Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P50583 (asymmetrical)
 12,197 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The present communication describes the production of a new series of murine Mabs against von Willebrand factor (vWf) in which specificity was tested using immunoperoxidase techniques. Seven Mabs showed specific reactivity with native and disaggregated vWf, whereas no binding was found to material from patients with severe homozygous (or doubly heterozygous) von Willebrand's disease (vWd) or factor VIII coagulant antigen (VIII:Ag). These Mabs are thought to carry separate specificities as only slight or no competitive activity was detected. Four Mabs partially inhibited the ristocetin-induced platelet agglutination and three interacted with vWf-binding to type I collagen. All antibodies bound to the complete range of vWf multimers of normal plasma. Excellent binding and detection properties of Mabs were found in asymmetrical two-site enzyme linked immunosorbent assays (ELISA) for quantitation of vWf antigen (vWf:Ag). One particular antibody (Mab vWf-33) discriminated vWf material from a number of subtype II vWd plasmas tested.
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PMID:Applications of immunoperoxidase techniques in specificity testing of monoclonal antibodies (Mabs) against von Willebrand factor (vWf). 326 Jan 53

The sequence of the chicken alpha 2(I) collagen promoter from -712 to -85, relative to exon 1, has been shown to be important for transcriptional activity. Within this region a pyrimidine/purine asymmetrical element at -200 bp forms an in vitro S1 nuclease-sensitive site. The pyrimidine-rich strand of this element interacts specifically with single-stranded DNA-binding proteins present in fibroblast nuclear extracts [Bayarsaihan and Lukens (1996) Biochem. J. 314, 293-296]. To identify these proteins we performed expression screening of a chick embryo fibroblast cDNA library using a single-stranded polypyrimidine sequence derived from this element. One of the isolated clones was found to encode a member of the cold-shock gene family, either chicken YB-1 or a highly homologous protein. This protein and a known chicken Y-box protein were both found to bind sequence-specifically to the pyrimidine-rich strand of the pyrimidine/purine asymmetrical element in the chicken alpha 2(I) collagen promoter. The binding mechanism of these proteins could be based on the formation of a non-canonical triplex DNA structure (H-DNA). Although members of this widespread and conserved protein family have been reported to modulate the expression of a number of genes, the findings reported here provide the first evidence for a possible role of cold-shock proteins in the regulation of type I collagen genes.
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PMID:Y-box proteins interact with the S1 nuclease-sensitive site in the chicken alpha 2(I) collagen gene promoter. 887 Jun 70