Phosphorylation of chicken cardiac C-protein by calcium/calmodulin-dependent protein kinase II
Chicken cardiac C-protein was readily phosphorylated by purified calcium/calmodulin-dependent protein kinase II (CaM-kinase II). Maximum incorporation was about 4 mol of 32P/mol of C-protein subunit. Peptide mapping indicated that some of the sites phosphorylated by CaM-kinase II were located on the...
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Veröffentlicht in: | The Journal of biological chemistry 1991-02, Vol.266 (5), p.2811-2817 |
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description | Chicken cardiac C-protein was readily phosphorylated by purified calcium/calmodulin-dependent protein kinase II (CaM-kinase
II). Maximum incorporation was about 4 mol of 32P/mol of C-protein subunit. Peptide mapping indicated that some of the sites
phosphorylated by CaM-kinase II were located on the same phosphopeptides obtained when C-protein was phosphorylated by the
cAMP-dependent protein kinase (peptides T1, T2, and T3). There was a fourth peptide (T3a) which was unique to CaM-kinase II
phosphorylation. 32P-Amino acid analysis showed that essentially all of the 32P of peptides T1, T2, and T3a was in phosphoserine.
cAMP-dependent protein kinase incorporated 32P only into threonine of peptide T3. Threonine was the preferred site of phosphorylation
by CaM-kinase II, but there was significant phosphorylation of a serine in peptide T3. Partially purified C-protein preparations
contained an associated calcium/calmodulin-dependent protein kinase. Peptide maps obtained from C-protein phosphorylated by
the endogenous kinase were similar to those obtained from C-protein phosphorylated by CaM-kinase II. However, the ratio of
phosphothreonine to phosphoserine in peptide T3 was lower. This was due to a contaminating phosphatase in the partially purified
C-protein which preferentially dephosphorylated the phosphothreonine of peptide T3. It is suggested that the calcium/calmodulin-dependent
protein kinase associated with C-protein is similar or identical to CaM-kinase II and that CaM-kinase II may play a role in
the phosphorylation of C-protein in the heart. |
doi_str_mv | 10.1016/S0021-9258(18)49919-X |
format | Article |
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II). Maximum incorporation was about 4 mol of 32P/mol of C-protein subunit. Peptide mapping indicated that some of the sites
phosphorylated by CaM-kinase II were located on the same phosphopeptides obtained when C-protein was phosphorylated by the
cAMP-dependent protein kinase (peptides T1, T2, and T3). There was a fourth peptide (T3a) which was unique to CaM-kinase II
phosphorylation. 32P-Amino acid analysis showed that essentially all of the 32P of peptides T1, T2, and T3a was in phosphoserine.
cAMP-dependent protein kinase incorporated 32P only into threonine of peptide T3. Threonine was the preferred site of phosphorylation
by CaM-kinase II, but there was significant phosphorylation of a serine in peptide T3. Partially purified C-protein preparations
contained an associated calcium/calmodulin-dependent protein kinase. Peptide maps obtained from C-protein phosphorylated by
the endogenous kinase were similar to those obtained from C-protein phosphorylated by CaM-kinase II. However, the ratio of
phosphothreonine to phosphoserine in peptide T3 was lower. This was due to a contaminating phosphatase in the partially purified
C-protein which preferentially dephosphorylated the phosphothreonine of peptide T3. It is suggested that the calcium/calmodulin-dependent
protein kinase associated with C-protein is similar or identical to CaM-kinase II and that CaM-kinase II may play a role in
the phosphorylation of C-protein in the heart.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)49919-X</identifier><identifier>PMID: 1671569</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>Analytical, structural and metabolic biochemistry ; Animals ; Autoradiography ; Biological and medical sciences ; Calcium-Calmodulin-Dependent Protein Kinases ; Carrier Proteins - metabolism ; Chickens ; Chromatography, High Pressure Liquid ; Electrophoresis, Polyacrylamide Gel ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; Hydrolysis ; Myocardium - metabolism ; Phosphorylation ; Protein Kinases - metabolism ; Transferases ; Trypsin</subject><ispartof>The Journal of biological chemistry, 1991-02, Vol.266 (5), p.2811-2817</ispartof><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c408t-d5555db7c5090caeb9494bbb77b2f9df8ce5d4f97267f9bab8a2077bb9e111963</citedby><cites>FETCH-LOGICAL-c408t-d5555db7c5090caeb9494bbb77b2f9df8ce5d4f97267f9bab8a2077bb9e111963</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19694852$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1671569$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>SCHLENDER, K. K</creatorcontrib><creatorcontrib>BEAN, L. J</creatorcontrib><title>Phosphorylation of chicken cardiac C-protein by calcium/calmodulin-dependent protein kinase II</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Chicken cardiac C-protein was readily phosphorylated by purified calcium/calmodulin-dependent protein kinase II (CaM-kinase
II). Maximum incorporation was about 4 mol of 32P/mol of C-protein subunit. Peptide mapping indicated that some of the sites
phosphorylated by CaM-kinase II were located on the same phosphopeptides obtained when C-protein was phosphorylated by the
cAMP-dependent protein kinase (peptides T1, T2, and T3). There was a fourth peptide (T3a) which was unique to CaM-kinase II
phosphorylation. 32P-Amino acid analysis showed that essentially all of the 32P of peptides T1, T2, and T3a was in phosphoserine.
cAMP-dependent protein kinase incorporated 32P only into threonine of peptide T3. Threonine was the preferred site of phosphorylation
by CaM-kinase II, but there was significant phosphorylation of a serine in peptide T3. Partially purified C-protein preparations
contained an associated calcium/calmodulin-dependent protein kinase. Peptide maps obtained from C-protein phosphorylated by
the endogenous kinase were similar to those obtained from C-protein phosphorylated by CaM-kinase II. However, the ratio of
phosphothreonine to phosphoserine in peptide T3 was lower. This was due to a contaminating phosphatase in the partially purified
C-protein which preferentially dephosphorylated the phosphothreonine of peptide T3. It is suggested that the calcium/calmodulin-dependent
protein kinase associated with C-protein is similar or identical to CaM-kinase II and that CaM-kinase II may play a role in
the phosphorylation of C-protein in the heart.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Autoradiography</subject><subject>Biological and medical sciences</subject><subject>Calcium-Calmodulin-Dependent Protein Kinases</subject><subject>Carrier Proteins - metabolism</subject><subject>Chickens</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hydrolysis</subject><subject>Myocardium - metabolism</subject><subject>Phosphorylation</subject><subject>Protein Kinases - metabolism</subject><subject>Transferases</subject><subject>Trypsin</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkF1LHDEUhkNRdLX9CcIgWOzFaM5MMpNclkXbBaEFW9irhnyNE51J1mSGsv_e6G7ruTlw3uechAehM8BXgKG5vse4gpJXlF0C-0I4B16uP6AFYFaXNYX1AVr8R47RSUqPOBfhcISOoGmBNnyB_vzsQ9r0IW4HObngi9AVunf6yfpCy2ic1MWy3MQwWecLtc3DQbt5vM59DGYenC-N3VhvrJ-Kf9yT8zLZYrX6iA47OST7ad9P0e_bm1_L7-Xdj2-r5de7UhPMptLQXEa1mmKOtbSKE06UUm2rqo6bjmlLDel4WzVtx5VUTFY4h4pbAOBNfYo-7-7mHzzPNk1idEnbYZDehjkJhgnBvK0zSHegjiGlaDuxiW6UcSsAi1ev4s2reJUmgIk3r2Kd9872D8xqtOZ9aycy5xf7XKaspovSa5feMd5wwmiVufMd17uH_q-LVigXdG9HUTWNoKJiAPUL4NGNfw</recordid><startdate>19910215</startdate><enddate>19910215</enddate><creator>SCHLENDER, K. K</creator><creator>BEAN, L. J</creator><general>American Society for Biochemistry and Molecular Biology</general><scope>IQODW</scope><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>19910215</creationdate><title>Phosphorylation of chicken cardiac C-protein by calcium/calmodulin-dependent protein kinase II</title><author>SCHLENDER, K. K ; BEAN, L. J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c408t-d5555db7c5090caeb9494bbb77b2f9df8ce5d4f97267f9bab8a2077bb9e111963</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Autoradiography</topic><topic>Biological and medical sciences</topic><topic>Calcium-Calmodulin-Dependent Protein Kinases</topic><topic>Carrier Proteins - metabolism</topic><topic>Chickens</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hydrolysis</topic><topic>Myocardium - metabolism</topic><topic>Phosphorylation</topic><topic>Protein Kinases - metabolism</topic><topic>Transferases</topic><topic>Trypsin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>SCHLENDER, K. K</creatorcontrib><creatorcontrib>BEAN, L. J</creatorcontrib><collection>Pascal-Francis</collection><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>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>SCHLENDER, K. K</au><au>BEAN, L. J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Phosphorylation of chicken cardiac C-protein by calcium/calmodulin-dependent protein kinase II</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1991-02-15</date><risdate>1991</risdate><volume>266</volume><issue>5</issue><spage>2811</spage><epage>2817</epage><pages>2811-2817</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>Chicken cardiac C-protein was readily phosphorylated by purified calcium/calmodulin-dependent protein kinase II (CaM-kinase
II). Maximum incorporation was about 4 mol of 32P/mol of C-protein subunit. Peptide mapping indicated that some of the sites
phosphorylated by CaM-kinase II were located on the same phosphopeptides obtained when C-protein was phosphorylated by the
cAMP-dependent protein kinase (peptides T1, T2, and T3). There was a fourth peptide (T3a) which was unique to CaM-kinase II
phosphorylation. 32P-Amino acid analysis showed that essentially all of the 32P of peptides T1, T2, and T3a was in phosphoserine.
cAMP-dependent protein kinase incorporated 32P only into threonine of peptide T3. Threonine was the preferred site of phosphorylation
by CaM-kinase II, but there was significant phosphorylation of a serine in peptide T3. Partially purified C-protein preparations
contained an associated calcium/calmodulin-dependent protein kinase. Peptide maps obtained from C-protein phosphorylated by
the endogenous kinase were similar to those obtained from C-protein phosphorylated by CaM-kinase II. However, the ratio of
phosphothreonine to phosphoserine in peptide T3 was lower. This was due to a contaminating phosphatase in the partially purified
C-protein which preferentially dephosphorylated the phosphothreonine of peptide T3. It is suggested that the calcium/calmodulin-dependent
protein kinase associated with C-protein is similar or identical to CaM-kinase II and that CaM-kinase II may play a role in
the phosphorylation of C-protein in the heart.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>1671569</pmid><doi>10.1016/S0021-9258(18)49919-X</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Analytical, structural and metabolic biochemistry Animals Autoradiography Biological and medical sciences Calcium-Calmodulin-Dependent Protein Kinases Carrier Proteins - metabolism Chickens Chromatography, High Pressure Liquid Electrophoresis, Polyacrylamide Gel Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Hydrolysis Myocardium - metabolism Phosphorylation Protein Kinases - metabolism Transferases Trypsin |
title | Phosphorylation of chicken cardiac C-protein by calcium/calmodulin-dependent protein kinase II |
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