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Gene Review

HABP2  -  hyaluronan binding protein 2

Homo sapiens

Synonyms: FSAP, Factor VII-activating protease, Factor seven-activating protease, HABP, HGFAL, ...
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Disease relevance of HABP2


Psychiatry related information on HABP2

  • Significant differences were observed in the various evaluation scales FSAP (general ability to solve problems), FSSW (general self-esteem), SGKB (state of health), and SKEF (physical fitness) [6].

High impact information on HABP2

  • The G534E polymorphism (Marburg I [MI]) of factor VII-activating protease (FSAP) is associated with carotid stenosis and cardiovascular disease [7].
  • We have previously demonstrated that FSAP is present in atherosclerotic plaques and it is a potent inhibitor of vascular smooth muscle proliferation and migration in vitro [7].
  • These include the ability of a peptide that specifically binds HA (HABR) to reduce locomotion, the ability of HA (0.001-0.1 micrograms/ml), added at 10-30 h after induction to stimulate locomotion back to the original, acute rate, and the ability of an mAb specific to a 56-kD fibroblast HABP to block locomotion [8].
  • Hyaluronan (HA) and one of its cell binding sites, fibroblast hyaluronan binding protein (HABP), is shown to contribute to the regulation of 10T1/2 cell locomotion that contain an EJ-ras-metallothionein (MT-1) hybrid gene [8].
  • Further, both HA and HABP products are regulated by induction of the ras gene [8].

Biological context of HABP2


Anatomical context of HABP2


Associations of HABP2 with chemical compounds

  • With the help of enzyme-linked immunosorbent assay (ELISA) and iodinated [125I]HABP, it has been shown that kidney HABP binds specifically to hyaluronic acid (HA) amongst all the glycosaminoglycans (GAGs), however, HABP can interact with other matrix proteins, e.g., laminin, fibronectin, and collagen type IV [10].
  • A serine protease isolated from plasma sharing structural characteristics with a hepatocyte growth factor activator-like protease has been demonstrated recently to activate FVII [15].
  • The (auto-)activation of FSAP is facilitated by polyanionic glycosaminoglycans, such as heparin or dextran sulphate, whereas calcium ions stabilize the active form of FSAP [14].
  • In a purified system, natural RNA augmented the FSAP-dependent Factor VII activation several-fold (as shown by subsequent Factor Xa generation), as well as the FSAP-mediated generation of urokinase [14].
  • The distribution of a hyaluronate-binding (HABP) and rhodamine B-isothiocyanate (RITC)-labeled hyaluronate (HA) were studied on both actively motile and stationary chick heart fibroblasts to assess the relationship of these molecules to each other, to other extracellular matrix molecules, to membrane protrusions and to adhesion sites [16].

Regulatory relationships of HABP2

  • PHBP did not cleave (activate) prothrombin and plasminogen, but it converted the inactive single chain urinary plasminogen activator to the active two chain form [17].

Other interactions of HABP2

  • The results showed that fibrinogen and fibronectin were the major substrates of PHBP [17].
  • Later on FSAP was identified as a potent activator of single chain plasminogen activators, in particular of prourokinase, as well [11].
  • Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis of HABP under reducing as well as nonreducing conditions revealed a single protein band of 34 kDa, thus indicating that kidney HABP is a homodimer and lacks interchain disulfide bond [10].
  • RNase A, but not other hydrolytic enzymes (proteases, glycanases and DNase), abolished the FSAP cofactor activity, which was subsequently isolated by anion-exchange chromatography and unequivocally identified as RNA [14].

Analytical, diagnostic and therapeutic context of HABP2

  • The objective of this case-control study was to assess FSAP Marburg I's role in the occurrence of venous thromboembolism (VTE) [3].
  • Polyclonal antibodies were raised against it, and the monospecificity of the antibodies towards HABP was confirmed by Western blot analysis of tissue extracts [10].
  • The specific binding of FSAP to RNA (but not to DNA) was shown by mobility-shift assays and UV crosslinking, thereby identifying FSAP as a new extracellular RNA-binding protein, the K(D) estimated to be 170-350 nM [14].
  • We further characterized the expression of WF-HABP in vivo and found that its expression colocalized with CD31-positive cells and was prominently expressed in microvessels in the human aorta and in atherectomy samples [18].
  • RITC-HA and HABP, detected by indirect immunofluorescence, were concentrated in the perinuclear region, the leading lamella and retraction processes of actively motile cells, although RITC-HA also occurred diffusely over the rest of the cell body [16].


  1. Novel candidate tumor marker genes for lung adenocarcinoma. Wang, K.K., Liu, N., Radulovich, N., Wigle, D.A., Johnston, M.R., Shepherd, F.A., Minden, M.D., Tsao, M.S. Oncogene (2002) [Pubmed]
  2. Marburg I polymorphism of factor VII-activating protease and risk of venous thromboembolism. Franchi, F., Martinelli, I., Biguzzi, E., Bucciarelli, P., Mannucci, P.M. Blood (2006) [Pubmed]
  3. Marburg I polymorphism of factor VII-activating protease is associated with idiopathic venous thromboembolism. Hoppe, B., Tolou, F., Radtke, H., Kiesewetter, H., Dörner, T., Salama, A. Blood (2005) [Pubmed]
  4. The Marburg I polymorphism of factor VII-activating protease is not associated with venous thrombosis. van Minkelen, R., de Visser, M.C., Vos, H.L., Bertina, R.M., Rosendaal, F.R. Blood (2005) [Pubmed]
  5. The factor VII activating protease G511E (Marburg) variant and cardiovascular risk. Ireland, H., Miller, G.J., Webb, K.E., Cooper, J.A., Humphries, S.E. Thromb. Haemost. (2004) [Pubmed]
  6. Changes in self-concept and body image during alopecia induced cancer chemotherapy. Münstedt, K., Manthey, N., Sachsse, S., Vahrson, H. Supportive care in cancer : official journal of the Multinational Association of Supportive Care in Cancer. (1997) [Pubmed]
  7. The G534E polymorphism of the gene encoding the factor VII-activating protease is associated with cardiovascular risk due to increased neointima formation. Sedding, D., Daniel, J.M., Muhl, L., Hersemeyer, K., Brunsch, H., Kemkes-Matthes, B., Braun-Dullaeus, R.C., Tillmanns, H., Weimer, T., Preissner, K.T., Kanse, S.M. J. Exp. Med. (2006) [Pubmed]
  8. Hyaluronan and a cell-associated hyaluronan binding protein regulate the locomotion of ras-transformed cells. Turley, E.A., Austen, L., Vandeligt, K., Clary, C. J. Cell Biol. (1991) [Pubmed]
  9. Isolation and characterization of the plasma hyaluronan-binding protein (PHBP) gene (HABP2). Sumiya, J., Asakawa, S., Tobe, T., Hashimoto, K., Saguchi, K., Choi-Miura, N.H., Shimizu, Y., Minoshima, S., Shimizu, N., Tomita, M. J. Biochem. (1997) [Pubmed]
  10. Purification, partial characterization of rat kidney hyaluronic acid binding protein and its localization on the cell surface. Gupta, S., Batchu, R.B., Datta, K. Eur. J. Cell Biol. (1991) [Pubmed]
  11. Factor VII activating protease (FSAP): a novel protease in hemostasis. Römisch, J. Biol. Chem. (2002) [Pubmed]
  12. Purification and characterization of a novel hyaluronan-binding protein (PHBP) from human plasma: it has three EGF, a kringle and a serine protease domain, similar to hepatocyte growth factor activator. Choi-Miura, N.H., Tobe, T., Sumiya, J., Nakano, Y., Sano, Y., Mazda, T., Tomita, M. J. Biochem. (1996) [Pubmed]
  13. The frequent Marburg I polymorphism impairs the pro-urokinase activating potency of the factor VII activating protease (FSAP). Roemisch, J., Feussner, A., Nerlich, C., Stoehr, H.A., Weimer, T. Blood Coagul. Fibrinolysis (2002) [Pubmed]
  14. Extracellular RNA is a natural cofactor for the (auto-)activation of Factor VII-activating protease (FSAP). Nakazawa, F., Kannemeier, C., Shibamiya, A., Song, Y., Tzima, E., Schubert, U., Koyama, T., Niepmann, M., Trusheim, H., Engelmann, B., Preissner, K.T. Biochem. J. (2005) [Pubmed]
  15. The FVII activating protease cleaves single-chain plasminogen activators. Römisch, J., Vermöhlen, S., Feussner, A., Stöhr, H. Haemostasis (1999) [Pubmed]
  16. Localization of hyaluronate and hyaluronate-binding protein on motile and non-motile fibroblasts. Turley, E.A., Torrance, J. Exp. Cell Res. (1985) [Pubmed]
  17. Identification of the substrates for plasma hyaluronan binding protein. Choi-Miura, N.H., Yoda, M., Saito, K., Takahashi, K., Tomita, M. Biol. Pharm. Bull. (2001) [Pubmed]
  18. Identification and characterization of three cDNAs that encode putative novel hyaluronan-binding proteins, including an endothelial cell-specific hyaluronan receptor. Tsifrina, E., Ananyeva, N.M., Hastings, G., Liau, G. Am. J. Pathol. (1999) [Pubmed]
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