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dc.contributor.authorCole, Elisabeth B.
dc.contributor.authorMiller, David M.
dc.contributor.authorRometo, David
dc.contributor.authorGreenberg, Robert M.
dc.contributor.authorBromme, Dieter
dc.contributor.authorCataltepe, Sule
dc.contributor.authorPak, Stephen C.
dc.contributor.authorMills, David R.
dc.contributor.authorSilverman, Gary A.
dc.contributor.authorLuke, Cliff J.
dc.date2022-08-11T08:08:53.000
dc.date.accessioned2022-08-23T16:11:05Z
dc.date.available2022-08-23T16:11:05Z
dc.date.issued2004-09-21
dc.date.submitted2009-07-16
dc.identifier.citation<p>Biochemistry. 2004 Sep 21;43(37):11750-9.</p>
dc.identifier.issn0006-2960
dc.identifier.doi10.1021/bi049020u
dc.identifier.pmid15362859
dc.identifier.urihttp://hdl.handle.net/20.500.14038/33083
dc.description.abstractDelineating the phylogenetic relationships among members of a protein family can provide a high degree of insight into the evolution of domain structure and function relationships. To identify an early metazoan member of the high molecular weight serine proteinase inhibitor (serpin) superfamily, we initiated a cDNA library screen of the cnidarian, Cyanea capillata. We identified one serpin cDNA encoding for a full-length serpin, jellypin. Phylogenetic analysis using the deduced amino acid sequence showed that jellypin was most similar to the platyhelminthe Echinococcus multiocularis serpin and the clade P serpins, suggesting that this serpin evolved approximately 1000 million years ago (MYA). Modeling of jellypin showed that it contained all the functional elements of an inhibitory serpin. In vitro biochemical analysis confirmed that jellypin was an inhibitor of the S1 clan SA family of serine proteinases. Analysis of the interactions between the human serine proteinases, chymotrypsin, cathepsin G, and elastase, showed that jellypin inhibited these enzymes in the classical serpin manner, forming a SDS stable enzyme/inhibitor complex. These data suggest that the coevolution of serpin structure and inhibitory function date back to at least early metazoan evolution, approximately 1000 MYA.
dc.language.isoen_US
dc.publisherAmerican Chemical Society
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=15362859&dopt=Abstract">Link to article in PubMed</a></p>
dc.relation.urlhttps://doi.org/10.1021/bi049020u/
dc.subjectAmino Acid Sequence; Animals; Cloning, Molecular; Gene Library; Humans; Molecular Sequence Data; Phylogeny; Protein Denaturation; Scyphozoa; Sequence Alignment; Serpins
dc.subjectBiochemistry, Biophysics, and Structural Biology
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleIdentification and activity of a lower eukaryotic serine proteinase inhibitor (serpin) from Cyanea capillata: analysis of a jellyfish serpin, jellypin
dc.typeJournal Article
dc.source.journaltitleBiochemistry
dc.source.volume43
dc.source.issue37
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/1628
dc.identifier.contextkey901817
html.description.abstract<p>Delineating the phylogenetic relationships among members of a protein family can provide a high degree of insight into the evolution of domain structure and function relationships. To identify an early metazoan member of the high molecular weight serine proteinase inhibitor (serpin) superfamily, we initiated a cDNA library screen of the cnidarian, Cyanea capillata. We identified one serpin cDNA encoding for a full-length serpin, jellypin. Phylogenetic analysis using the deduced amino acid sequence showed that jellypin was most similar to the platyhelminthe Echinococcus multiocularis serpin and the clade P serpins, suggesting that this serpin evolved approximately 1000 million years ago (MYA). Modeling of jellypin showed that it contained all the functional elements of an inhibitory serpin. In vitro biochemical analysis confirmed that jellypin was an inhibitor of the S1 clan SA family of serine proteinases. Analysis of the interactions between the human serine proteinases, chymotrypsin, cathepsin G, and elastase, showed that jellypin inhibited these enzymes in the classical serpin manner, forming a SDS stable enzyme/inhibitor complex. These data suggest that the coevolution of serpin structure and inhibitory function date back to at least early metazoan evolution, approximately 1000 MYA.</p>
dc.identifier.submissionpathgsbs_sp/1628
dc.contributor.studentDavid M. Miller


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