In vitro evaluation of the haemostatic value of the LFB-von Willebrand factor concentrate.
Identifieur interne : 002646 ( PubMed/Corpus ); précédent : 002645; suivant : 002647In vitro evaluation of the haemostatic value of the LFB-von Willebrand factor concentrate.
Auteurs : C. MazurierSource :
- Haemophilia : the official journal of the World Federation of Hemophilia [ 1351-8216 ] ; 1998.
English descriptors
- KwdEn :
- Collagen (metabolism), Factor VIII (metabolism), Hemostatics (analysis), Hemostatics (metabolism), Humans, Platelet Glycoprotein GPIIb-IIIa Complex (metabolism), Platelet Glycoprotein GPIb-IX Complex, Platelet Membrane Glycoproteins, Receptors, Cell Surface (metabolism), von Willebrand Factor (analysis), von Willebrand Factor (metabolism).
- MESH :
- chemical , analysis : Hemostatics, von Willebrand Factor.
- chemical , metabolism : Collagen, Factor VIII, Hemostatics, Platelet Glycoprotein GPIIb-IIIa Complex, Receptors, Cell Surface, von Willebrand Factor.
- Humans, Platelet Glycoprotein GPIb-IX Complex, Platelet Membrane Glycoproteins.
Abstract
The structural and functional studies of the concentrate of von Willebrand factor (vWF) manufactured by LFB have been first performed as part of the preclinical development of this product specially intended for the treatment of von Willebrand disease. The electrophoretic analyses showed the high purity of LFB-vWF concentrate (specific activity of 100 IU of ristocetin cofactor activity per milligram of protein) and the multimeric pattern attesting the presence of high molecular weight multimeters (> or = 15-mers). The measurements of vWF capacity to bind to: (1) platelet glycoprotein (GP) Ib in the presence of ristocetin; (2) GPIIb/IIIa in the presence of thrombin; (3) types I and III collagen; (4) factor VIII (FVIII) gave evidence that the functional activity of purified vWF was similar to that of native plasma vWF. Furthermore the LFB-vWF concentrate was able to promote platelet adhesion to collagen. The release of the therapeutic batches of this product rely presently on their potency measured with the ristocetin cofactor activity (40-70 IU ml-1) and the quantitative evaluation of vWF multimeric distribution studied using electrophoresis in 1.5% agarose. These validated techniques ensure the consistency and haemostatic properties of the different lots of LFB-vWF concentrate.
DOI: 10.1046/j.1365-2516.1998.0040s3040.x
PubMed: 10028317
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pubmed:10028317Le document en format XML
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Mazurier</name><affiliation><nlm:affiliation>Unité de Développement Pré-Clinique, Laboratoire Français du Fractionnement et des Biotechnologies, Lille, France.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1998">1998</date><idno type="RBID">pubmed:10028317</idno><idno type="pmid">10028317</idno><idno type="doi">10.1046/j.1365-2516.1998.0040s3040.x</idno><idno type="wicri:Area/PubMed/Corpus">002646</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002646</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">In vitro evaluation of the haemostatic value of the LFB-von Willebrand factor concentrate.</title><author><name sortKey="Mazurier, C" sort="Mazurier, C" uniqKey="Mazurier C" first="C" last="Mazurier">C. Mazurier</name><affiliation><nlm:affiliation>Unité de Développement Pré-Clinique, Laboratoire Français du Fractionnement et des Biotechnologies, Lille, France.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Haemophilia : the official journal of the World Federation of Hemophilia</title><idno type="ISSN">1351-8216</idno><imprint><date when="1998" type="published">1998</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Collagen (metabolism)</term><term>Factor VIII (metabolism)</term><term>Hemostatics (analysis)</term><term>Hemostatics (metabolism)</term><term>Humans</term><term>Platelet Glycoprotein GPIIb-IIIa Complex (metabolism)</term><term>Platelet Glycoprotein GPIb-IX Complex</term><term>Platelet Membrane Glycoproteins</term><term>Receptors, Cell Surface (metabolism)</term><term>von Willebrand Factor (analysis)</term><term>von Willebrand Factor (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Hemostatics</term><term>von Willebrand Factor</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Collagen</term><term>Factor VIII</term><term>Hemostatics</term><term>Platelet Glycoprotein GPIIb-IIIa Complex</term><term>Receptors, Cell Surface</term><term>von Willebrand Factor</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Humans</term><term>Platelet Glycoprotein GPIb-IX Complex</term><term>Platelet Membrane Glycoproteins</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The structural and functional studies of the concentrate of von Willebrand factor (vWF) manufactured by LFB have been first performed as part of the preclinical development of this product specially intended for the treatment of von Willebrand disease. The electrophoretic analyses showed the high purity of LFB-vWF concentrate (specific activity of 100 IU of ristocetin cofactor activity per milligram of protein) and the multimeric pattern attesting the presence of high molecular weight multimeters (> or = 15-mers). The measurements of vWF capacity to bind to: (1) platelet glycoprotein (GP) Ib in the presence of ristocetin; (2) GPIIb/IIIa in the presence of thrombin; (3) types I and III collagen; (4) factor VIII (FVIII) gave evidence that the functional activity of purified vWF was similar to that of native plasma vWF. Furthermore the LFB-vWF concentrate was able to promote platelet adhesion to collagen. The release of the therapeutic batches of this product rely presently on their potency measured with the ristocetin cofactor activity (40-70 IU ml-1) and the quantitative evaluation of vWF multimeric distribution studied using electrophoresis in 1.5% agarose. These validated techniques ensure the consistency and haemostatic properties of the different lots of LFB-vWF concentrate.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">10028317</PMID><DateCompleted><Year>1999</Year><Month>03</Month><Day>11</Day></DateCompleted><DateRevised><Year>2019</Year><Month>11</Month><Day>02</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1351-8216</ISSN><JournalIssue CitedMedium="Print"><Volume>4 Suppl 3</Volume><PubDate><Year>1998</Year></PubDate></JournalIssue><Title>Haemophilia : the official journal of the World Federation of Hemophilia</Title><ISOAbbreviation>Haemophilia</ISOAbbreviation></Journal><ArticleTitle>In vitro evaluation of the haemostatic value of the LFB-von Willebrand factor concentrate.</ArticleTitle><Pagination><MedlinePgn>40-3</MedlinePgn></Pagination><Abstract><AbstractText>The structural and functional studies of the concentrate of von Willebrand factor (vWF) manufactured by LFB have been first performed as part of the preclinical development of this product specially intended for the treatment of von Willebrand disease. The electrophoretic analyses showed the high purity of LFB-vWF concentrate (specific activity of 100 IU of ristocetin cofactor activity per milligram of protein) and the multimeric pattern attesting the presence of high molecular weight multimeters (> or = 15-mers). The measurements of vWF capacity to bind to: (1) platelet glycoprotein (GP) Ib in the presence of ristocetin; (2) GPIIb/IIIa in the presence of thrombin; (3) types I and III collagen; (4) factor VIII (FVIII) gave evidence that the functional activity of purified vWF was similar to that of native plasma vWF. Furthermore the LFB-vWF concentrate was able to promote platelet adhesion to collagen. The release of the therapeutic batches of this product rely presently on their potency measured with the ristocetin cofactor activity (40-70 IU ml-1) and the quantitative evaluation of vWF multimeric distribution studied using electrophoresis in 1.5% agarose. These validated techniques ensure the consistency and haemostatic properties of the different lots of LFB-vWF concentrate.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Mazurier</LastName><ForeName>C</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Unité de Développement Pré-Clinique, Laboratoire Français du Fractionnement et des Biotechnologies, Lille, France.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Haemophilia</MedlineTA><NlmUniqueID>9442916</NlmUniqueID><ISSNLinking>1351-8216</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D006490">Hemostatics</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D019039">Platelet Glycoprotein GPIIb-IIIa Complex</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D019038">Platelet Glycoprotein GPIb-IX Complex</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010980">Platelet Membrane Glycoproteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011956">Receptors, Cell Surface</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C032193">glycoprotein receptor GPIb-IX</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014841">von Willebrand Factor</NameOfSubstance></Chemical><Chemical><RegistryNumber>9001-27-8</RegistryNumber><NameOfSubstance UI="D005169">Factor VIII</NameOfSubstance></Chemical><Chemical><RegistryNumber>9007-34-5</RegistryNumber><NameOfSubstance UI="D003094">Collagen</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D003094" MajorTopicYN="N">Collagen</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005169" MajorTopicYN="N">Factor VIII</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006490" MajorTopicYN="N">Hemostatics</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="Y">analysis</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019039" MajorTopicYN="N">Platelet Glycoprotein GPIIb-IIIa Complex</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019038" MajorTopicYN="Y">Platelet Glycoprotein GPIb-IX Complex</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010980" MajorTopicYN="Y">Platelet Membrane Glycoproteins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011956" MajorTopicYN="N">Receptors, Cell Surface</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014841" MajorTopicYN="N">von Willebrand Factor</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="Y">analysis</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1999</Year><Month>2</Month><Day>24</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1999</Year><Month>2</Month><Day>24</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1999</Year><Month>2</Month><Day>24</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">10028317</ArticleId><ArticleId IdType="doi">10.1046/j.1365-2516.1998.0040s3040.x</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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