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Thromb Haemost 1998; 80(04): 677-685
DOI: 10.1055/s-0037-1615441
Rapid Communication
Schattauer GmbH

Porcine Platelet von Willebrand Antigen II (vW AgII): Inhibitory Effect on Collagen-induced Aggregation and Comparative Distribution with Human Platelets

Teresa Royo
1   From the Cardiovascular Research Center, CSIC-Hospital de la Santa Creu i Sant Pau-UAB
2   From the Institut de Recerca Hospital de la Santa Creu i Sant Pau, Barcelona, Spain
,
Matilde Vidal
1   From the Cardiovascular Research Center, CSIC-Hospital de la Santa Creu i Sant Pau-UAB
,
Lina Badimon
1   From the Cardiovascular Research Center, CSIC-Hospital de la Santa Creu i Sant Pau-UAB
› Author AffiliationsSupported in part by FISss 95/1381, Marató TV3-Malaltíes Cardíaques/ 96-10, Fundación de Investigación Cardiovascular (FIC)-Catalana Occidente and Fundación Española de Arteriosclerosis (FEA)
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Publication History

Received 04 December 1997

Accepted after resubmission 15 May 1998

Publication Date:
08 December 2017 (online)

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Summary

Von Willebrand factor (vWF) is synthesized by human endothelial cells and megakaryocytes as a large precursor, the pre-provWF, which is finally cleaved into the propolypeptide of vWF (pp-vWF) and the mature vWF. We have purified in parallel the pp-vWF and the GP IIb-IIIa from porcine platelets. The N-terminus comparative analysis of porcine pp-vWF with respect to other species revealed more than a 75% and 65% homology with the bovine and human pp-vWF, respectively. Purified pp-vWF inhibited collagen-induced platelet aggregation in porcine platelet rich plasma (PRP) and specifically binds to collagen. Polyclonal antibody pabBp19 against the purified protein was prepared and characterized by ELISA, Western-blot and immunocytochemistry. The distribution of pp-vWF in soluble and membrane fractions from pig platelets has been performed by immunolabeling detection. pabBp19 did not blot human platelet lysates but human pp-vWF was detectable using the antibody Frieda 013091. Cell distribution and quantification studies of human and porcine platelet pp-vWF showed that the protein exists in the soluble and membrane fractions and its pattern is similar in both species.

 

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