Histidine-rich glycoproteins

The high affinity LBS is involved in the interaction of plasminogen with fibrin, a2-antiplasmin, and a plasmin inhibitor called histidine-rich glycoprotein. It has been observed that plasminogen activation takes place on the surface of fibrin and that a2-antiplasmin competitively inhibits the plasminogen—fibrin interaction at the high affinity LBS. 

Leung L Saigo K., Grant D. Heparin binds to human monocytes and modulates their procoagulant activities and secretory phenotypes. Effect of histidine-rich glycoprotein. Blood 1989 73, 177-84. 

Burch, M.K. and Morgan, W.T. (1985) Preferred heme binding sites of histidine-rich glycoprotein. Biochemistry 24, 5919-5924. 

Koide, T., Foster, D.C., Yoshitake, S. and Davie, E.W. (1986) Amino acid sequence of human histidine-rich glycoprotein derived from the nucleotide sequence of its cDNA. Biochemistry 25, 2220-2225. 

Morgan, W.T. (1981) Interactions of the histidine-rich glycoprotein of serum with metals. Biochemistry 20, 1054-1061. 

Sazuka, M., Itoi, T., Suzuki, Y., Odani, S., Koide, T., and Isemura, M., Evidence for the interaction between (—)-epigallocatechin gallate and human plasma proteins fibronectin, fibrinogen, and histidine-rich glycoprotein, Biosci. Biotechnol. Biochem., 60, 1317, 1996. 

Blank, M. and Shoenfeld, Y. (2008). Histidine-rich glycoprotein modulation of immune/ autoimmune, vascular, and coagulation systems. Clin. Rev. Allergy Immunol. 34,307-312. 

Manderson, G. A., Martin, M., Onnerfjord, P., Saxne, T., Schmidtchen, A., Mollnes, T. E., Heinegard, D., and Blom, A. M. (2009). Interactions of histidine-rich glycoprotein with immunoglobulins and proteins of the complement system. Mol. Immunol. 46, 3388-3398. 

Poon, I. K., Flulett, M. D., and Parish, C. R. (2010). Histidine-rich glycoprotein is a novel plasma pattern recognition molecule that recruits IgG to facilitate necrotic cell clearance via FcgammaRI on phagocytes. Blood 115, 2473-2482. 

Neural Membrance Protein Transposon Cytochrome c oxidase Cytochrome b Histidine rich glycoprotein BKM-like protein ATP synthase Ankyrin... 

Peterson CB, Morgan WT, Blackburn MN. Histidine-rich glycoprotein modulation of the anticoagulant activity of heparin. J Biol Chem 1987 262 7567-7574. 

Engesser L, Kluft C, Briet E, Brommer E. Familial elevation of plasma histidine-rich glycoprotein in a family with thrombophilia. BrJ Haematol 1987 67 355-358. 

These templates, like HRPll, were shown to promote HZ formation at a parasite DV relevant pH 4.0-4.5. In fact, HRPll is active from pH 4.5 to pH 6.0. HZ formation slows at pH values below 2.0 and above 5.0 (22). Although an increase in pH does cause an increase in binding of heme to HRPll, the HZ produced actually decreases leading, instead, to the formation of p.-oxo-heme dimers (22). Therefore, the bis-histidyl heme binding observed on other proteins like histidine-rich glycoprotein (HRG) at physiologic pH 7.0 differs from the HRPll nucle-ation of HZ in the parasite s acidic DV (23), although a pH 7 HRPll model was attempted by Schneider and Marietta in 2005... 

Chang N-S, Leu RW, Rummage ja, Anderson JK, Mole JE. R adon of complement functional efficiency by histidine-rich glycoprotein. Blood 79 2973-2980,1992. 

The following inhibitors are synthesized in the hver, independently of vitamin K AT 111, protein C inhibitor, Cpesterase inhibitor, a2-macroglobulin, histidine-rich glycoprotein, etc. 

Tab. 35.4 Abnormal coagulation factors, coagulation inhibitors and fibrinolytic system values in hepatic cirrhosis (TPT = thromboplastin time PTT = partial thromboplastin time HRGP = histidine-rich glycoprotein t-PA = tissue plasminogen activator)...

Based on the observation that the octapeptide repeats share the sequence PHG with the histidine-rich glycoprotein, which is thought to be involved in plasma copper transport, Hornshaw et al. (1995a) bypoth-... 

Silverstein, R.L., Leung, L.K., Harpel, P.C. and Nachman, R.L. (1986). Platelet thrombospondin forms a trimolecular complex with plasminogen and histidine-rich glycoprotein. ]. Clin. Invest., 75, 2065-2073... 

Selenoprotein P is a glycoprotein the sequence of the protein moiety within it, having a molecular mass of about 41 kDa, was deduced from the nucleotide sequence of the rat gene. It is unique since, dependent on the organism, it contains more than a dozen selenocysteine residues per monomer. The sequence also contains histidine- and cysteine-rich stretches, which could be involved in metal binding. Other... 

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