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  • Title: Epitope mapping of human VWF A3 recognized by monoclonal antibody SZ-123 and SZ-125 using MALDI mass spectrometry.
    Author: Jiang M, Zhao Y, Shen F, Wang F, He Y, Ruan C.
    Journal: Int J Hematol; 2011 Sep; 94(3):241-247. PubMed ID: 21822587.
    Abstract:
    von Willebrand factor (VWF) serves as a molecular bridge between the constituents of the subendothelium, such as collagen, and receptors of the platelet membrane, primarily GPIb. We have previously reported two monoclonal antibodies (mAbs), SZ-123 and SZ-125, which specifically bind the VWF A3 domain and block the interaction of VWF with collagen type III and ristocetin- or botrocetin-induced platelet aggregation. Here, we identified the epitopes recognized by SZ-123 and SZ-125 using matrix-assisted laser desorption ionization mass spectrometry in combination with proteolysis protection assays. Our results demonstrated that SZ-123 recognizes a discontinuous epitope, involving the residues (989)AHLLSLVDVMQR(1000) and (1017)YLTSEMHGARPGASK(1031) of VWF. SZ-125 recognizes a linear epitope, encompassing the sequence (1001)EGGPSQIGDALGFAVR(1016). Immunoassays further indicated that the synthetic peptide, NH2-EGGPSQIGDALGFAVR-COOH, is sufficient for the binding to SZ-125. These results provide insight into the mechanistic basis for the inhibition of VWF binding to collagen by SZ-123/SZ-125.
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