The amyloid precursor protein of Alzheimer's disease is released by human platelets
Western blots of normal human platelets, employing a monoclonal antibody raised against the full-length amyloid precursor protein of Alzheimer's disease (APP695), revealed major bands of 100-110 and 120-130 kDa in both cytosolic, membrane, and released fractions. These species were similar in s...
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| Veröffentlicht in: | The Journal of biological chemistry 1990-09, Vol.265 (26), p.15977-15983 |
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| container_title | The Journal of biological chemistry |
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| creator | BUSH, A. I MARTINS, R. N BEYREUTHER, K MASTERS, C. L MOIR, R FULLER, S MIWARD, E CURRIE, J AMES, D WEIDEMANN, A FISCHER, P MULTHAUP, G |
| description | Western blots of normal human platelets, employing a monoclonal antibody raised against the full-length amyloid precursor
protein of Alzheimer's disease (APP695), revealed major bands of 100-110 and 120-130 kDa in both cytosolic, membrane, and
released fractions. These species were similar in size to forms seen in brain preparations and in plasma. There was no difference
in Western blots of platelet preparations from Alzheimer patients compared with controls. Purified platelet amyloid precursor
proteins were sequenced and shown to be amino terminally homogeneous. Immunohistochemistry localized the antigen to the platelet
and megakaryocyte and demonstrated weak immunostaining of some lymphocytes. Immunoprecipitation of material released from
platelets demonstrated that sedimentable full-length APP with the carboxyl-terminal epitope, and soluble APP lacking the carboxyl-terminal
epitope, may exist in the circulation. Western blots and carboxyl-terminal and amino-terminal APP radioimmunoassay of material
released by platelets in response to stimulation revealed that platelets release APP during degranulation. The function of
platelet APP is yet to be determined, but the present studies suggest a role in regulation of the coagulation cascade or in
platelet aggregation. |
| doi_str_mv | 10.1016/s0021-9258(18)55493-4 |
| format | Article |
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protein of Alzheimer's disease (APP695), revealed major bands of 100-110 and 120-130 kDa in both cytosolic, membrane, and
released fractions. These species were similar in size to forms seen in brain preparations and in plasma. There was no difference
in Western blots of platelet preparations from Alzheimer patients compared with controls. Purified platelet amyloid precursor
proteins were sequenced and shown to be amino terminally homogeneous. Immunohistochemistry localized the antigen to the platelet
and megakaryocyte and demonstrated weak immunostaining of some lymphocytes. Immunoprecipitation of material released from
platelets demonstrated that sedimentable full-length APP with the carboxyl-terminal epitope, and soluble APP lacking the carboxyl-terminal
epitope, may exist in the circulation. Western blots and carboxyl-terminal and amino-terminal APP radioimmunoassay of material
released by platelets in response to stimulation revealed that platelets release APP during degranulation. The function of
platelet APP is yet to be determined, but the present studies suggest a role in regulation of the coagulation cascade or in
platelet aggregation.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/s0021-9258(18)55493-4</identifier><identifier>PMID: 2118534</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>Alzheimer Disease - blood ; Amino Acid Sequence ; Amyloid - blood ; Amyloid - isolation & purification ; Amyloid beta-Protein Precursor ; Analytical, structural and metabolic biochemistry ; Biological and medical sciences ; Blood Platelets - drug effects ; Blood Platelets - metabolism ; Blotting, Western ; Cerebral Cortex - analysis ; Electrophoresis, Polyacrylamide Gel ; Epoprostenol - pharmacology ; Fundamental and applied biological sciences. Psychology ; Humans ; Immunoenzyme Techniques ; Miscellaneous ; Molecular Sequence Data ; Protease Inhibitors - blood ; Protein Precursors - blood ; Protein Precursors - isolation & purification ; Proteins ; Reference Values</subject><ispartof>The Journal of biological chemistry, 1990-09, Vol.265 (26), p.15977-15983</ispartof><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c476t-5c493853f2d97b5c80e73efab9bddf01b870bb2e3dd27052c07b7b92b2b9f7eb3</citedby><cites>FETCH-LOGICAL-c476t-5c493853f2d97b5c80e73efab9bddf01b870bb2e3dd27052c07b7b92b2b9f7eb3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,27906,27907</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19465894$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2118534$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>BUSH, A. I</creatorcontrib><creatorcontrib>MARTINS, R. N</creatorcontrib><creatorcontrib>BEYREUTHER, K</creatorcontrib><creatorcontrib>MASTERS, C. L</creatorcontrib><creatorcontrib>MOIR, R</creatorcontrib><creatorcontrib>FULLER, S</creatorcontrib><creatorcontrib>MIWARD, E</creatorcontrib><creatorcontrib>CURRIE, J</creatorcontrib><creatorcontrib>AMES, D</creatorcontrib><creatorcontrib>WEIDEMANN, A</creatorcontrib><creatorcontrib>FISCHER, P</creatorcontrib><creatorcontrib>MULTHAUP, G</creatorcontrib><title>The amyloid precursor protein of Alzheimer's disease is released by human platelets</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Western blots of normal human platelets, employing a monoclonal antibody raised against the full-length amyloid precursor
protein of Alzheimer's disease (APP695), revealed major bands of 100-110 and 120-130 kDa in both cytosolic, membrane, and
released fractions. These species were similar in size to forms seen in brain preparations and in plasma. There was no difference
in Western blots of platelet preparations from Alzheimer patients compared with controls. Purified platelet amyloid precursor
proteins were sequenced and shown to be amino terminally homogeneous. Immunohistochemistry localized the antigen to the platelet
and megakaryocyte and demonstrated weak immunostaining of some lymphocytes. Immunoprecipitation of material released from
platelets demonstrated that sedimentable full-length APP with the carboxyl-terminal epitope, and soluble APP lacking the carboxyl-terminal
epitope, may exist in the circulation. Western blots and carboxyl-terminal and amino-terminal APP radioimmunoassay of material
released by platelets in response to stimulation revealed that platelets release APP during degranulation. The function of
platelet APP is yet to be determined, but the present studies suggest a role in regulation of the coagulation cascade or in
platelet aggregation.</description><subject>Alzheimer Disease - blood</subject><subject>Amino Acid Sequence</subject><subject>Amyloid - blood</subject><subject>Amyloid - isolation & purification</subject><subject>Amyloid beta-Protein Precursor</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>Blood Platelets - drug effects</subject><subject>Blood Platelets - metabolism</subject><subject>Blotting, Western</subject><subject>Cerebral Cortex - analysis</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Epoprostenol - pharmacology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humans</subject><subject>Immunoenzyme Techniques</subject><subject>Miscellaneous</subject><subject>Molecular Sequence Data</subject><subject>Protease Inhibitors - blood</subject><subject>Protein Precursors - blood</subject><subject>Protein Precursors - isolation & purification</subject><subject>Proteins</subject><subject>Reference Values</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkE1r3DAQhkVpSTdpfkJAhzZJD24k2VpJxxCStBDoISn0JvQxrlXs9VZjEza_vnJ3SQWDhplnZl5eQs44-8IZX18hY4JXRkh9yfVnKRtTV80bsuJM11Ut-c-3ZPWKvCfHiL9ZeY3hR-RIcK5l3azI41MH1A27fkyRbjOEOeOYSzZOkDZ0bOl1_9JBGiBfII0JwSHQhDRDv6SR-h3t5sFt6LZ3UylO-IG8a12PcHr4T8iPu9unm6_Vw_f7bzfXD1Vo1HqqZCiSi4pWRKO8DJqBqqF13vgYW8a9Vsx7AXWMQjEpAlNeeSO88KZV4OsTcr7fW9T-mQEnOyQM0PduA-OMVhmjxVqKAso9GPKImKG125wGl3eWM7uYaR8Xp-zilOXa_jPTNmXu7HBg9gPE16mDe6X_6dB3GFzfZrcJCf8vN81aarNwH_dcl351zymD9WkMHQy2yCthuTRK1X8BiQSJmw</recordid><startdate>19900915</startdate><enddate>19900915</enddate><creator>BUSH, A. I</creator><creator>MARTINS, R. N</creator><creator>BEYREUTHER, K</creator><creator>MASTERS, C. L</creator><creator>MOIR, R</creator><creator>FULLER, S</creator><creator>MIWARD, E</creator><creator>CURRIE, J</creator><creator>AMES, D</creator><creator>WEIDEMANN, A</creator><creator>FISCHER, P</creator><creator>MULTHAUP, G</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>19900915</creationdate><title>The amyloid precursor protein of Alzheimer's disease is released by human platelets</title><author>BUSH, A. I ; MARTINS, R. N ; BEYREUTHER, K ; MASTERS, C. L ; MOIR, R ; FULLER, S ; MIWARD, E ; CURRIE, J ; AMES, D ; WEIDEMANN, A ; FISCHER, P ; MULTHAUP, G</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c476t-5c493853f2d97b5c80e73efab9bddf01b870bb2e3dd27052c07b7b92b2b9f7eb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>Alzheimer Disease - blood</topic><topic>Amino Acid Sequence</topic><topic>Amyloid - blood</topic><topic>Amyloid - isolation & purification</topic><topic>Amyloid beta-Protein Precursor</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Biological and medical sciences</topic><topic>Blood Platelets - drug effects</topic><topic>Blood Platelets - metabolism</topic><topic>Blotting, Western</topic><topic>Cerebral Cortex - analysis</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Epoprostenol - pharmacology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Humans</topic><topic>Immunoenzyme Techniques</topic><topic>Miscellaneous</topic><topic>Molecular Sequence Data</topic><topic>Protease Inhibitors - blood</topic><topic>Protein Precursors - blood</topic><topic>Protein Precursors - isolation & purification</topic><topic>Proteins</topic><topic>Reference Values</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>BUSH, A. I</creatorcontrib><creatorcontrib>MARTINS, R. N</creatorcontrib><creatorcontrib>BEYREUTHER, K</creatorcontrib><creatorcontrib>MASTERS, C. L</creatorcontrib><creatorcontrib>MOIR, R</creatorcontrib><creatorcontrib>FULLER, S</creatorcontrib><creatorcontrib>MIWARD, E</creatorcontrib><creatorcontrib>CURRIE, J</creatorcontrib><creatorcontrib>AMES, D</creatorcontrib><creatorcontrib>WEIDEMANN, A</creatorcontrib><creatorcontrib>FISCHER, P</creatorcontrib><creatorcontrib>MULTHAUP, G</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>BUSH, A. I</au><au>MARTINS, R. N</au><au>BEYREUTHER, K</au><au>MASTERS, C. L</au><au>MOIR, R</au><au>FULLER, S</au><au>MIWARD, E</au><au>CURRIE, J</au><au>AMES, D</au><au>WEIDEMANN, A</au><au>FISCHER, P</au><au>MULTHAUP, G</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The amyloid precursor protein of Alzheimer's disease is released by human platelets</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1990-09-15</date><risdate>1990</risdate><volume>265</volume><issue>26</issue><spage>15977</spage><epage>15983</epage><pages>15977-15983</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>Western blots of normal human platelets, employing a monoclonal antibody raised against the full-length amyloid precursor
protein of Alzheimer's disease (APP695), revealed major bands of 100-110 and 120-130 kDa in both cytosolic, membrane, and
released fractions. These species were similar in size to forms seen in brain preparations and in plasma. There was no difference
in Western blots of platelet preparations from Alzheimer patients compared with controls. Purified platelet amyloid precursor
proteins were sequenced and shown to be amino terminally homogeneous. Immunohistochemistry localized the antigen to the platelet
and megakaryocyte and demonstrated weak immunostaining of some lymphocytes. Immunoprecipitation of material released from
platelets demonstrated that sedimentable full-length APP with the carboxyl-terminal epitope, and soluble APP lacking the carboxyl-terminal
epitope, may exist in the circulation. Western blots and carboxyl-terminal and amino-terminal APP radioimmunoassay of material
released by platelets in response to stimulation revealed that platelets release APP during degranulation. The function of
platelet APP is yet to be determined, but the present studies suggest a role in regulation of the coagulation cascade or in
platelet aggregation.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>2118534</pmid><doi>10.1016/s0021-9258(18)55493-4</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1990-09, Vol.265 (26), p.15977-15983 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_79982652 |
| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Alzheimer Disease - blood Amino Acid Sequence Amyloid - blood Amyloid - isolation & purification Amyloid beta-Protein Precursor Analytical, structural and metabolic biochemistry Biological and medical sciences Blood Platelets - drug effects Blood Platelets - metabolism Blotting, Western Cerebral Cortex - analysis Electrophoresis, Polyacrylamide Gel Epoprostenol - pharmacology Fundamental and applied biological sciences. Psychology Humans Immunoenzyme Techniques Miscellaneous Molecular Sequence Data Protease Inhibitors - blood Protein Precursors - blood Protein Precursors - isolation & purification Proteins Reference Values |
| title | The amyloid precursor protein of Alzheimer's disease is released by human platelets |
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