogels with immobilized substrates, we show that desquamin degrades both casein and human keratins. 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Psychology ; General aspects, investigation methods ; Humans ; Hydrogen-Ion Concentration ; Kinetics ; Molecular Sequence Data ; Serine Endopeptidases - isolation & purification ; Serine Endopeptidases - metabolism ; Skin - enzymology ; Substrate Specificity ; Tissue Plasminogen Activator - antagonists & inhibitors</subject><ispartof>Experimental cell research, 1994-09, Vol.214 (1), p.22-26</ispartof><rights>1994 Academic Press</rights><rights>1994 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c368t-574f577da6c5be5f40f7e49f0b5585d2d67f6ab80ca05c36d48910202dde5e8d3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1006/excr.1994.1229$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>315,781,785,3551,27929,27930,46000</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4245441$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8082725$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Brysk, Miriam M.</creatorcontrib><creatorcontrib>Bell, Trace</creatorcontrib><creatorcontrib>Brysk, Henry</creatorcontrib><creatorcontrib>Selvanayagam, Peter</creatorcontrib><creatorcontrib>Rajaraman, Srinivasan</creatorcontrib><title>Enzymatic Activity of Desquamin</title><title>Experimental cell research</title><addtitle>Exp Cell Res</addtitle><description>We have previously described the properties of desquamin, a cell adhesion molecule in the stratum corneum with lectin-like properties specific for amine sugars. We report here that desquamin is also a trypsin-like serine proteinase. It degrades several chromogenic peptides with arginine in the P1 position, with greatest activity for the tissue plasminogen activator peptide; it has no chymotrypsin-like activity. The enzymatic activity of desquamin is inhibited by aprotinin, leupeptin, and soybean trypsin inhibitor. The Km for all active substrates is in the millimole range and the pH for optimal activity is near 10. The enzymatic activity is stable in the temperature range from 37 to 80°C, peaking near the upper end; it is only partially inhibited at 100°C. Using zymogels with immobilized substrates, we show that desquamin degrades both casein and human keratins. Because desquamin is localized to the lipid envelopes of the stratum corneum and can function as an enzyme (and is extremely resistant to chemical and thermal degradation), it is in a position to play a crucial role in desquamation.</description><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>Cell Adhesion Molecules - isolation & purification</subject><subject>Cell Adhesion Molecules - metabolism</subject><subject>Cell Differentiation</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Epidermis - enzymology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>General aspects, investigation methods</subject><subject>Humans</subject><subject>Hydrogen-Ion Concentration</subject><subject>Kinetics</subject><subject>Molecular Sequence Data</subject><subject>Serine Endopeptidases - isolation & purification</subject><subject>Serine Endopeptidases - metabolism</subject><subject>Skin - enzymology</subject><subject>Substrate Specificity</subject><subject>Tissue Plasminogen Activator - antagonists & inhibitors</subject><issn>0014-4827</issn><issn>1090-2422</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kD1PwzAQhi0EKqWwsiE6ILaEs2snzliV8iFVYoHZcuyzZNQkrZ1WlF9PokbdmE66e97T3UPILYWUAmRP-GNCSouCp5Sx4oyMKRSQMM7YORkDUJ5wyfJLchXjNwBISbMRGUnomkyMyf2y_j1UuvVmOjet3_v2MG3c9BnjdqcrX1-TC6fXEW-GOiFfL8vPxVuy-nh9X8xXiZllsk1Ezp3Ic6szI0oUjoPLkRcOSiGksMxmuct0KcFoEF3EcllQYMCsRYHSzibk8bh3E5rtDmOrKh8Nrte6xmYXVZ7l_X-yA9MjaEITY0CnNsFXOhwUBdUbUb0R1RtRfaIL3A2bd2WF9oQPCrr5wzDX0ei1C7o2Pp4wzrjgnHaYPGLYWdh7DCoaj7VB6wOaVtnG_3fBHwsReuM</recordid><startdate>19940901</startdate><enddate>19940901</enddate><creator>Brysk, Miriam M.</creator><creator>Bell, Trace</creator><creator>Brysk, Henry</creator><creator>Selvanayagam, Peter</creator><creator>Rajaraman, Srinivasan</creator><general>Elsevier Inc</general><general>Elsevier</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>7X8</scope></search><sort><creationdate>19940901</creationdate><title>Enzymatic Activity of Desquamin</title><author>Brysk, Miriam M. ; Bell, Trace ; Brysk, Henry ; Selvanayagam, Peter ; Rajaraman, Srinivasan</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c368t-574f577da6c5be5f40f7e49f0b5585d2d67f6ab80ca05c36d48910202dde5e8d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Biological and medical sciences</topic><topic>Cell Adhesion Molecules - isolation & purification</topic><topic>Cell Adhesion Molecules - metabolism</topic><topic>Cell Differentiation</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Epidermis - enzymology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>General aspects, investigation methods</topic><topic>Humans</topic><topic>Hydrogen-Ion Concentration</topic><topic>Kinetics</topic><topic>Molecular Sequence Data</topic><topic>Serine Endopeptidases - isolation & purification</topic><topic>Serine Endopeptidases - metabolism</topic><topic>Skin - enzymology</topic><topic>Substrate Specificity</topic><topic>Tissue Plasminogen Activator - antagonists & inhibitors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Brysk, Miriam M.</creatorcontrib><creatorcontrib>Bell, Trace</creatorcontrib><creatorcontrib>Brysk, Henry</creatorcontrib><creatorcontrib>Selvanayagam, Peter</creatorcontrib><creatorcontrib>Rajaraman, Srinivasan</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>MEDLINE - Academic</collection><jtitle>Experimental cell research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Brysk, Miriam M.</au><au>Bell, Trace</au><au>Brysk, Henry</au><au>Selvanayagam, Peter</au><au>Rajaraman, Srinivasan</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Enzymatic Activity of Desquamin</atitle><jtitle>Experimental cell research</jtitle><addtitle>Exp Cell Res</addtitle><date>1994-09-01</date><risdate>1994</risdate><volume>214</volume><issue>1</issue><spage>22</spage><epage>26</epage><pages>22-26</pages><issn>0014-4827</issn><eissn>1090-2422</eissn><coden>ECREAL</coden><abstract>We have previously described the properties of desquamin, a cell adhesion molecule in the stratum corneum with lectin-like properties specific for amine sugars. We report here that desquamin is also a trypsin-like serine proteinase. It degrades several chromogenic peptides with arginine in the P1 position, with greatest activity for the tissue plasminogen activator peptide; it has no chymotrypsin-like activity. The enzymatic activity of desquamin is inhibited by aprotinin, leupeptin, and soybean trypsin inhibitor. The Km for all active substrates is in the millimole range and the pH for optimal activity is near 10. The enzymatic activity is stable in the temperature range from 37 to 80°C, peaking near the upper end; it is only partially inhibited at 100°C. Using zymogels with immobilized substrates, we show that desquamin degrades both casein and human keratins. Because desquamin is localized to the lipid envelopes of the stratum corneum and can function as an enzyme (and is extremely resistant to chemical and thermal degradation), it is in a position to play a crucial role in desquamation.</abstract><cop>Orlando, FL</cop><pub>Elsevier Inc</pub><pmid>8082725</pmid><doi>10.1006/excr.1994.1229</doi><tpages>5</tpages></addata></record> |
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| ispartof | Experimental cell research, 1994-09, Vol.214 (1), p.22-26 |
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| subjects | Amino Acid Sequence Analytical, structural and metabolic biochemistry Biological and medical sciences Cell Adhesion Molecules - isolation & purification Cell Adhesion Molecules - metabolism Cell Differentiation Enzymes and enzyme inhibitors Epidermis - enzymology Fundamental and applied biological sciences. Psychology General aspects, investigation methods Humans Hydrogen-Ion Concentration Kinetics Molecular Sequence Data Serine Endopeptidases - isolation & purification Serine Endopeptidases - metabolism Skin - enzymology Substrate Specificity Tissue Plasminogen Activator - antagonists & inhibitors |
| title | Enzymatic Activity of Desquamin |
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