Fibrinogen-related protein

Mollusca Gastropods, Bivalves Lectins, PO, AMPs, molluscan defense molecules, fibrinogen related proteins, cytokines... 

Zhang. S. M. and Loker, E. S., Representation of an immune responsive gene family encoding fibrinogen-related proteins in the freshwater mollusk Biomphalaria glabrata, Gene, 341, 255, 2004. 

Yoshino, 1984). Evidence also exists for a variety of soluble factors that may contribute to resistance of the snail to infection, e.g. plasma factors (Bayne et al., 1985), fibrinogen-related proteins (FREPs) (Adema and Loker, 1997) and cytokine-like components (Granath et al., 1994). 

Gorbushin AM, Panchin YV, Iakovleva NV. In search of the origin of FREPs characterization of Aplysia californica fibrinogen-related proteins. Dev Comp Immunol. 2010 34 465-73. 

Lee, E. C., Yu, S. Y., Hu, X., Mlodzik, M., and Baker, N. E. (1998). Functional analysis of the fibrinogen-related scabrous gene from Drosophila melanogaster identifies potential effector and stimulatory protein domains. Genetics 150, 663-673. 

The extracellular domains of integrins interact with a variety of profeins of the extracellular matrix. These include fibronectin, fibrinogen, vifronecfin, collagen, and entacfin. Other large cell surface adhesins include laminin and osteopontin (Chapfer 8), thrombospondin, von Willebrand factor, and related proteins. These adhesins appear to depend upon the sequence Arg-Gly-Asp (RGD), which binds nonco-valently to integrins, which act as cell-surface receptors. See also Chapter 12, Section C,9. 

Courtney HS, Hasty DL, Dale JB. Anti-phagocytic mechanisms of Streptococcus pyogenes binding of fibrinogen to M-related protein. Mol Microbiol 2006 59(3) 936-947. 

Changes in the number of free amino residues alter the modified proteins susceptibility to proteolysis. Albumin chlorination and /V-chloramine formation decreases susceptibility to trypsin digestion. Removing of chloramine residues by treatment with thiosulfate shows that chlorination alters albumin properties by a biphasic mode the reversible chlorination and removal of chloramine moieties markedly increases albumin susceptibility to proteolysis, whereas chlorination produces the irreversible loss of amino moieties and carbonyl group formation effects decrease in albumin susceptibility to trypsin digestion. The effect is related to the number of lost amino residues. A similar relationship was observed for IgG. Fibrinogen and protamine, on the other hand, did not show dependence between chlorination and proneness to trypsin proteolysis (06). 

Fibrates should be used cautiously with warfarin and other coumarins, as the INR may rise significantly. The dose of anticoagulant should be reduced by 50% and then adjusted to INR or PT, using serial measurements [1, 28]. This is in addition to the effect of fibrates on haemoglobin, fibrinogen and antithrombin III, and the interaction may be related to displacement of warfarin from protein-binding site [28]. Fatalities have been reported. 

Fio. 2. Relation between log s and ionic strength of ammonium sulfate for several proteins. From Cohn and Edsall (1943). F = fibrinogen COHb = carboxyhemo-globin PG = pseudoglobulin SA = serum albumin COMb = carboxymyoglobin. 

Adsorption of albumin, y-globulin, and fibrinogen from single solutions onto several hydrophobic polymers was studied using internal reflection IR spectroscopy. The adsorption isotherms have a Langmuir-type form. The calculated rate and amount of protein adsorbed was dependent on the polymer substrate and the flow rate of the solution. Competitive adsorption experiments were also investigated to determine the specific adsorption of each I-labelled protein from a mixture of proteins. Platelet adhesion to these proteinated surfaces is discussed in relation to a model previously proposed. 

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