A Peptide Sequence of Heparin/Heparan Sulfate (HP/HS)-interacting Protein Supports Selective, High Affinity Binding of HP/HS and Cell Attachment

Liu, Shouchun; Julian, JoAnne; Carson, Daniel D.

doi:10.1074/jbc.273.16.9718

Cited by 31 publications

(35 citation statements)

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“…This is consistent with its expression pattern in the human and its suggested role as a Hp/HS-dependent adhesion promoting protein for embryo attachment to the uterine epithelium (6). In previous studies, it was shown that human HIP and a peptide domain within human HIP supports cell attachment of human trophoblast cell lines (8,9). HIP is normally expressed by human trophoblasts in close apposition to perlecan-enriched matrices of the fetal-maternal interface (30).…”

Section: Discussionsupporting

confidence: 63%

“…Purified human HIP as well as a recombinant HIP protein expressed in Escherichia coli were shown to bind Hp selectively and saturably and also support Hp/HS-dependent cell adhesion (8). In addition to reports on HIP protein, a peptide sequence within HIP has been shown to bind specific Hp/HS sequences within the Hp/HS chain (9). Notably, this peptide domain binds the same Hp/HS pentasaccharide that is recognized by the anticoagulant protein, antithrombin III (10).…”

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confidence: 99%

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Murine HIP/L29 Is a Heparin-binding Protein with a Restricted Pattern of Expression in Adult Tissues

Hoke

Regisford

Julian

et al. 1998

Journal of Biological Chemistry

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Heparin/heparan sulfate (Hp/HS)-binding proteins are implicated in a variety of cell biological processes including cell adhesion, modulation of blood coagulation, and cytokine/growth factor action. Hp/HS-interacting protein (HIP) has been identified in various adult tissues in humans. HIP supports high affinity, selective binding to Hp/HS, promotes cell adhesion, and modulates blood coagulation activities via Hp/HS-dependent mechanisms. Herein, a murine ortholog of human HIP is described that is 78.8% identical to human HIP and 99.8% identical at the cDNA level and identical at the amino acid level to a previously described murine ribosomal protein, L29. Western blot analyses and immunohistological staining with affinity-purified antibodies generated against two distinct peptide sequences of murine HIP/L29 indicate that HIP/L29 is differentially expressed in adult murine tissues and cell types. In the normal murine mammary epithelial cell line, NMuMG, HIP/L29 is enriched in the 100,000 ؋ g particulate fraction. HIP/L29 can be solubilized from the 100,000 ؋ g particulate fraction with 0.8 M NaCl, suggesting that it is a peripheral membrane protein. HIP/L29 directly binds 125 I-Hp in gel overlay assays and requires 0.75 M NaCl for elution from Hp-agarose. In addition, recombinant murine HIP expressed in Escherichia coli binds Hp in a saturable and highly selective manner, compared with other glycosaminoglycans including dermatan sulfate, chondroitin sulfate, keratan sulfate, and hyaluronic acid. Collectively, these data indicate that murine HIP/ L29, like its human ortholog, is a Hp-binding protein expressed in a restricted manner in adult tissues.

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Section: Discussionsupporting

confidence: 63%

mentioning

confidence: 99%

Murine HIP/L29 Is a Heparin-binding Protein with a Restricted Pattern of Expression in Adult Tissues

Hoke

Regisford

Julian

et al. 1998

Journal of Biological Chemistry

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“…* To whom correspondence should be addressed. Telephone: 951-827-3585, Fax: 951-827-2435, E-mail: dlrab@ucrac1.ucr [25][26][27][28].…”

Section: Introductionmentioning

confidence: 99%

“…The heparin-binding domain was found to have the sequence CRPKAKAKAKAKDQTK (26). A synthetic peptide of the same sequence (HIP peptide) competes with AT for heparin and neutralizes the anticoagulant activity of heparin in blood plasma assays (26), which suggests that HIP peptide or peptides with similar sequences may have potential as clinical agents for neutralization of the anticoagulant activity of heparin (25)(26)(27)(28).…”

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confidence: 99%

“…* To whom correspondence should be addressed. Telephone: 951-827-3585, Fax: 951-827-2435, E-mail: dlrab@ucrac1.ucr [25][26][27][28].In this paper, we report on the interaction of heparin with two synthetic analogs of HIP peptide: Ac-SRGKAKVKAKVKDQTK-NH 2 and the same peptide synthesized with all D-amino acids, L-HIP analog peptide (L-HIPAP) and D-HIPAP, respectively. As compared to HIP peptide, the N-terminus has been acetylated and the C-terminus amidated to eliminate end group effects, the cysteine residue has been substituted by serine to eliminate dimerization by disulfide bond formation, the proline has been substituted by glycine to eliminate cis/trans isomerism across the arginine-proline peptide bond, and two alanine residues have been replaced by valine to facilitate characterization of the interaction of the peptides with heparin by NMR.…”

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Interaction of Heparin with Two Synthetic Peptides that Neutralize the Anticoagulant Activity of Heparin

Wang

Rabenstein

2006

Biochemistry

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Two synthetic analogs of the heparin-binding domain of heparin/heparan sulfate-interacting protein: Ac-SRGKAKVKAKVKDQTK-NH 2 and the all-D-amino acid version of the same peptide (L-HIPAP and D-HIPAP, respectively) were synthesized and their efficacy as agents for neutralization of the anticoagulant activity of heparin was assayed. The two analog peptides were found to be equally effective for neutralization of the anticoagulant activity of heparin, as measured by restoration of the activity of serine protease Factor Xa by the Coatest Heparin Method. The finding that L-HIPAP and D-HIPAP are equally effective suggests that D-amino acid peptides show promise as proteolytically stable therapeutic agents for neutralization of the anticoagulant activity of heparin. The interaction of L-HIPAP and D-HIPAP with heparin was characterized by 1 H NMR, isothermal titration calorimetry (ITC) and heparin affinity chromatography. The two peptides were found to interact identically with heparin. Analysis of the dependence of heparin-peptide binding constants on Na + concentration by counterion condensation theory indicates that, on average, 2.35 Na + ions are displaced from heparin per peptide molecule bound and one peptide molecule binds per hexasaccharide segment of heparin. The analysis also indicates that both ionic and nonionic interactions contribute to the binding constant, with the ionic contribution decreasing as the Na + concentration increases.Heparin, a linear polysaccharide comprised of highly sulfated 1→4 linked uronic acid-(1→4)-D-glucosamine repeating disaccharide units, has been used clinically as an anticoagulant for more than half a century (1,2). Other biological activities include release of lipoprotein lipase and hepatic lipase (3,4), regulation of complement activation (5), regulation of angiogenesis and tumor growth (6-8), regulation of Burkitt's lymphoma growth (9), modulation of inflammation (10) and antiviral activity (11)(12)(13)(14)(15). The biological activity of heparin results from its interaction with proteins, and hundreds of proteins have been shown to interact with heparin (2,(16)(17)(18).Heparin functions as an anticoagulant by binding to antithrombin III (AT 1 ), a serine protease inhibitor that mediates the coagulation cascade; binding causes a conformational change that accelerates inhibition of serine protease factor Xa by AT (19). In some clinical situations, for example where extracorporeal blood circulation is necessary or when patients experience moderate to severe bleeding, the anticoagulant activity must be neutralized to reduce the risk of hemorrhagic hazard. Protamine, a complex mixture of arginine-rich peptides, is used for this purpose. However, protamine can induce life-threatening side effects, such as hypotension + This work was supported in part by National Institutes of Health Grant HL56588. Funding for the Varian Inova 500 spectrometer was provided in part by NSF-ARI Grant 9601831. ‡ Present address: Momenta Pharmaceuticals, Boston MA. * To whom correspondence shou...

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Heparan sulfate proteoglycans: Coordinators of multiple signaling pathways during chondrogenesis

Kirn‐Safran

Gomes

Brown

et al. 2004

Birth Defects Research Pt C

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Heparan sulfate proteoglycans are abundantly expressed in the pericellular matrix of both developing and mature cartilage. Increasing evidence indicates that the action of numerous chondroregulatory molecules depends on these proteoglycans. This review summarizes the current understanding of the interactions of heparan sulfate chains of cartilage proteoglycans with both soluble and nonsoluble ligands during the process of chondrogenesis. In addition, the consequences of mutating genes encoding heparan sulfate biosynthetic enzymes or heparan sulfate proteoglycan core proteins on cartilage development are discussed.

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A Peptide Sequence of Heparin/Heparan Sulfate (HP/HS)-interacting Protein Supports Selective, High Affinity Binding of HP/HS and Cell Attachment

Cited by 31 publications

References 36 publications

Murine HIP/L29 Is a Heparin-binding Protein with a Restricted Pattern of Expression in Adult Tissues

Murine HIP/L29 Is a Heparin-binding Protein with a Restricted Pattern of Expression in Adult Tissues

Interaction of Heparin with Two Synthetic Peptides that Neutralize the Anticoagulant Activity of Heparin

Heparan sulfate proteoglycans: Coordinators of multiple signaling pathways during chondrogenesis

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