title: A heparin binding synthetic peptide from human HIP / RPL29 fails to specifically differentiate between anticoagulantly active and inactive species of heparin.
abstract: 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.
authors.affiliation: Center for Extracellular Matrix Biology; The Texas A&M University System Health Science Center, Institute of Biosciences and Technology, Houston, Texas 77030, USA. dehoke@unimelb.edu.au
authors.forename: David E
authors.initials: DE
authors.lastname: Hoke
authors.forename: Daniel D
authors.initials: DD
authors.lastname: Carson
authors.forename: Magnus
authors.initials: M
authors.lastname: Höök
mesh_terms: D000818:Animals; D000925:Anticoagulants / Q000494:pharmacology*; D000990:Antithrombin III; D001665:Binding Sites; D001779:Blood Coagulation Factors / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D002846:Chromatography, Affinity; D002852:Chromatography, Ion Exchange; D006025:Glycosaminoglycans / Q000378:metabolism; D006493:Heparin / Q000145:classification* / Q000302:isolation & purification / Q000378:metabolism; D006801:Humans; D007413:Intestinal Mucosa; D010446:Peptide Fragments / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D016601:RNA-Binding Proteins; D012269:Ribosomal Proteins; D013552:Swine
chemical_list: D000925:Anticoagulants; D001779:Blood Coagulation Factors; D006025:Glycosaminoglycans; D010446:Peptide Fragments; D016601:RNA-Binding Proteins; C104946:RPL29 protein, human; D012269:Ribosomal Proteins; D000990:Antithrombin III; D006493:Heparin