Synthesis of a new cell penetrating calpain inhibitor (calpeptin)
N-terminal of Leu-norleucinal or Leu-methioninal was modified to obtain a cell penetrative peptide inhibitor against calpain. Benzyloxycarbonyl (Z) derivatives had less active against papain than phenylbutyryl derivatives and leupeptin. Z-Leu-nLeu-H (calpeptin) was more sensitive to calpain I than Z...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1988-06, Vol.153 (3), p.1201-1208 |
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| container_end_page | 1208 |
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| container_issue | 3 |
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| container_title | Biochemical and biophysical research communications |
| container_volume | 153 |
| creator | Tsujinaka, Toshimasa Kajiwara, Yuki Kambayashi, Junichi Sakon, Masato Higuchi, Naoki Tanaka, Takaharu Mori, Takesada |
| description | N-terminal of Leu-norleucinal or Leu-methioninal was modified to obtain a cell penetrative peptide inhibitor against calpain. Benzyloxycarbonyl (Z) derivatives had less active against papain than phenylbutyryl derivatives and leupeptin. Z-Leu-nLeu-H (calpeptin) was more sensitive to calpain I than Z-Leu-Met-H and leupeptin. Calpeptin was most potent among synthesized inhibitors in terms of preventing the Ca
2+-ionophore induced degradation of actin binding protein and P235 in intact platelets. After 30 min incubation with intact platelets, calpeptin completely abolished calpain activity in platelets but no effect was observed in case of leupeptin. Calpeptin also inhibited 20K phosphorylation in platelets stimulated by thrombin, ionomycin or collagen. Thus calpeptin was found to be a useful cell-penetrative calpain inhibitor. |
| doi_str_mv | 10.1016/S0006-291X(88)81355-X |
| format | Article |
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2+-ionophore induced degradation of actin binding protein and P235 in intact platelets. After 30 min incubation with intact platelets, calpeptin completely abolished calpain activity in platelets but no effect was observed in case of leupeptin. Calpeptin also inhibited 20K phosphorylation in platelets stimulated by thrombin, ionomycin or collagen. Thus calpeptin was found to be a useful cell-penetrative calpain inhibitor.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/S0006-291X(88)81355-X</identifier><identifier>PMID: 2839170</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Blood Platelets - enzymology ; Blood Platelets - metabolism ; Calcimycin - pharmacology ; Calpain - antagonists & inhibitors ; Cell Membrane Permeability - drug effects ; Dipeptides - chemical synthesis ; Dipeptides - pharmacology ; Leupeptins - pharmacology ; Microfilament Proteins - metabolism ; Papain - antagonists & inhibitors ; Peptides - chemical synthesis ; Peptides - pharmacology ; Swine</subject><ispartof>Biochemical and biophysical research communications, 1988-06, Vol.153 (3), p.1201-1208</ispartof><rights>1988 Academic Press, Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c457t-834b8623ebafb6d50a78fbad2ec79ce0cbaa78593c12dd450ed2460d7a2e344f3</citedby><cites>FETCH-LOGICAL-c457t-834b8623ebafb6d50a78fbad2ec79ce0cbaa78593c12dd450ed2460d7a2e344f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0006291X8881355X$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2839170$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Tsujinaka, Toshimasa</creatorcontrib><creatorcontrib>Kajiwara, Yuki</creatorcontrib><creatorcontrib>Kambayashi, Junichi</creatorcontrib><creatorcontrib>Sakon, Masato</creatorcontrib><creatorcontrib>Higuchi, Naoki</creatorcontrib><creatorcontrib>Tanaka, Takaharu</creatorcontrib><creatorcontrib>Mori, Takesada</creatorcontrib><title>Synthesis of a new cell penetrating calpain inhibitor (calpeptin)</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>N-terminal of Leu-norleucinal or Leu-methioninal was modified to obtain a cell penetrative peptide inhibitor against calpain. Benzyloxycarbonyl (Z) derivatives had less active against papain than phenylbutyryl derivatives and leupeptin. Z-Leu-nLeu-H (calpeptin) was more sensitive to calpain I than Z-Leu-Met-H and leupeptin. Calpeptin was most potent among synthesized inhibitors in terms of preventing the Ca
2+-ionophore induced degradation of actin binding protein and P235 in intact platelets. After 30 min incubation with intact platelets, calpeptin completely abolished calpain activity in platelets but no effect was observed in case of leupeptin. Calpeptin also inhibited 20K phosphorylation in platelets stimulated by thrombin, ionomycin or collagen. Thus calpeptin was found to be a useful cell-penetrative calpain inhibitor.</description><subject>Animals</subject><subject>Blood Platelets - enzymology</subject><subject>Blood Platelets - metabolism</subject><subject>Calcimycin - pharmacology</subject><subject>Calpain - antagonists & inhibitors</subject><subject>Cell Membrane Permeability - drug effects</subject><subject>Dipeptides - chemical synthesis</subject><subject>Dipeptides - pharmacology</subject><subject>Leupeptins - pharmacology</subject><subject>Microfilament Proteins - metabolism</subject><subject>Papain - antagonists & inhibitors</subject><subject>Peptides - chemical synthesis</subject><subject>Peptides - pharmacology</subject><subject>Swine</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1988</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkEtLw0AQxxdRaq1-hEJO0h6is48km5NI8QUFD1XobdnsTuxKm8TdVOm3N33Qa08D_8fM8CNkSOGOAk3vZwCQxiyn85GUY0l5ksTzM9KnkEPMKIhz0j9GLslVCN8AlIo075EekzynGfTJ42xTtQsMLkR1Gemowr_I4HIZNVhh63Xrqq_I6GWjXRW5auEK19Y-Gm0lbDp3fE0uSr0MeHOYA_L5_PQxeY2n7y9vk8dpbESStbHkopAp41joskhtAjqTZaEtQ5PlBsEUulOSnBvKrBUJoGUiBZtphlyIkg_I7X5v4-ufNYZWrVzYvqorrNdBZZKDSBk9GaQJpJxT0QWTfdD4OgSPpWq8W2m_URTUlrHaMVZbgEpKtWOs5l1veDiwLlZoj60D1M5_2PvY4fh16FUwDiuD1nk0rbK1O3HhHwLQjE0</recordid><startdate>19880630</startdate><enddate>19880630</enddate><creator>Tsujinaka, Toshimasa</creator><creator>Kajiwara, Yuki</creator><creator>Kambayashi, Junichi</creator><creator>Sakon, Masato</creator><creator>Higuchi, Naoki</creator><creator>Tanaka, Takaharu</creator><creator>Mori, Takesada</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>7QP</scope><scope>7X8</scope></search><sort><creationdate>19880630</creationdate><title>Synthesis of a new cell penetrating calpain inhibitor (calpeptin)</title><author>Tsujinaka, Toshimasa ; Kajiwara, Yuki ; Kambayashi, Junichi ; Sakon, Masato ; Higuchi, Naoki ; Tanaka, Takaharu ; Mori, Takesada</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c457t-834b8623ebafb6d50a78fbad2ec79ce0cbaa78593c12dd450ed2460d7a2e344f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1988</creationdate><topic>Animals</topic><topic>Blood Platelets - enzymology</topic><topic>Blood Platelets - metabolism</topic><topic>Calcimycin - pharmacology</topic><topic>Calpain - antagonists & inhibitors</topic><topic>Cell Membrane Permeability - drug effects</topic><topic>Dipeptides - chemical synthesis</topic><topic>Dipeptides - pharmacology</topic><topic>Leupeptins - pharmacology</topic><topic>Microfilament Proteins - metabolism</topic><topic>Papain - antagonists & inhibitors</topic><topic>Peptides - chemical synthesis</topic><topic>Peptides - pharmacology</topic><topic>Swine</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tsujinaka, Toshimasa</creatorcontrib><creatorcontrib>Kajiwara, Yuki</creatorcontrib><creatorcontrib>Kambayashi, Junichi</creatorcontrib><creatorcontrib>Sakon, Masato</creatorcontrib><creatorcontrib>Higuchi, Naoki</creatorcontrib><creatorcontrib>Tanaka, Takaharu</creatorcontrib><creatorcontrib>Mori, Takesada</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Calcium & Calcified Tissue Abstracts</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>Tsujinaka, Toshimasa</au><au>Kajiwara, Yuki</au><au>Kambayashi, Junichi</au><au>Sakon, Masato</au><au>Higuchi, Naoki</au><au>Tanaka, Takaharu</au><au>Mori, Takesada</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Synthesis of a new cell penetrating calpain inhibitor (calpeptin)</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1988-06-30</date><risdate>1988</risdate><volume>153</volume><issue>3</issue><spage>1201</spage><epage>1208</epage><pages>1201-1208</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>N-terminal of Leu-norleucinal or Leu-methioninal was modified to obtain a cell penetrative peptide inhibitor against calpain. 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2+-ionophore induced degradation of actin binding protein and P235 in intact platelets. After 30 min incubation with intact platelets, calpeptin completely abolished calpain activity in platelets but no effect was observed in case of leupeptin. Calpeptin also inhibited 20K phosphorylation in platelets stimulated by thrombin, ionomycin or collagen. Thus calpeptin was found to be a useful cell-penetrative calpain inhibitor.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>2839170</pmid><doi>10.1016/S0006-291X(88)81355-X</doi><tpages>8</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-291X |
| ispartof | Biochemical and biophysical research communications, 1988-06, Vol.153 (3), p.1201-1208 |
| issn | 0006-291X 1090-2104 |
| language | eng |
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| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Animals Blood Platelets - enzymology Blood Platelets - metabolism Calcimycin - pharmacology Calpain - antagonists & inhibitors Cell Membrane Permeability - drug effects Dipeptides - chemical synthesis Dipeptides - pharmacology Leupeptins - pharmacology Microfilament Proteins - metabolism Papain - antagonists & inhibitors Peptides - chemical synthesis Peptides - pharmacology Swine |
| title | Synthesis of a new cell penetrating calpain inhibitor (calpeptin) |
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