Platelet Membrane Studies in the May-Hegglin Anomaly
Since studies of the giant platelets in the Bernard-Soulier syndrome have shown decreased electrophoretic mobility, decreased sialic acid, and an abnormality in a membrane glycoprotein, we performed similar studies on the giant platelets from two patients with the May-Hegglin anomaly. The patients’...
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Veröffentlicht in: | Blood 1981-08, Vol.58 (2), p.279-284 |
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description | Since studies of the giant platelets in the Bernard-Soulier syndrome have shown decreased electrophoretic mobility, decreased sialic acid, and an abnormality in a membrane glycoprotein, we performed similar studies on the giant platelets from two patients with the May-Hegglin anomaly. The patients’ platelet electrophoretic mobilities did not differ from control. Although the total sialic acid contents of the patients’ platelets were greater than control when calculated per platelet, they were very similar to control when normalized for differences in platelet volume and surface area. When platelet proteins were separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis, there were no differences between the glycoproteins of control and patient platelets as judged by the patterns of periodic acid Schiff staining and fluorescein-labeled concanavalin A binding. Similarly, patterns of surface glycoprotein labeling by neuraminidase/galactose oxidase/KB3M4 were identical. We conclude that unlike the giant platelets in the Bernard-Soulier syndrome, those of the May-Hegglin anomaly are not associated with a membrane abnormality detectable by these techniques. |
doi_str_mv | 10.1182/blood.V58.2.279.279 |
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The patients’ platelet electrophoretic mobilities did not differ from control. Although the total sialic acid contents of the patients’ platelets were greater than control when calculated per platelet, they were very similar to control when normalized for differences in platelet volume and surface area. When platelet proteins were separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis, there were no differences between the glycoproteins of control and patient platelets as judged by the patterns of periodic acid Schiff staining and fluorescein-labeled concanavalin A binding. Similarly, patterns of surface glycoprotein labeling by neuraminidase/galactose oxidase/KB3M4 were identical. We conclude that unlike the giant platelets in the Bernard-Soulier syndrome, those of the May-Hegglin anomaly are not associated with a membrane abnormality detectable by these techniques.</description><identifier>ISSN: 0006-4971</identifier><identifier>EISSN: 1528-0020</identifier><identifier>DOI: 10.1182/blood.V58.2.279.279</identifier><identifier>PMID: 7248522</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Adult ; Blood Platelet Disorders - blood ; Blood Platelets - cytology ; Blood Proteins ; Cell Membrane ; Electrophoresis ; Electrophoresis, Polyacrylamide Gel ; Female ; Galactose Oxidase ; Humans ; Membrane Proteins - metabolism ; Neuraminidase ; Sialic Acids</subject><ispartof>Blood, 1981-08, Vol.58 (2), p.279-284</ispartof><rights>1981 American Society of Hematology</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c331t-b1e456255ebe2b08d3e5387ec23a98b98762d325a97762622e064d01621f12363</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7248522$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Coller, Barry S.</creatorcontrib><creatorcontrib>Zarrabi, Mohammad H.</creatorcontrib><title>Platelet Membrane Studies in the May-Hegglin Anomaly</title><title>Blood</title><addtitle>Blood</addtitle><description>Since studies of the giant platelets in the Bernard-Soulier syndrome have shown decreased electrophoretic mobility, decreased sialic acid, and an abnormality in a membrane glycoprotein, we performed similar studies on the giant platelets from two patients with the May-Hegglin anomaly. The patients’ platelet electrophoretic mobilities did not differ from control. Although the total sialic acid contents of the patients’ platelets were greater than control when calculated per platelet, they were very similar to control when normalized for differences in platelet volume and surface area. When platelet proteins were separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis, there were no differences between the glycoproteins of control and patient platelets as judged by the patterns of periodic acid Schiff staining and fluorescein-labeled concanavalin A binding. Similarly, patterns of surface glycoprotein labeling by neuraminidase/galactose oxidase/KB3M4 were identical. We conclude that unlike the giant platelets in the Bernard-Soulier syndrome, those of the May-Hegglin anomaly are not associated with a membrane abnormality detectable by these techniques.</description><subject>Adult</subject><subject>Blood Platelet Disorders - blood</subject><subject>Blood Platelets - cytology</subject><subject>Blood Proteins</subject><subject>Cell Membrane</subject><subject>Electrophoresis</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Female</subject><subject>Galactose Oxidase</subject><subject>Humans</subject><subject>Membrane Proteins - metabolism</subject><subject>Neuraminidase</subject><subject>Sialic Acids</subject><issn>0006-4971</issn><issn>1528-0020</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1981</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1PwzAMhiMEGmPwCxBST9xaEqdp0wOHaQKGtAkkPq5R2ngjKG1H0yLt35OxiSMHy7Zsv3r9EHLJaMKYhJvSta1J3oVMIIG82MURGTMBMqYU6DEZU0qzOC1ydkrOvP-klKUcxIiMckilABiT9NnpHh320RLrstMNRi_9YCz6yDZR_4HRUm_jOa7XLvTTpq21256Tk5V2Hi8OeULe7u9eZ_N48fTwOJsu4opz1sclw1RkIASWCCWVhqPgMscKuC5kWcg8AxP86CIPVQaANEsNZRmwFQOe8Qm53utuuvZrQN-r2voKnQs228GrnItUCFqERb5frLrW-w5XatPZWndbxajasVK_rFRgpUAFTrsIV1cH-aGs0fzdHOCE-e1-juHHb4ud8pXFpkJjO6x6ZVr7r_4PRbR4vw</recordid><startdate>198108</startdate><enddate>198108</enddate><creator>Coller, Barry S.</creator><creator>Zarrabi, Mohammad H.</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</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>198108</creationdate><title>Platelet Membrane Studies in the May-Hegglin Anomaly</title><author>Coller, Barry S. ; Zarrabi, Mohammad H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c331t-b1e456255ebe2b08d3e5387ec23a98b98762d325a97762622e064d01621f12363</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1981</creationdate><topic>Adult</topic><topic>Blood Platelet Disorders - blood</topic><topic>Blood Platelets - cytology</topic><topic>Blood Proteins</topic><topic>Cell Membrane</topic><topic>Electrophoresis</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Female</topic><topic>Galactose Oxidase</topic><topic>Humans</topic><topic>Membrane Proteins - metabolism</topic><topic>Neuraminidase</topic><topic>Sialic Acids</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Coller, Barry S.</creatorcontrib><creatorcontrib>Zarrabi, Mohammad H.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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>Blood</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Coller, Barry S.</au><au>Zarrabi, Mohammad H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Platelet Membrane Studies in the May-Hegglin Anomaly</atitle><jtitle>Blood</jtitle><addtitle>Blood</addtitle><date>1981-08</date><risdate>1981</risdate><volume>58</volume><issue>2</issue><spage>279</spage><epage>284</epage><pages>279-284</pages><issn>0006-4971</issn><eissn>1528-0020</eissn><abstract>Since studies of the giant platelets in the Bernard-Soulier syndrome have shown decreased electrophoretic mobility, decreased sialic acid, and an abnormality in a membrane glycoprotein, we performed similar studies on the giant platelets from two patients with the May-Hegglin anomaly. The patients’ platelet electrophoretic mobilities did not differ from control. Although the total sialic acid contents of the patients’ platelets were greater than control when calculated per platelet, they were very similar to control when normalized for differences in platelet volume and surface area. When platelet proteins were separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis, there were no differences between the glycoproteins of control and patient platelets as judged by the patterns of periodic acid Schiff staining and fluorescein-labeled concanavalin A binding. Similarly, patterns of surface glycoprotein labeling by neuraminidase/galactose oxidase/KB3M4 were identical. We conclude that unlike the giant platelets in the Bernard-Soulier syndrome, those of the May-Hegglin anomaly are not associated with a membrane abnormality detectable by these techniques.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>7248522</pmid><doi>10.1182/blood.V58.2.279.279</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Adult Blood Platelet Disorders - blood Blood Platelets - cytology Blood Proteins Cell Membrane Electrophoresis Electrophoresis, Polyacrylamide Gel Female Galactose Oxidase Humans Membrane Proteins - metabolism Neuraminidase Sialic Acids |
title | Platelet Membrane Studies in the May-Hegglin Anomaly |
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