pp60src is an endogenous substrate for calpain in human blood platelets
Calpain is distributed ubiquitously in virtually every tissue (Croall, D. E., and DeMartino, G. N. (1991) Physiol. Rev. 71, 813-846), but its physiological role remains to be determined. The identification of its natural endogenous substrates would be of great interest. Since pp60src, a major tyrosi...
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| creator | ODA, A DRUKER, B. J ARIYOSHI, H SMITH, M SALZMAN, E. W |
| description | Calpain is distributed ubiquitously in virtually every tissue (Croall, D. E., and DeMartino, G. N. (1991) Physiol. Rev. 71,
813-846), but its physiological role remains to be determined. The identification of its natural endogenous substrates would
be of great interest. Since pp60src, a major tyrosine kinase in platelets, is known to be easily cleaved during purification
from cells (Feder, D., and Bishop, J. M. (1990) J. Biol. Chem. 265, 8205-8211), we examined the possibility that it is an
endogenous substrate of calpain. In the whole cell lysate from resting platelets, which was analyzed by Western blotting with
monoclonal antibody 327, we found pp60src almost exclusively in a 60-kDa form, with a trace of 52-kDa form. Addition of A23187
(a calcium ionophore) or dibucaine, which are known to be activators of platelet calpain (Croall and DeMartino, 1991; Fox,
J. E., Reynolds, C., Morrow, J. S., and Phillips, D. R. (1987) Blood 76, 2510-2519; Fox, J. E., Austin, C. D., Boyles, J.
K., and Steffen, P. K. (1990b) J. Cell Biol. 111, 483-493), caused dose- and time-dependent cleavage of actin-binding protein
and p235 protein (talin). At the same time, loss of the 60-kDa species of pp60src and generation of the 52-kDa (occasionally
seen as doublets) and 47-kDa species were detected by the Western blotting. In platelets aggregated by 1 unit/ml thrombin,
apparently identical cleavage products were found. The cleavage of pp60src was inhibited by calpeptin (20 microM), an inhibitor
of calpain (Tsujinaka, T., Kajiwara, Y., Kambayashi, J., Sakon, M., Higuchi, N., Tanaka, T., and Mori, T. (1988) Biochem.
Biophys. Res. Commun. 153, 1201-1208; Tsujinaka, T., Ariyoshi, H., Uemura, Y., Sakon, M., Kambayashi, J., and Mori, T. (1990)
Life Sci. 46, 1059-1066; Fox, J. E., Clifford, C. C., and Austin, C. D. (1990) Blood 76, 2510-2519; Fox, J. E., Austin, C.
D., Boyles, J. K., and Steffen, P. K. (1990) J. Cell. Biol. 111, 483-493; Fox, J. E., Austin, C. D., Clifford, C. C., and
Steffen, P. K. (1991) J. Biol. Chem. 266, 13289-13295). Addition of EGTA (3 mM) to the extracellular media completely inhibited
the cleavage of actin-binding protein, talin, and pp60src in response to A23187 (1 microM). Intact pp60src was distributed
in both cytosolic and particulate (membrane) fractions. Cleaved species were found exclusively in the cytosolic fraction.
pp60src-associated enolase kinase activity was reduced. Thus, pp60src is an endogenous substrate for calpain, the cleavage
of which may ha |
| doi_str_mv | 10.1016/S0021-9258(18)31431-5 |
| format | Article |
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813-846), but its physiological role remains to be determined. The identification of its natural endogenous substrates would
be of great interest. Since pp60src, a major tyrosine kinase in platelets, is known to be easily cleaved during purification
from cells (Feder, D., and Bishop, J. M. (1990) J. Biol. Chem. 265, 8205-8211), we examined the possibility that it is an
endogenous substrate of calpain. In the whole cell lysate from resting platelets, which was analyzed by Western blotting with
monoclonal antibody 327, we found pp60src almost exclusively in a 60-kDa form, with a trace of 52-kDa form. Addition of A23187
(a calcium ionophore) or dibucaine, which are known to be activators of platelet calpain (Croall and DeMartino, 1991; Fox,
J. E., Reynolds, C., Morrow, J. S., and Phillips, D. R. (1987) Blood 76, 2510-2519; Fox, J. E., Austin, C. D., Boyles, J.
K., and Steffen, P. K. (1990b) J. Cell Biol. 111, 483-493), caused dose- and time-dependent cleavage of actin-binding protein
and p235 protein (talin). At the same time, loss of the 60-kDa species of pp60src and generation of the 52-kDa (occasionally
seen as doublets) and 47-kDa species were detected by the Western blotting. In platelets aggregated by 1 unit/ml thrombin,
apparently identical cleavage products were found. The cleavage of pp60src was inhibited by calpeptin (20 microM), an inhibitor
of calpain (Tsujinaka, T., Kajiwara, Y., Kambayashi, J., Sakon, M., Higuchi, N., Tanaka, T., and Mori, T. (1988) Biochem.
Biophys. Res. Commun. 153, 1201-1208; Tsujinaka, T., Ariyoshi, H., Uemura, Y., Sakon, M., Kambayashi, J., and Mori, T. (1990)
Life Sci. 46, 1059-1066; Fox, J. E., Clifford, C. C., and Austin, C. D. (1990) Blood 76, 2510-2519; Fox, J. E., Austin, C.
D., Boyles, J. K., and Steffen, P. K. (1990) J. Cell. Biol. 111, 483-493; Fox, J. E., Austin, C. D., Clifford, C. C., and
Steffen, P. K. (1991) J. Biol. Chem. 266, 13289-13295). Addition of EGTA (3 mM) to the extracellular media completely inhibited
the cleavage of actin-binding protein, talin, and pp60src in response to A23187 (1 microM). Intact pp60src was distributed
in both cytosolic and particulate (membrane) fractions. Cleaved species were found exclusively in the cytosolic fraction.
pp60src-associated enolase kinase activity was reduced. Thus, pp60src is an endogenous substrate for calpain, the cleavage
of which may have regulatory effects on the kinase.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)31431-5</identifier><identifier>PMID: 7685344</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 ; Antibodies, Monoclonal ; Biological and medical sciences ; Blood Platelets - enzymology ; Blotting, Western ; Calcimycin - pharmacology ; Calcium - pharmacology ; Calpain - blood ; Dimethyl Sulfoxide - pharmacology ; Dipeptides - pharmacology ; Egtazic Acid - pharmacology ; Electrophoresis, Polyacrylamide Gel ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; Humans ; Hydrolases ; Microfilament Proteins - metabolism ; Molecular Weight ; Platelet Aggregation ; Proto-Oncogene Proteins pp60(c-src) - blood ; Proto-Oncogene Proteins pp60(c-src) - isolation & purification ; Substrate Specificity ; Talin - metabolism</subject><ispartof>The Journal of biological chemistry, 1993-06, Vol.268 (17), p.12603-12608</ispartof><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c409t-eba6af7084a8ecd8f61e2a5fdc0c25a19e3cbf775f8f0521339e263c352455043</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4820580$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7685344$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>ODA, A</creatorcontrib><creatorcontrib>DRUKER, B. J</creatorcontrib><creatorcontrib>ARIYOSHI, H</creatorcontrib><creatorcontrib>SMITH, M</creatorcontrib><creatorcontrib>SALZMAN, E. W</creatorcontrib><title>pp60src is an endogenous substrate for calpain in human blood platelets</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Calpain is distributed ubiquitously in virtually every tissue (Croall, D. E., and DeMartino, G. N. (1991) Physiol. Rev. 71,
813-846), but its physiological role remains to be determined. The identification of its natural endogenous substrates would
be of great interest. Since pp60src, a major tyrosine kinase in platelets, is known to be easily cleaved during purification
from cells (Feder, D., and Bishop, J. M. (1990) J. Biol. Chem. 265, 8205-8211), we examined the possibility that it is an
endogenous substrate of calpain. In the whole cell lysate from resting platelets, which was analyzed by Western blotting with
monoclonal antibody 327, we found pp60src almost exclusively in a 60-kDa form, with a trace of 52-kDa form. Addition of A23187
(a calcium ionophore) or dibucaine, which are known to be activators of platelet calpain (Croall and DeMartino, 1991; Fox,
J. E., Reynolds, C., Morrow, J. S., and Phillips, D. R. (1987) Blood 76, 2510-2519; Fox, J. E., Austin, C. D., Boyles, J.
K., and Steffen, P. K. (1990b) J. Cell Biol. 111, 483-493), caused dose- and time-dependent cleavage of actin-binding protein
and p235 protein (talin). At the same time, loss of the 60-kDa species of pp60src and generation of the 52-kDa (occasionally
seen as doublets) and 47-kDa species were detected by the Western blotting. In platelets aggregated by 1 unit/ml thrombin,
apparently identical cleavage products were found. The cleavage of pp60src was inhibited by calpeptin (20 microM), an inhibitor
of calpain (Tsujinaka, T., Kajiwara, Y., Kambayashi, J., Sakon, M., Higuchi, N., Tanaka, T., and Mori, T. (1988) Biochem.
Biophys. Res. Commun. 153, 1201-1208; Tsujinaka, T., Ariyoshi, H., Uemura, Y., Sakon, M., Kambayashi, J., and Mori, T. (1990)
Life Sci. 46, 1059-1066; Fox, J. E., Clifford, C. C., and Austin, C. D. (1990) Blood 76, 2510-2519; Fox, J. E., Austin, C.
D., Boyles, J. K., and Steffen, P. K. (1990) J. Cell. Biol. 111, 483-493; Fox, J. E., Austin, C. D., Clifford, C. C., and
Steffen, P. K. (1991) J. Biol. Chem. 266, 13289-13295). Addition of EGTA (3 mM) to the extracellular media completely inhibited
the cleavage of actin-binding protein, talin, and pp60src in response to A23187 (1 microM). Intact pp60src was distributed
in both cytosolic and particulate (membrane) fractions. Cleaved species were found exclusively in the cytosolic fraction.
pp60src-associated enolase kinase activity was reduced. Thus, pp60src is an endogenous substrate for calpain, the cleavage
of which may have regulatory effects on the kinase.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Antibodies, Monoclonal</subject><subject>Biological and medical sciences</subject><subject>Blood Platelets - enzymology</subject><subject>Blotting, Western</subject><subject>Calcimycin - pharmacology</subject><subject>Calcium - pharmacology</subject><subject>Calpain - blood</subject><subject>Dimethyl Sulfoxide - pharmacology</subject><subject>Dipeptides - pharmacology</subject><subject>Egtazic Acid - pharmacology</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humans</subject><subject>Hydrolases</subject><subject>Microfilament Proteins - metabolism</subject><subject>Molecular Weight</subject><subject>Platelet Aggregation</subject><subject>Proto-Oncogene Proteins pp60(c-src) - blood</subject><subject>Proto-Oncogene Proteins pp60(c-src) - isolation & purification</subject><subject>Substrate Specificity</subject><subject>Talin - metabolism</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkFtLHTEQgIO06NH2Jwj7IKV9WM0kmWz2UaTVguBDFXwL2ezEs7I3k12k_75RD6fDwDzMNxc-xk6BnwMHffGHcwFlLdB8B_NDgpJQ4gHbADeylAiPn9hmjxyx45SeeQ5VwyE7rLRBqdSGXc-z5in6okuFGwsa2-mJxmlNRVqbtES3UBGmWHjXz64bi5zbdchk009TW8x9Bnpa0hf2Obg-0dddPWEPv37eX92Ut3fXv68ub0uveL2U1DjtQsWNcoZ8a4IGEg5D67kX6KAm6ZtQVRhM4ChAypqEll6iUIhcyRP27WPvHKeXldJihy556ns3Uv7aVlhpxBoyiB-gj1NKkYKdYze4-NcCt28C7btA-2bHgrHvAi3mudPdgbUZqN1P7Yzl_tmu71KWEqIbfZf2mDKCo-H_sW33tH3tItmmm_yWBit0vldZEJpL-Q-EWIPT</recordid><startdate>19930615</startdate><enddate>19930615</enddate><creator>ODA, A</creator><creator>DRUKER, B. J</creator><creator>ARIYOSHI, H</creator><creator>SMITH, M</creator><creator>SALZMAN, E. W</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>19930615</creationdate><title>pp60src is an endogenous substrate for calpain in human blood platelets</title><author>ODA, A ; DRUKER, B. J ; ARIYOSHI, H ; SMITH, M ; SALZMAN, E. W</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c409t-eba6af7084a8ecd8f61e2a5fdc0c25a19e3cbf775f8f0521339e263c352455043</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Antibodies, Monoclonal</topic><topic>Biological and medical sciences</topic><topic>Blood Platelets - enzymology</topic><topic>Blotting, Western</topic><topic>Calcimycin - pharmacology</topic><topic>Calcium - pharmacology</topic><topic>Calpain - blood</topic><topic>Dimethyl Sulfoxide - pharmacology</topic><topic>Dipeptides - pharmacology</topic><topic>Egtazic Acid - pharmacology</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Humans</topic><topic>Hydrolases</topic><topic>Microfilament Proteins - metabolism</topic><topic>Molecular Weight</topic><topic>Platelet Aggregation</topic><topic>Proto-Oncogene Proteins pp60(c-src) - blood</topic><topic>Proto-Oncogene Proteins pp60(c-src) - isolation & purification</topic><topic>Substrate Specificity</topic><topic>Talin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>ODA, A</creatorcontrib><creatorcontrib>DRUKER, B. J</creatorcontrib><creatorcontrib>ARIYOSHI, H</creatorcontrib><creatorcontrib>SMITH, M</creatorcontrib><creatorcontrib>SALZMAN, E. W</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>ODA, A</au><au>DRUKER, B. J</au><au>ARIYOSHI, H</au><au>SMITH, M</au><au>SALZMAN, E. W</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>pp60src is an endogenous substrate for calpain in human blood platelets</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1993-06-15</date><risdate>1993</risdate><volume>268</volume><issue>17</issue><spage>12603</spage><epage>12608</epage><pages>12603-12608</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>Calpain is distributed ubiquitously in virtually every tissue (Croall, D. E., and DeMartino, G. N. (1991) Physiol. Rev. 71,
813-846), but its physiological role remains to be determined. The identification of its natural endogenous substrates would
be of great interest. Since pp60src, a major tyrosine kinase in platelets, is known to be easily cleaved during purification
from cells (Feder, D., and Bishop, J. M. (1990) J. Biol. Chem. 265, 8205-8211), we examined the possibility that it is an
endogenous substrate of calpain. In the whole cell lysate from resting platelets, which was analyzed by Western blotting with
monoclonal antibody 327, we found pp60src almost exclusively in a 60-kDa form, with a trace of 52-kDa form. Addition of A23187
(a calcium ionophore) or dibucaine, which are known to be activators of platelet calpain (Croall and DeMartino, 1991; Fox,
J. E., Reynolds, C., Morrow, J. S., and Phillips, D. R. (1987) Blood 76, 2510-2519; Fox, J. E., Austin, C. D., Boyles, J.
K., and Steffen, P. K. (1990b) J. Cell Biol. 111, 483-493), caused dose- and time-dependent cleavage of actin-binding protein
and p235 protein (talin). At the same time, loss of the 60-kDa species of pp60src and generation of the 52-kDa (occasionally
seen as doublets) and 47-kDa species were detected by the Western blotting. In platelets aggregated by 1 unit/ml thrombin,
apparently identical cleavage products were found. The cleavage of pp60src was inhibited by calpeptin (20 microM), an inhibitor
of calpain (Tsujinaka, T., Kajiwara, Y., Kambayashi, J., Sakon, M., Higuchi, N., Tanaka, T., and Mori, T. (1988) Biochem.
Biophys. Res. Commun. 153, 1201-1208; Tsujinaka, T., Ariyoshi, H., Uemura, Y., Sakon, M., Kambayashi, J., and Mori, T. (1990)
Life Sci. 46, 1059-1066; Fox, J. E., Clifford, C. C., and Austin, C. D. (1990) Blood 76, 2510-2519; Fox, J. E., Austin, C.
D., Boyles, J. K., and Steffen, P. K. (1990) J. Cell. Biol. 111, 483-493; Fox, J. E., Austin, C. D., Clifford, C. C., and
Steffen, P. K. (1991) J. Biol. Chem. 266, 13289-13295). Addition of EGTA (3 mM) to the extracellular media completely inhibited
the cleavage of actin-binding protein, talin, and pp60src in response to A23187 (1 microM). Intact pp60src was distributed
in both cytosolic and particulate (membrane) fractions. Cleaved species were found exclusively in the cytosolic fraction.
pp60src-associated enolase kinase activity was reduced. Thus, pp60src is an endogenous substrate for calpain, the cleavage
of which may have regulatory effects on the kinase.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>7685344</pmid><doi>10.1016/S0021-9258(18)31431-5</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| language | eng |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Analytical, structural and metabolic biochemistry Antibodies, Monoclonal Biological and medical sciences Blood Platelets - enzymology Blotting, Western Calcimycin - pharmacology Calcium - pharmacology Calpain - blood Dimethyl Sulfoxide - pharmacology Dipeptides - pharmacology Egtazic Acid - pharmacology Electrophoresis, Polyacrylamide Gel Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Humans Hydrolases Microfilament Proteins - metabolism Molecular Weight Platelet Aggregation Proto-Oncogene Proteins pp60(c-src) - blood Proto-Oncogene Proteins pp60(c-src) - isolation & purification Substrate Specificity Talin - metabolism |
| title | pp60src is an endogenous substrate for calpain in human blood platelets |
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