NDLI: Identification of a cleavage site directing the immunochemical detection of molecular abnormalities in type IIA von Willebrand factor.

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Identification of a cleavage site directing the immunochemical detection of molecular abnormalities in type IIA von Willebrand factor.

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Identification of a cleavage site directing the immunochemical detection of molecular abnormalities in type IIA von Willebrand factor.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Dent, J. A. Ware, J. Kasper, C. K. Berkowitz, S. D. Ruggeri, Z. M.
Description	Author Affiliation: Dent JA ( Department of Molecular and Experimental Medicine, Research Institute of Scripps Clinic, La Jolla, CA 92037.);
Abstract	Proteolytic cleavage of the von Willebrand factor subunit may be important for processing and/or function of the molecule and is altered in certain subtypes of von Willebrand disease. It results in the generation of two main fragments with apparent molecular masses of 140 kDa and 176 kDa from the 225-kDa subunit. We have now obtained chemical evidence to locate the protease-sensitive bond between residues Tyr-842 and Met-843, a site that appears to reflect the specificity of calcium-dependent neutral proteases (calpains). Antibodies were raised against four synthetic peptides that represented sequences immediately preceding or following or including the cleavage site. One antibody (against the fragment from Ala-837 through Asp-851) reacted only with the intact subunit, and its epitope included the cleavage site. All others reacted specifically with either the 140-kDa or the 176-kDa fragment, demonstrating their origin from a single cleavage. In samples of purified von Willebrand factor from four of five patients with type IIA von Willebrand disease, the anti-peptide antibodies showed markedly decreased reactivity with either the 140-kDa or the 176-kDa fragment, suggesting the existence of distinct molecular abnormalities clustered around the cleavage site. Thus, in the majority of type IIA patients, a common pathogenetic mechanism may lead to the disappearance of the larger multimers as a consequence of structural changes that may expose a sensitive bond to the action of specific proteases. These studies demonstrate the use of anti-peptide antibodies directed at a relevant structural domain for the immunochemical differentiation of normal and mutant molecules.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	16
Volume Number	87
Language	English
Publisher	National Academy of Sciences
Publisher Date	1990-09-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Mutation Von Willebrand Diseases Genetics Von Willebrand Factor Amino Acid Sequence Amino Acids DNA Immunoblotting Molecular Sequence Data Oligonucleotide Probes Polymerase Chain Reaction Blood Isolation & Purification Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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