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dc.contributor.authorVan de Westerlo, Els M.A.
dc.contributor.authorSmetsers, Toon F.C.M.
dc.contributor.authorDennissen, Michel A.B.A.
dc.contributor.authorLinhardt, Robert J.
dc.contributor.authorVeerkamp, Jacques H.
dc.contributor.authorVan Muijen, Goos N.P.
dc.contributor.authorVan Kuppevelt, Toin H.
dc.identifier.citationHuman Single Chain Antibodies Against Heparin: Selection, Characterization and Effect on Coagulation, E.M.A. van de Westerlo, T.F.C.M. Smetsers, M.A.B.A. Dennissen, R.J. Linhardt, J.H. Veerkamp, G.N.P. van Muijen, T.H. van Kuppevelt, Blood, 99, 2427-2433, 2002.
dc.descriptionBlood, 99, 2427-2433
dc.descriptionNote : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
dc.description.abstractHeparin, located in mast cells and basophilic granulocytes, is widely used as an anticoagulant. It belongs to a class of linear polysaccharides called glycosaminoglycans (GAGs). Using phage display technology, we have selected 19 unique human antiheparin antibodies. Some antibodies react almost exclusively with heparin, others also react with the structurally related heparan sulfate, and some with chondroitin sulfate. In all cases, sulfate groups are essential for binding. For activity of some antibodies, O-sulfation is more important than N-sulfation. Antibodies are reactive with heparin in mast cells. Each antibody showed a defined staining pattern on cryosections of rat kidney, pancreas, and testis. Enzymatic digestion with glycosidases on tissue sections further indicated that the antibodies are specific for GAGs. All antibodies recognize a unique epitope. The effect of the antibodies on heparin as an anticoagulant was also studied. There were 3 antibodies that were very effective inhibitors of heparin action in the activated partial thromboplastin time (APTT) clotting assay, and their effect was related to the amount of heparin bound. Some antibodies reacted strongly with the pentasaccharide, which interacts with antithrombin III. The human antibodies selected represent unique tools to study the structure, location, and function of heparin and related GAGs, and some may be used as blocking agents.
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleHuman Single Chain Antibodies Against Heparin: Selection, Characterization and Effect on Coagulation
dc.rights.holderIn Copyright : this Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s).
dc.relation.departmentThe Linhardt Research Labs.
dc.relation.departmentThe Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)

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