MS-271, a novel inhibitor of calmodulin-activated myosin light chain kinase from Streptomyces sp.—I. isolation, structural determination and biological properties of MS-271
A novel cyclic peptide, MS-271, was isolated from the culture broth of an actinomycete, Streptomyces sp. M-271 as an inhibitor of smooth muscle myosin light chain kinase (MLCK). MS-271 inhibited the MLCK from chicken gizzard with an IC 50, value of 8 μM. MS-271 did not inhibit cyclic AMP-dependent p...
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| Veröffentlicht in: | Bioorganic & medicinal chemistry 1996, Vol.4 (1), p.115-120 |
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| container_title | Bioorganic & medicinal chemistry |
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| creator | Yano, Keiichi Toki, Shinichiro Nakanishi, Satoshi Ochiai, Keiko Ando, Katsuhiko Yoshida, Mayumi Matsuda, Yuzuru Yamasaki, Motoo |
| description | A novel cyclic peptide, MS-271, was isolated from the culture broth of an actinomycete,
Streptomyces sp. M-271 as an inhibitor of smooth muscle myosin light chain kinase (MLCK). MS-271 inhibited the MLCK from chicken gizzard with an IC
50, value of 8 μM. MS-271 did not inhibit cyclic AMP-dependent protein kinase, protein kinase C or calcium/calmodulin-dependent cyclic nucleotide phosphodiesterase at concentrations up to 400 μM. The primary structure of MS-271 was identical to that of siamycin I, an anti-HIV peptide isolated from a microbial source.
A novel cyclic peptide, MS-271, was isolated from the culture broth of an actinomycete,
Streptomyces sp. M-271 as an inhibitor of smooth muscle myosin light chain kinase (MLCK). MS-271 inhibited the MLCK from chicken gizzard with an IC
50 value of 8 μM, MS-271 did not inhibit cyclic AMP-dependent protein kinase, protein kinase C or calcium/calmodulin-dependent cyclic nucleotide phosphodiesterase at concentrations up to 400 μM. The primary structure of MS-271 was identical to that of siamycin I, an anti-HIV peptide isolated from a microbial source. |
| doi_str_mv | 10.1016/0968-0896(95)00175-1 |
| format | Article |
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Streptomyces sp. M-271 as an inhibitor of smooth muscle myosin light chain kinase (MLCK). MS-271 inhibited the MLCK from chicken gizzard with an IC
50, value of 8 μM. MS-271 did not inhibit cyclic AMP-dependent protein kinase, protein kinase C or calcium/calmodulin-dependent cyclic nucleotide phosphodiesterase at concentrations up to 400 μM. The primary structure of MS-271 was identical to that of siamycin I, an anti-HIV peptide isolated from a microbial source.
A novel cyclic peptide, MS-271, was isolated from the culture broth of an actinomycete,
Streptomyces sp. M-271 as an inhibitor of smooth muscle myosin light chain kinase (MLCK). MS-271 inhibited the MLCK from chicken gizzard with an IC
50 value of 8 μM, MS-271 did not inhibit cyclic AMP-dependent protein kinase, protein kinase C or calcium/calmodulin-dependent cyclic nucleotide phosphodiesterase at concentrations up to 400 μM. The primary structure of MS-271 was identical to that of siamycin I, an anti-HIV peptide isolated from a microbial source.</description><identifier>ISSN: 0968-0896</identifier><identifier>EISSN: 1464-3391</identifier><identifier>DOI: 10.1016/0968-0896(95)00175-1</identifier><identifier>PMID: 8689231</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Adenosine Triphosphate - metabolism ; AIDS/HIV ; Amino Acid Sequence ; Amino Acids - analysis ; Animals ; Anti-Bacterial Agents ; anti-HIV ; Antifungal Agents ; Cattle ; Chickens ; Cyclic AMP-Dependent Protein Kinases - antagonists & inhibitors ; Enzyme Inhibitors - chemistry ; Enzyme Inhibitors - isolation & purification ; Enzyme Inhibitors - pharmacology ; Fermentation ; inhibitor ; Microbial Sensitivity Tests ; Molecular Sequence Data ; Myosin light chain kinase ; Myosin-Light-Chain Kinase - antagonists & inhibitors ; Peptides, Cyclic - biosynthesis ; Peptides, Cyclic - chemistry ; Peptides, Cyclic - isolation & purification ; Peptides, Cyclic - pharmacology ; primary structure ; Rats ; Streptomyces ; Streptomyces - chemistry ; Streptomyces - metabolism</subject><ispartof>Bioorganic & medicinal chemistry, 1996, Vol.4 (1), p.115-120</ispartof><rights>1996</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c338t-aebac3a9cc5a83efea9eb5dd58075d412b6353f2caa4f978e856876cf74ef8903</citedby><cites>FETCH-LOGICAL-c338t-aebac3a9cc5a83efea9eb5dd58075d412b6353f2caa4f978e856876cf74ef8903</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0968089695001751$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,4010,27900,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8689231$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yano, Keiichi</creatorcontrib><creatorcontrib>Toki, Shinichiro</creatorcontrib><creatorcontrib>Nakanishi, Satoshi</creatorcontrib><creatorcontrib>Ochiai, Keiko</creatorcontrib><creatorcontrib>Ando, Katsuhiko</creatorcontrib><creatorcontrib>Yoshida, Mayumi</creatorcontrib><creatorcontrib>Matsuda, Yuzuru</creatorcontrib><creatorcontrib>Yamasaki, Motoo</creatorcontrib><title>MS-271, a novel inhibitor of calmodulin-activated myosin light chain kinase from Streptomyces sp.—I. isolation, structural determination and biological properties of MS-271</title><title>Bioorganic & medicinal chemistry</title><addtitle>Bioorg Med Chem</addtitle><description>A novel cyclic peptide, MS-271, was isolated from the culture broth of an actinomycete,
Streptomyces sp. M-271 as an inhibitor of smooth muscle myosin light chain kinase (MLCK). MS-271 inhibited the MLCK from chicken gizzard with an IC
50, value of 8 μM. MS-271 did not inhibit cyclic AMP-dependent protein kinase, protein kinase C or calcium/calmodulin-dependent cyclic nucleotide phosphodiesterase at concentrations up to 400 μM. The primary structure of MS-271 was identical to that of siamycin I, an anti-HIV peptide isolated from a microbial source.
A novel cyclic peptide, MS-271, was isolated from the culture broth of an actinomycete,
Streptomyces sp. M-271 as an inhibitor of smooth muscle myosin light chain kinase (MLCK). MS-271 inhibited the MLCK from chicken gizzard with an IC
50 value of 8 μM, MS-271 did not inhibit cyclic AMP-dependent protein kinase, protein kinase C or calcium/calmodulin-dependent cyclic nucleotide phosphodiesterase at concentrations up to 400 μM. The primary structure of MS-271 was identical to that of siamycin I, an anti-HIV peptide isolated from a microbial source.</description><subject>Adenosine Triphosphate - metabolism</subject><subject>AIDS/HIV</subject><subject>Amino Acid Sequence</subject><subject>Amino Acids - analysis</subject><subject>Animals</subject><subject>Anti-Bacterial Agents</subject><subject>anti-HIV</subject><subject>Antifungal Agents</subject><subject>Cattle</subject><subject>Chickens</subject><subject>Cyclic AMP-Dependent Protein Kinases - antagonists & inhibitors</subject><subject>Enzyme Inhibitors - chemistry</subject><subject>Enzyme Inhibitors - isolation & purification</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Fermentation</subject><subject>inhibitor</subject><subject>Microbial Sensitivity Tests</subject><subject>Molecular Sequence Data</subject><subject>Myosin light chain kinase</subject><subject>Myosin-Light-Chain Kinase - antagonists & inhibitors</subject><subject>Peptides, Cyclic - biosynthesis</subject><subject>Peptides, Cyclic - chemistry</subject><subject>Peptides, Cyclic - isolation & purification</subject><subject>Peptides, Cyclic - pharmacology</subject><subject>primary structure</subject><subject>Rats</subject><subject>Streptomyces</subject><subject>Streptomyces - chemistry</subject><subject>Streptomyces - metabolism</subject><issn>0968-0896</issn><issn>1464-3391</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9UcuKFDEUDaKM7egfKGQlClNtUqlHshmQwcfAiIvRdUglt6avpiptkmronR_hd_hRfolpu5mlq3vhPO65HEKec7bmjHdvmOpkxaTqXqn2NWO8byv-gKx40zWVEIo_JKt7ymPyJKVvjLG6UfyMnMlOqlrwFfn96baqe35BDZ3DDjzFeYMD5hBpGKk1fgpu8ThXxmbcmQyOTvuQcKYe7zaZ2o0p-3ecTQI6xjDR2xxhm8O0t5Bo2q7__Px1vaaYgjcZw3xBU46LzUs0njrIEKciPiDUzI4OGHy4w3KYbmPYQsxYbEqUY86n5NFofIJnp3lOvr5_9-XqY3Xz-cP11dubygohc2VgMFYYZW1rpIARjIKhda6VrG9dw-uhE60Ya2tMM6pegmw72Xd27BsYpWLinLw8-pYQPxZIWU-YLHhvZghL0r3kXEnZF2JzJNoYUoow6m3EycS95kwfatKHDvShA61a_a8mzYvsxcl_GSZw96JTLwW_POJQntwhRJ0swmzBYQSbtQv4_wN_ASeophc</recordid><startdate>1996</startdate><enddate>1996</enddate><creator>Yano, Keiichi</creator><creator>Toki, Shinichiro</creator><creator>Nakanishi, Satoshi</creator><creator>Ochiai, Keiko</creator><creator>Ando, Katsuhiko</creator><creator>Yoshida, Mayumi</creator><creator>Matsuda, Yuzuru</creator><creator>Yamasaki, Motoo</creator><general>Elsevier Ltd</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>7X8</scope></search><sort><creationdate>1996</creationdate><title>MS-271, a novel inhibitor of calmodulin-activated myosin light chain kinase from Streptomyces sp.—I. isolation, structural determination and biological properties of MS-271</title><author>Yano, Keiichi ; Toki, Shinichiro ; Nakanishi, Satoshi ; Ochiai, Keiko ; Ando, Katsuhiko ; Yoshida, Mayumi ; Matsuda, Yuzuru ; Yamasaki, Motoo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c338t-aebac3a9cc5a83efea9eb5dd58075d412b6353f2caa4f978e856876cf74ef8903</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Adenosine Triphosphate - metabolism</topic><topic>AIDS/HIV</topic><topic>Amino Acid Sequence</topic><topic>Amino Acids - analysis</topic><topic>Animals</topic><topic>Anti-Bacterial Agents</topic><topic>anti-HIV</topic><topic>Antifungal Agents</topic><topic>Cattle</topic><topic>Chickens</topic><topic>Cyclic AMP-Dependent Protein Kinases - antagonists & inhibitors</topic><topic>Enzyme Inhibitors - chemistry</topic><topic>Enzyme Inhibitors - isolation & purification</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>Fermentation</topic><topic>inhibitor</topic><topic>Microbial Sensitivity Tests</topic><topic>Molecular Sequence Data</topic><topic>Myosin light chain kinase</topic><topic>Myosin-Light-Chain Kinase - antagonists & inhibitors</topic><topic>Peptides, Cyclic - biosynthesis</topic><topic>Peptides, Cyclic - chemistry</topic><topic>Peptides, Cyclic - isolation & purification</topic><topic>Peptides, Cyclic - pharmacology</topic><topic>primary structure</topic><topic>Rats</topic><topic>Streptomyces</topic><topic>Streptomyces - chemistry</topic><topic>Streptomyces - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yano, Keiichi</creatorcontrib><creatorcontrib>Toki, Shinichiro</creatorcontrib><creatorcontrib>Nakanishi, Satoshi</creatorcontrib><creatorcontrib>Ochiai, Keiko</creatorcontrib><creatorcontrib>Ando, Katsuhiko</creatorcontrib><creatorcontrib>Yoshida, Mayumi</creatorcontrib><creatorcontrib>Matsuda, Yuzuru</creatorcontrib><creatorcontrib>Yamasaki, Motoo</creatorcontrib><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>Bioorganic & medicinal chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yano, Keiichi</au><au>Toki, Shinichiro</au><au>Nakanishi, Satoshi</au><au>Ochiai, Keiko</au><au>Ando, Katsuhiko</au><au>Yoshida, Mayumi</au><au>Matsuda, Yuzuru</au><au>Yamasaki, Motoo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>MS-271, a novel inhibitor of calmodulin-activated myosin light chain kinase from Streptomyces sp.—I. isolation, structural determination and biological properties of MS-271</atitle><jtitle>Bioorganic & medicinal chemistry</jtitle><addtitle>Bioorg Med Chem</addtitle><date>1996</date><risdate>1996</risdate><volume>4</volume><issue>1</issue><spage>115</spage><epage>120</epage><pages>115-120</pages><issn>0968-0896</issn><eissn>1464-3391</eissn><abstract>A novel cyclic peptide, MS-271, was isolated from the culture broth of an actinomycete,
Streptomyces sp. M-271 as an inhibitor of smooth muscle myosin light chain kinase (MLCK). MS-271 inhibited the MLCK from chicken gizzard with an IC
50, value of 8 μM. MS-271 did not inhibit cyclic AMP-dependent protein kinase, protein kinase C or calcium/calmodulin-dependent cyclic nucleotide phosphodiesterase at concentrations up to 400 μM. The primary structure of MS-271 was identical to that of siamycin I, an anti-HIV peptide isolated from a microbial source.
A novel cyclic peptide, MS-271, was isolated from the culture broth of an actinomycete,
Streptomyces sp. M-271 as an inhibitor of smooth muscle myosin light chain kinase (MLCK). MS-271 inhibited the MLCK from chicken gizzard with an IC
50 value of 8 μM, MS-271 did not inhibit cyclic AMP-dependent protein kinase, protein kinase C or calcium/calmodulin-dependent cyclic nucleotide phosphodiesterase at concentrations up to 400 μM. The primary structure of MS-271 was identical to that of siamycin I, an anti-HIV peptide isolated from a microbial source.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>8689231</pmid><doi>10.1016/0968-0896(95)00175-1</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0968-0896 |
| ispartof | Bioorganic & medicinal chemistry, 1996, Vol.4 (1), p.115-120 |
| issn | 0968-0896 1464-3391 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_78119887 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Adenosine Triphosphate - metabolism AIDS/HIV Amino Acid Sequence Amino Acids - analysis Animals Anti-Bacterial Agents anti-HIV Antifungal Agents Cattle Chickens Cyclic AMP-Dependent Protein Kinases - antagonists & inhibitors Enzyme Inhibitors - chemistry Enzyme Inhibitors - isolation & purification Enzyme Inhibitors - pharmacology Fermentation inhibitor Microbial Sensitivity Tests Molecular Sequence Data Myosin light chain kinase Myosin-Light-Chain Kinase - antagonists & inhibitors Peptides, Cyclic - biosynthesis Peptides, Cyclic - chemistry Peptides, Cyclic - isolation & purification Peptides, Cyclic - pharmacology primary structure Rats Streptomyces Streptomyces - chemistry Streptomyces - metabolism |
| title | MS-271, a novel inhibitor of calmodulin-activated myosin light chain kinase from Streptomyces sp.—I. isolation, structural determination and biological properties of MS-271 |
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