Low molecular weight inhibitors of cathepsins B, H and T in human serum, synovial fluid and CSF
When human plasma was chromatographed on a Sephadex G-75 column, cathepsin B inhibitors with molecular weights of 80,000 and 13,000 were eluted. The high molecular weight peak (TPI-H) contained α-thiol proteinase inhibitor and haptoglobin, both of which inhibited cathepsins B and H. The low molecula...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1982-10, Vol.108 (4), p.1581-1587 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Lenney, James F. Liao, John Rose Sugg, Sonia L. Gopalakrishnan, Vijaya Wong, Henry C.H. Ouye, Keith H. Chan, Paul W.H. |
| description | When human plasma was chromatographed on a Sephadex G-75 column, cathepsin B inhibitors with molecular weights of 80,000 and 13,000 were eluted. The high molecular weight peak (TPI-H) contained α-thiol proteinase inhibitor and haptoglobin, both of which inhibited cathepsins B and H. The low molecular weight peak (TPI-L) inhibited cathepsins B, H and T, but had little or no activity against papain, ficin or bromelain. TPI-L from plasma contained two molecular forms of inhibitor, while TPI-L from pooled serum samples contained nine. Serum TPI-L was found to be different from the low molecular weight inhibitors present in lung and many other organs. When rheumatoid synovial fluid was analyzed by gel filtration, the eluate contained TPI-H and TPI-L. Human cerebrospinal fluid eluates contained TPI-L, but not TPI-H. |
| doi_str_mv | 10.1016/S0006-291X(82)80088-0 |
| format | Article |
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The high molecular weight peak (TPI-H) contained α-thiol proteinase inhibitor and haptoglobin, both of which inhibited cathepsins B and H. The low molecular weight peak (TPI-L) inhibited cathepsins B, H and T, but had little or no activity against papain, ficin or bromelain. TPI-L from plasma contained two molecular forms of inhibitor, while TPI-L from pooled serum samples contained nine. Serum TPI-L was found to be different from the low molecular weight inhibitors present in lung and many other organs. When rheumatoid synovial fluid was analyzed by gel filtration, the eluate contained TPI-H and TPI-L. Human cerebrospinal fluid eluates contained TPI-L, but not TPI-H.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/S0006-291X(82)80088-0</identifier><identifier>PMID: 7181908</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Cathepsin B ; Cathepsin H ; Cathepsins - antagonists & inhibitors ; cerebrospinal fluid ; Cysteine Endopeptidases ; cysteine proteinase inhibitor ; Humans ; Kidney - enzymology ; Liver - enzymology ; man ; Molecular Weight ; purification ; Rats ; serum ; synovial fluid ; Synovial Fluid - analysis ; Trypsin - cerebrospinal fluid ; Trypsin - metabolism ; Trypsin Inhibitors - blood ; Trypsin Inhibitors - isolation & purification</subject><ispartof>Biochemical and biophysical research communications, 1982-10, Vol.108 (4), p.1581-1587</ispartof><rights>1982 Academic Press, Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c306t-ad20e65ed3af55b7bea430f160b6f0a83788a4a1e09795cd1cc9ce79da04bc5d3</citedby><cites>FETCH-LOGICAL-c306t-ad20e65ed3af55b7bea430f160b6f0a83788a4a1e09795cd1cc9ce79da04bc5d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0006-291X(82)80088-0$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,778,782,3539,27911,27912,45982</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7181908$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lenney, James F.</creatorcontrib><creatorcontrib>Liao, John Rose</creatorcontrib><creatorcontrib>Sugg, Sonia L.</creatorcontrib><creatorcontrib>Gopalakrishnan, Vijaya</creatorcontrib><creatorcontrib>Wong, Henry C.H.</creatorcontrib><creatorcontrib>Ouye, Keith H.</creatorcontrib><creatorcontrib>Chan, Paul W.H.</creatorcontrib><title>Low molecular weight inhibitors of cathepsins B, H and T in human serum, synovial fluid and CSF</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>When human plasma was chromatographed on a Sephadex G-75 column, cathepsin B inhibitors with molecular weights of 80,000 and 13,000 were eluted. The high molecular weight peak (TPI-H) contained α-thiol proteinase inhibitor and haptoglobin, both of which inhibited cathepsins B and H. The low molecular weight peak (TPI-L) inhibited cathepsins B, H and T, but had little or no activity against papain, ficin or bromelain. TPI-L from plasma contained two molecular forms of inhibitor, while TPI-L from pooled serum samples contained nine. Serum TPI-L was found to be different from the low molecular weight inhibitors present in lung and many other organs. When rheumatoid synovial fluid was analyzed by gel filtration, the eluate contained TPI-H and TPI-L. Human cerebrospinal fluid eluates contained TPI-L, but not TPI-H.</description><subject>Animals</subject><subject>Cathepsin B</subject><subject>Cathepsin H</subject><subject>Cathepsins - antagonists & inhibitors</subject><subject>cerebrospinal fluid</subject><subject>Cysteine Endopeptidases</subject><subject>cysteine proteinase inhibitor</subject><subject>Humans</subject><subject>Kidney - enzymology</subject><subject>Liver - enzymology</subject><subject>man</subject><subject>Molecular Weight</subject><subject>purification</subject><subject>Rats</subject><subject>serum</subject><subject>synovial fluid</subject><subject>Synovial Fluid - analysis</subject><subject>Trypsin - cerebrospinal fluid</subject><subject>Trypsin - metabolism</subject><subject>Trypsin Inhibitors - blood</subject><subject>Trypsin Inhibitors - isolation & purification</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1982</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtLxDAUhYMoOj5-gpCVKFi9aZo2XYkOvmDAhQruQprcOpG2GZN2xH9vnRncurqL85174BxCjhlcMGD55TMA5ElasrdTmZ5JACkT2CITBiUkKYNsm0z-kD2yH-MHAGNZXu6S3YJJVoKcEDXzX7T1DZqh0YF-oXuf99R1c1e53odIfU2N7ue4iK6L9OacPlDdWfoyMnQ-tLqjEcPQntP43fml0w2tm8HZFTR9vjskO7VuIh5t7gF5vbt9mT4ks6f7x-n1LDEc8j7RNgXMBVquayGqokKdcahZDlVeg5a8kFJnmiGURSmMZcaUBovSasgqIyw_ICfrv4vgPweMvWpdNNg0ukM_RCUhzVLOxb8gEwJ4KvkIijVogo8xYK0WwbU6fCsG6ncBtVpA_darZKpWCygYfcebgKFq0f65NpWP-tVax7GOpcOgonHYGbQuoOmV9e6fhB-jC5WK</recordid><startdate>19821029</startdate><enddate>19821029</enddate><creator>Lenney, James F.</creator><creator>Liao, John Rose</creator><creator>Sugg, Sonia L.</creator><creator>Gopalakrishnan, Vijaya</creator><creator>Wong, Henry C.H.</creator><creator>Ouye, Keith H.</creator><creator>Chan, Paul W.H.</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>7QL</scope><scope>7TK</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>19821029</creationdate><title>Low molecular weight inhibitors of cathepsins B, H and T in human serum, synovial fluid and CSF</title><author>Lenney, James F. ; Liao, John Rose ; Sugg, Sonia L. ; Gopalakrishnan, Vijaya ; Wong, Henry C.H. ; Ouye, Keith H. ; Chan, Paul W.H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c306t-ad20e65ed3af55b7bea430f160b6f0a83788a4a1e09795cd1cc9ce79da04bc5d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1982</creationdate><topic>Animals</topic><topic>Cathepsin B</topic><topic>Cathepsin H</topic><topic>Cathepsins - antagonists & inhibitors</topic><topic>cerebrospinal fluid</topic><topic>Cysteine Endopeptidases</topic><topic>cysteine proteinase inhibitor</topic><topic>Humans</topic><topic>Kidney - enzymology</topic><topic>Liver - enzymology</topic><topic>man</topic><topic>Molecular Weight</topic><topic>purification</topic><topic>Rats</topic><topic>serum</topic><topic>synovial fluid</topic><topic>Synovial Fluid - analysis</topic><topic>Trypsin - cerebrospinal fluid</topic><topic>Trypsin - metabolism</topic><topic>Trypsin Inhibitors - blood</topic><topic>Trypsin Inhibitors - isolation & purification</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lenney, James F.</creatorcontrib><creatorcontrib>Liao, John Rose</creatorcontrib><creatorcontrib>Sugg, Sonia L.</creatorcontrib><creatorcontrib>Gopalakrishnan, Vijaya</creatorcontrib><creatorcontrib>Wong, Henry C.H.</creatorcontrib><creatorcontrib>Ouye, Keith H.</creatorcontrib><creatorcontrib>Chan, Paul W.H.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Neurosciences Abstracts</collection><collection>Environmental Sciences and Pollution Management</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>Lenney, James F.</au><au>Liao, John Rose</au><au>Sugg, Sonia L.</au><au>Gopalakrishnan, Vijaya</au><au>Wong, Henry C.H.</au><au>Ouye, Keith H.</au><au>Chan, Paul W.H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Low molecular weight inhibitors of cathepsins B, H and T in human serum, synovial fluid and CSF</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1982-10-29</date><risdate>1982</risdate><volume>108</volume><issue>4</issue><spage>1581</spage><epage>1587</epage><pages>1581-1587</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>When human plasma was chromatographed on a Sephadex G-75 column, cathepsin B inhibitors with molecular weights of 80,000 and 13,000 were eluted. The high molecular weight peak (TPI-H) contained α-thiol proteinase inhibitor and haptoglobin, both of which inhibited cathepsins B and H. The low molecular weight peak (TPI-L) inhibited cathepsins B, H and T, but had little or no activity against papain, ficin or bromelain. TPI-L from plasma contained two molecular forms of inhibitor, while TPI-L from pooled serum samples contained nine. Serum TPI-L was found to be different from the low molecular weight inhibitors present in lung and many other organs. When rheumatoid synovial fluid was analyzed by gel filtration, the eluate contained TPI-H and TPI-L. Human cerebrospinal fluid eluates contained TPI-L, but not TPI-H.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>7181908</pmid><doi>10.1016/S0006-291X(82)80088-0</doi><tpages>7</tpages></addata></record> |
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| source | Elsevier ScienceDirect Journals Complete - AutoHoldings; MEDLINE |
| subjects | Animals Cathepsin B Cathepsin H Cathepsins - antagonists & inhibitors cerebrospinal fluid Cysteine Endopeptidases cysteine proteinase inhibitor Humans Kidney - enzymology Liver - enzymology man Molecular Weight purification Rats serum synovial fluid Synovial Fluid - analysis Trypsin - cerebrospinal fluid Trypsin - metabolism Trypsin Inhibitors - blood Trypsin Inhibitors - isolation & purification |
| title | Low molecular weight inhibitors of cathepsins B, H and T in human serum, synovial fluid and CSF |
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