Degradation of the Cleaved Leader Peptide of Thiolase by a Peroxisomal Proteinase
A peroxisomal location for insulin-degrading enzyme (IDE) has been defined by confocal immunofluorescence microscopy of stably transfected CHO cells overexpressing IDE and digitonin-permeabilization studies in normal nontransfected fibroblasts. The functional significance of IDE in degrading cleaved...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1995-04, Vol.92 (9), p.3859-3863 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Authier, François John J. M. Bergeron Ou, Wei-Jia Rachubinski, Richard A. Posner, Barry I. Walton, Paul A. |
| description | A peroxisomal location for insulin-degrading enzyme (IDE) has been defined by confocal immunofluorescence microscopy of stably transfected CHO cells overexpressing IDE and digitonin-permeabilization studies in normal nontransfected fibroblasts. The functional significance of IDE in degrading cleaved leader peptides of peroxisomal proteins targeted by the type II motif was evaluated with a synthetic peptide corresponding to the type II leader peptide of prethiolase. The peptide effectively competed for degradation and cross-linking of the high-affinity substrate125I-labeled insulin to IDE. Direct proteolysis of the leader peptide of prethiolase was confirmed by HPLC; degradation was inhibited by immunodepletion with an antibody to IDE. Phylogenetic analysis of proteinases related to IDE revealed sequence similarity to mitochondrial processing peptidases. |
| doi_str_mv | 10.1073/pnas.92.9.3859 |
| format | Article |
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M. Bergeron ; Ou, Wei-Jia ; Rachubinski, Richard A. ; Posner, Barry I. ; Walton, Paul A.</creator><creatorcontrib>Authier, François ; John J. M. Bergeron ; Ou, Wei-Jia ; Rachubinski, Richard A. ; Posner, Barry I. ; Walton, Paul A.</creatorcontrib><description>A peroxisomal location for insulin-degrading enzyme (IDE) has been defined by confocal immunofluorescence microscopy of stably transfected CHO cells overexpressing IDE and digitonin-permeabilization studies in normal nontransfected fibroblasts. The functional significance of IDE in degrading cleaved leader peptides of peroxisomal proteins targeted by the type II motif was evaluated with a synthetic peptide corresponding to the type II leader peptide of prethiolase. The peptide effectively competed for degradation and cross-linking of the high-affinity substrate125I-labeled insulin to IDE. Direct proteolysis of the leader peptide of prethiolase was confirmed by HPLC; degradation was inhibited by immunodepletion with an antibody to IDE. Phylogenetic analysis of proteinases related to IDE revealed sequence similarity to mitochondrial processing peptidases.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.92.9.3859</identifier><identifier>PMID: 7731996</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>Acetyl-CoA C-Acetyltransferase - biosynthesis ; Acetyl-CoA C-Acetyltransferase - metabolism ; Amino Acid Sequence ; Animals ; Antibodies ; Cell Line ; Cellular biology ; CHO Cells ; Cricetinae ; Endopeptidases - biosynthesis ; Endopeptidases - genetics ; Endopeptidases - metabolism ; Enzymes ; Fibroblasts ; Insulin ; Liver ; Liver - enzymology ; Microbodies - enzymology ; Mitochondria - enzymology ; Molecular Sequence Data ; Peptides ; Peptides - chemical synthesis ; Peptides - immunology ; Peroxisomes ; Phylogenetics ; Phylogeny ; Protein precursors ; Protein Processing, Post-Translational ; Protein Sorting Signals - metabolism ; Proteins ; Rats ; Recombinant Proteins - biosynthesis ; Recombinant Proteins - metabolism ; Transfection</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1995-04, Vol.92 (9), p.3859-3863</ispartof><rights>Copyright 1995 The National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Apr 25, 1995</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c550t-209dc30098d028aa33434fd75e9979aef8f15254d30979ff66748cfad10646f23</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/92/9.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2367446$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2367446$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,724,777,781,800,882,27905,27906,53772,53774,57998,58231</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7731996$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Authier, François</creatorcontrib><creatorcontrib>John J. 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The peptide effectively competed for degradation and cross-linking of the high-affinity substrate125I-labeled insulin to IDE. Direct proteolysis of the leader peptide of prethiolase was confirmed by HPLC; degradation was inhibited by immunodepletion with an antibody to IDE. Phylogenetic analysis of proteinases related to IDE revealed sequence similarity to mitochondrial processing peptidases.</description><subject>Acetyl-CoA C-Acetyltransferase - biosynthesis</subject><subject>Acetyl-CoA C-Acetyltransferase - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antibodies</subject><subject>Cell Line</subject><subject>Cellular biology</subject><subject>CHO Cells</subject><subject>Cricetinae</subject><subject>Endopeptidases - biosynthesis</subject><subject>Endopeptidases - genetics</subject><subject>Endopeptidases - metabolism</subject><subject>Enzymes</subject><subject>Fibroblasts</subject><subject>Insulin</subject><subject>Liver</subject><subject>Liver - enzymology</subject><subject>Microbodies - enzymology</subject><subject>Mitochondria - enzymology</subject><subject>Molecular Sequence Data</subject><subject>Peptides</subject><subject>Peptides - chemical synthesis</subject><subject>Peptides - immunology</subject><subject>Peroxisomes</subject><subject>Phylogenetics</subject><subject>Phylogeny</subject><subject>Protein precursors</subject><subject>Protein Processing, Post-Translational</subject><subject>Protein Sorting Signals - metabolism</subject><subject>Proteins</subject><subject>Rats</subject><subject>Recombinant Proteins - biosynthesis</subject><subject>Recombinant Proteins - metabolism</subject><subject>Transfection</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkc9rFDEcxYModa1ePSkMHrzNNL8mmYAXWX8VFlqhnkM6-aY7S3ayJpnS_vdm2HVZi6cQ3uc9XvIQektwQ7BkF7vRpEbRRjWsa9UztCBYkVpwhZ-jBcZU1h2n_CV6ldIGY6zaDp-hMykZUUos0M8vcBeNNXkIYxVclddQLT2Ye7DVCoyFWF3DLg8WZvVmPQRvElS3j5UpQgwPQwpb46vrGDIMpQu8Ri-c8QneHM5z9Ovb15vlj3p19f1y-XlV922Lc02xsj0rhTqLaWcMY5xxZ2ULSkllwHWOtLTlluFyd04IybveGUuw4MJRdo4-7XN30-0WbA9jjsbrXRy2Jj7qYAb9rzIOa30X7jWnWJBi_3iwx_B7gpT1dkg9eG9GCFPSUlJOpBAF_PAE3IQpjuVpmmJCZavaOa3ZQ30MKUVwxx4E63knPe-kFdVKzzsVw_vT9kf8MMxJvdn3Vz36tZu8z_CQT4L-Cxb93V7fpBziEaCs_CcX7A-2wq-B</recordid><startdate>19950425</startdate><enddate>19950425</enddate><creator>Authier, François</creator><creator>John J. 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| subjects | Acetyl-CoA C-Acetyltransferase - biosynthesis Acetyl-CoA C-Acetyltransferase - metabolism Amino Acid Sequence Animals Antibodies Cell Line Cellular biology CHO Cells Cricetinae Endopeptidases - biosynthesis Endopeptidases - genetics Endopeptidases - metabolism Enzymes Fibroblasts Insulin Liver Liver - enzymology Microbodies - enzymology Mitochondria - enzymology Molecular Sequence Data Peptides Peptides - chemical synthesis Peptides - immunology Peroxisomes Phylogenetics Phylogeny Protein precursors Protein Processing, Post-Translational Protein Sorting Signals - metabolism Proteins Rats Recombinant Proteins - biosynthesis Recombinant Proteins - metabolism Transfection |
| title | Degradation of the Cleaved Leader Peptide of Thiolase by a Peroxisomal Proteinase |
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