A heparin binding synthetic peptide from human HIP / RPL29 fails to specifically differentiate between anticoagulantly active and inactive species of heparin

Journal of Negative Results in Biomedicine

Magnus Höök³  Daniel D Carson¹  David E Hoke² 

[1] Department of Biological Sciences; University of Delaware; Newark, Delaware 19716, U.S.A;Current Address: Department of Pathology; University of Melbourne; Parkville, Victoria 3010, Australia;Center for Extracellular Matrix Biology; The Texas A&M University System Health Science Center Institute of Biosciences and Technology; Houston, Texas 77030, U.S.A

关键词: HIP peptide-1;    heparin;    glycosaminoglycan;    antithrombin III;    anticoagulant;   

Others  :  824284
DOI  :  10.1186/1477-5751-2-1

 received in 2002-08-29, accepted in 2003-02-25,  发布年份 2003

【 摘 要 】

Despite extensive progress in determining structures within heparin and heparan sulfate (Hp/HS) and the discovery of numerous proteinaceous binding partners for Hp/HS so far; the only detailed characterization of a specific protein-glycosaminoglycan interaction is antithrombin III (ATIII) binding to a Hp pentasaccharide containing a unique 3-O-sulfated glucosamine residue. Previously, it was reported from our laboratories that a 16 amino acid synthetic peptide derived from the C-terminus of human HIP/RPL29 (HIP peptide-1) enriched for ATIII-dependent anticoagulant activity, presumably by specifically binding the ATIII pentasaccharide. Herein, we demonstrate that HIP peptide-1 cannot enrich ATIII-dependent anticoagulant activity from a starting pool of porcine intestinal mucosa Hp through a bio-specific interaction. However, a HIP peptide-1 column can be used to enrich for anticoagulantly active Hp from a diverse pool of glycosaminoglycans known as Hp byproducts by a mechanism of nonspecific charge interactions. Thus, HIP peptide-1 cannot recognize Hp via bio-specific interactions but binds glycosaminoglycans by non-specific charge interactions.

【 授权许可】

   
2003 Hoke et al; licensee BioMed Central Ltd. This is an Open Access article: verbatim copying and redistribution of this article are permitted in all media for any purpose, provided this notice is preserved along with the article's original URL.

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