Formyl-Met-Leu-Phe-dependent serine kinase for a 64,000 molecular weight protein of polymorphonuclear leukocytes in a cell-lysate system
In the Triton X-100 treated polymorphonuclear leukocytes (PMN), which were stimulated with formyl-Met-Leu-Phe (FMLP) for 1 min, a 64,000 molecular weight protein (p64) was preferentially phosphorylated by the incubation with [ γ- 32P]ATP in the presence of Mg 2+, but not in the presence of Ca 2+. Ph...
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| Veröffentlicht in: | Cellular signalling 1990, Vol.2 (5), p.471-477 |
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| creator | Koshio, Osamu Mizuno, Satoshi Suzuki, Kazuo |
| description | In the Triton X-100 treated polymorphonuclear leukocytes (PMN), which were stimulated with formyl-Met-Leu-Phe (FMLP) for 1 min, a 64,000 molecular weight protein (p64) was preferentially phosphorylated by the incubation with [
γ-
32P]ATP in the presence of Mg
2+, but not in the presence of Ca
2+. Phosphoamino acid analysis of pp64 revealed that the p64-kinase was a serine-specific protein kinase. The p64 was maximally phosphorylated in the first minute, suggesting that the rapid phosphorylation was related to the initial reaction for activation of the FMLP-stimulated PMN functions. The FMLP-stimulated phosphorylation of p64 was slightly inhibited by the addition of cGMP in the reaction mixture. However, addition of cAMP, the cyclic nucleotide-dependent kinase inhibitor (H-8), protein kinase C-inhibitor (H-7) or Ca/calmodulin-dependent kinase inhibitor (W-7), showed no effect on the phosphorylation. These data suggest that phosphorylation of p64 seems to be a novel protein kinase specific to p64. |
| doi_str_mv | 10.1016/0898-6568(90)90043-A |
| format | Article |
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γ-
32P]ATP in the presence of Mg
2+, but not in the presence of Ca
2+. Phosphoamino acid analysis of pp64 revealed that the p64-kinase was a serine-specific protein kinase. The p64 was maximally phosphorylated in the first minute, suggesting that the rapid phosphorylation was related to the initial reaction for activation of the FMLP-stimulated PMN functions. The FMLP-stimulated phosphorylation of p64 was slightly inhibited by the addition of cGMP in the reaction mixture. However, addition of cAMP, the cyclic nucleotide-dependent kinase inhibitor (H-8), protein kinase C-inhibitor (H-7) or Ca/calmodulin-dependent kinase inhibitor (W-7), showed no effect on the phosphorylation. These data suggest that phosphorylation of p64 seems to be a novel protein kinase specific to p64.</description><identifier>ISSN: 0898-6568</identifier><identifier>EISSN: 1873-3913</identifier><identifier>DOI: 10.1016/0898-6568(90)90043-A</identifier><identifier>PMID: 2149031</identifier><language>eng</language><publisher>England: Elsevier Inc</publisher><subject>Adenosine Triphosphate - metabolism ; Blood Proteins - metabolism ; Calcium - metabolism ; Cell-Free System ; chemoattractant-dependent kinase ; Detergents ; Formyl-Met-Leu-Phe ; Humans ; Magnesium - metabolism ; Molecular Weight ; N-Formylmethionine Leucyl-Phenylalanine - pharmacology ; Neutrophils - enzymology ; Octoxynol ; Phosphoproteins - analysis ; Phosphoproteins - metabolism ; Phosphorylation ; Polyethylene Glycols ; polymorphonuclear leukocytes ; Protein Kinase C - antagonists & inhibitors ; Protein Kinases - metabolism ; protein phosphorylation ; Protein-Serine-Threonine Kinases ; serine-kinase ; Triton X-100 lysate</subject><ispartof>Cellular signalling, 1990, Vol.2 (5), p.471-477</ispartof><rights>1990</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c357t-cf773ef254a9d9303aa8fda618bb2b3c06e41b815ceb325d8e1d8171578c04a03</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/089865689090043A$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,4010,27900,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2149031$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Koshio, Osamu</creatorcontrib><creatorcontrib>Mizuno, Satoshi</creatorcontrib><creatorcontrib>Suzuki, Kazuo</creatorcontrib><title>Formyl-Met-Leu-Phe-dependent serine kinase for a 64,000 molecular weight protein of polymorphonuclear leukocytes in a cell-lysate system</title><title>Cellular signalling</title><addtitle>Cell Signal</addtitle><description>In the Triton X-100 treated polymorphonuclear leukocytes (PMN), which were stimulated with formyl-Met-Leu-Phe (FMLP) for 1 min, a 64,000 molecular weight protein (p64) was preferentially phosphorylated by the incubation with [
γ-
32P]ATP in the presence of Mg
2+, but not in the presence of Ca
2+. Phosphoamino acid analysis of pp64 revealed that the p64-kinase was a serine-specific protein kinase. The p64 was maximally phosphorylated in the first minute, suggesting that the rapid phosphorylation was related to the initial reaction for activation of the FMLP-stimulated PMN functions. The FMLP-stimulated phosphorylation of p64 was slightly inhibited by the addition of cGMP in the reaction mixture. However, addition of cAMP, the cyclic nucleotide-dependent kinase inhibitor (H-8), protein kinase C-inhibitor (H-7) or Ca/calmodulin-dependent kinase inhibitor (W-7), showed no effect on the phosphorylation. These data suggest that phosphorylation of p64 seems to be a novel protein kinase specific to p64.</description><subject>Adenosine Triphosphate - metabolism</subject><subject>Blood Proteins - metabolism</subject><subject>Calcium - metabolism</subject><subject>Cell-Free System</subject><subject>chemoattractant-dependent kinase</subject><subject>Detergents</subject><subject>Formyl-Met-Leu-Phe</subject><subject>Humans</subject><subject>Magnesium - metabolism</subject><subject>Molecular Weight</subject><subject>N-Formylmethionine Leucyl-Phenylalanine - pharmacology</subject><subject>Neutrophils - enzymology</subject><subject>Octoxynol</subject><subject>Phosphoproteins - analysis</subject><subject>Phosphoproteins - metabolism</subject><subject>Phosphorylation</subject><subject>Polyethylene Glycols</subject><subject>polymorphonuclear leukocytes</subject><subject>Protein Kinase C - antagonists & inhibitors</subject><subject>Protein Kinases - metabolism</subject><subject>protein phosphorylation</subject><subject>Protein-Serine-Threonine Kinases</subject><subject>serine-kinase</subject><subject>Triton X-100 lysate</subject><issn>0898-6568</issn><issn>1873-3913</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kc9u1DAQxi1EVbaFNwDJJ0QlDOM4f5wL0qqiUGkRHOBsOfaENXXiYDtFeQMemyy76rGnOczvm_nmG0JecnjHgdfvQbaS1VUt37Rw1QKUgm2fkA2XjWCi5eIp2Twgz8hFSr8AeAV1cU7OC162IPiG_L0JcVg8-4KZ7XBm3_bILE44WhwzTRjdiPTOjToh7UOkmtblWwCgQ_BoZq8j_YPu5z7TKYaMbqShp1PwyxDitA_jbDyujMf5LpglY6IroqlB75lfks5I05IyDs_JWa99whenekl-3Hz8fv2Z7b5-ur3e7pgRVZOZ6ZtGYF9UpW5tK0BoLXuray67ruiEgRpL3kleGexEUVmJ3Ere8KqRBkoN4pK8Ps5d_f6eMWU1uHSwo0cMc1ISCgFNzVewPIImhpQi9mqKbtBxURzU4QHqkK46pKtaUP8foLar7NVp_twNaB9Ep8TX_odjH9cj7x1GlYzD0aB1EU1WNrjHF_wDeiuWnQ</recordid><startdate>1990</startdate><enddate>1990</enddate><creator>Koshio, Osamu</creator><creator>Mizuno, Satoshi</creator><creator>Suzuki, Kazuo</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>7X8</scope></search><sort><creationdate>1990</creationdate><title>Formyl-Met-Leu-Phe-dependent serine kinase for a 64,000 molecular weight protein of polymorphonuclear leukocytes in a cell-lysate system</title><author>Koshio, Osamu ; Mizuno, Satoshi ; Suzuki, Kazuo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c357t-cf773ef254a9d9303aa8fda618bb2b3c06e41b815ceb325d8e1d8171578c04a03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>Adenosine Triphosphate - metabolism</topic><topic>Blood Proteins - metabolism</topic><topic>Calcium - metabolism</topic><topic>Cell-Free System</topic><topic>chemoattractant-dependent kinase</topic><topic>Detergents</topic><topic>Formyl-Met-Leu-Phe</topic><topic>Humans</topic><topic>Magnesium - metabolism</topic><topic>Molecular Weight</topic><topic>N-Formylmethionine Leucyl-Phenylalanine - pharmacology</topic><topic>Neutrophils - enzymology</topic><topic>Octoxynol</topic><topic>Phosphoproteins - analysis</topic><topic>Phosphoproteins - metabolism</topic><topic>Phosphorylation</topic><topic>Polyethylene Glycols</topic><topic>polymorphonuclear leukocytes</topic><topic>Protein Kinase C - antagonists & inhibitors</topic><topic>Protein Kinases - metabolism</topic><topic>protein phosphorylation</topic><topic>Protein-Serine-Threonine Kinases</topic><topic>serine-kinase</topic><topic>Triton X-100 lysate</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Koshio, Osamu</creatorcontrib><creatorcontrib>Mizuno, Satoshi</creatorcontrib><creatorcontrib>Suzuki, Kazuo</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>Cellular signalling</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Koshio, Osamu</au><au>Mizuno, Satoshi</au><au>Suzuki, Kazuo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Formyl-Met-Leu-Phe-dependent serine kinase for a 64,000 molecular weight protein of polymorphonuclear leukocytes in a cell-lysate system</atitle><jtitle>Cellular signalling</jtitle><addtitle>Cell Signal</addtitle><date>1990</date><risdate>1990</risdate><volume>2</volume><issue>5</issue><spage>471</spage><epage>477</epage><pages>471-477</pages><issn>0898-6568</issn><eissn>1873-3913</eissn><abstract>In the Triton X-100 treated polymorphonuclear leukocytes (PMN), which were stimulated with formyl-Met-Leu-Phe (FMLP) for 1 min, a 64,000 molecular weight protein (p64) was preferentially phosphorylated by the incubation with [
γ-
32P]ATP in the presence of Mg
2+, but not in the presence of Ca
2+. Phosphoamino acid analysis of pp64 revealed that the p64-kinase was a serine-specific protein kinase. The p64 was maximally phosphorylated in the first minute, suggesting that the rapid phosphorylation was related to the initial reaction for activation of the FMLP-stimulated PMN functions. The FMLP-stimulated phosphorylation of p64 was slightly inhibited by the addition of cGMP in the reaction mixture. However, addition of cAMP, the cyclic nucleotide-dependent kinase inhibitor (H-8), protein kinase C-inhibitor (H-7) or Ca/calmodulin-dependent kinase inhibitor (W-7), showed no effect on the phosphorylation. These data suggest that phosphorylation of p64 seems to be a novel protein kinase specific to p64.</abstract><cop>England</cop><pub>Elsevier Inc</pub><pmid>2149031</pmid><doi>10.1016/0898-6568(90)90043-A</doi><tpages>7</tpages></addata></record> |
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| ispartof | Cellular signalling, 1990, Vol.2 (5), p.471-477 |
| issn | 0898-6568 1873-3913 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Adenosine Triphosphate - metabolism Blood Proteins - metabolism Calcium - metabolism Cell-Free System chemoattractant-dependent kinase Detergents Formyl-Met-Leu-Phe Humans Magnesium - metabolism Molecular Weight N-Formylmethionine Leucyl-Phenylalanine - pharmacology Neutrophils - enzymology Octoxynol Phosphoproteins - analysis Phosphoproteins - metabolism Phosphorylation Polyethylene Glycols polymorphonuclear leukocytes Protein Kinase C - antagonists & inhibitors Protein Kinases - metabolism protein phosphorylation Protein-Serine-Threonine Kinases serine-kinase Triton X-100 lysate |
| title | Formyl-Met-Leu-Phe-dependent serine kinase for a 64,000 molecular weight protein of polymorphonuclear leukocytes in a cell-lysate system |
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