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CFP  -  complement factor properdin

Homo sapiens

 
 
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Disease relevance of CFP

 

Psychiatry related information on CFP

 

High impact information on CFP

  • Properdin deficiency with IgA nephropathy [5].
  • The C3-activator fragment of the properdin complex was identified in fresh serum samples obtained from two of the three patients with circulating cryoprotein complexes and arthritis [6].
  • Taken together, these findings are consistent with activation of C3 and the terminal complement sequence, C5-C9, occurring primarily by the properdin pathway, in patients with gram-negative bacteremia eventuating in shock [7].
  • A highly conserved amino-acid sequence in thrombospondin, properdin and in proteins from sporozoites and blood stages of a human malaria parasite [8].
  • The ability of B. rodhaini to penetrate red cells depends on factors of the alternative complement pathway (properdin and factor B) as well as ionic magnesium and the third (C3) and the fifth (C5) components of complement [9].
 

Chemical compound and disease context of CFP

 

Biological context of CFP

 

Anatomical context of CFP

 

Associations of CFP with chemical compounds

  • Analysis of the interaction between properdin and factor B, components of the alternative-pathway C3 convertase of complement [14].
  • The 140 kDa B-P conjugate formed was cleaved by Factor D to yield a single product of 85 kDa [14].
  • Fluid-phase complexes of the purified components C3i, B and P were probed with the homobifunctional cross-linking reagent disuccinimidyl tartarate, and efficient cross-linking of B to P was observed [14].
  • Cleavage of the third complement component (C3) and generation of the spasmogenic peptide, C3a, in human serum via the properdin pathway: demonstration of inhibitory as well as enhancing effects of epsilon-amino-caproic acid [18].
  • The dysfunctional properdin was found to be caused by a single T to G mutation in exon 9, which gives rise to a substitution of a tyrosine by an aspartic acid residue at position 387 [13].
 

Physical interactions of CFP

  • The interactions of properdin with both surface-bound and fluid-phase C3 (the third component of complement) and its activation products have been investigated by using a purified preparation of the 'native' form [10].
  • The antiangiogenic activity of TSP-1 is mediated by the binding of properdin-like type I repeats to the receptor CD36 [19].
  • Properdin-stabilized C5 convertase sites were assembled on the non-activating cells of the alternative pathway, sheep erythrocytes (Es), and on the activating cells, desialated Es and rabbit erythrocytes (Er) [20].
 

Regulatory relationships of CFP

  • In serum the inhibitory effect of 1 M EACA on C3bINA appears to allow escape of the properdin system from its control and thus to increase its net activity toward C3 despite inhibition of the enzymic reactions proper [18].
  • To further elucidate the potential immuno-modulatory functions of flavanol-rich cocoa, the present investigation examined whether isolated CFP fractions (monomers through decamers) influence the secretion of tumor necrosis factor-alpha (TNF-alpha) from resting and phytohemagluttinin (PHA)-stimulated human peripheral blood mononuclear cells (PBMC) [21].
 

Other interactions of CFP

  • Analysis of the interactions between properdin, the third component of complement (C3), and its physiological activation products [10].
  • In contrast, the affinities of properdin for fluid-phase C3b, iC3b and C3c (the larger product of Factors I and H or CR1 (the C3b receptor) action on iC3b) were all very similar, and apparently much weaker than that for cell-bound C3b [10].
  • Serum amyloid A, properdin, complement 3, and toll-like receptors are expressed locally in human sinonasal tissue [22].
  • The deposited MBL/MASP-1 was observed to associate with C3b/C3c and C5b-9 but not with IgG, IgM, C1q, C4c, or properdin [23].
  • The ELISA detects the third component of complement (C3b), proteolytic fragment of complement Factor B (Bb), and properdin (P) complex or its derivative product, C3b,P [24].
 

Analytical, diagnostic and therapeutic context of CFP

  • This places PFC in the region Xp11.3-Xp11.23, thus refining previous in situ hybridization data [11].
  • Subcellular fractionation using Percoll density gradients and Western blot analyses revealed that the bulk of properdin is contained in the secondary granules [16].
  • In this study I used surface plasmon resonance assays to examine properdin interactions with C3b and factor B. I demonstrated that properdin promotes the association of C3b with factor B and provides a focal point for the assembly of C3bBb on a surface [25].
  • Northern blot analysis indicated that the mRNA for human properdin is approximately 1.5 kb long and that its level in U-937 cells is increased by pretreating the cells with phorbol 12-myristate 13-acetate (PMA) [26].
  • Molecular cloning of the cDNA coding for properdin, a positive regulator of the alternative pathway of human complement [26].

References

  1. Complement system in pneumococcal infections. Reed, W.P., Davidson, M.S., Williams, R.C. Infect. Immun. (1976) [Pubmed]
  2. Localization of the properdin structural locus to Xp11.23-Xp21.1. Goundis, D., Holt, S.M., Boyd, Y., Reid, K.B. Genomics (1989) [Pubmed]
  3. Properdin deficiency in a family with fulminant meningococcal infections. Sjöholm, A.G., Braconier, J.H., Söderström, C. Clin. Exp. Immunol. (1982) [Pubmed]
  4. Association between combined properdin and mannose-binding lectin deficiency and infection with Neisseria meningitidis. Bathum, L., Hansen, H., Teisner, B., Koch, C., Garred, P., Rasmussen, K., Wang, P. Mol. Immunol. (2006) [Pubmed]
  5. Properdin deficiency with IgA nephropathy. Wyatt, R.J., Julian, B.A., Galla, J.H. N. Engl. J. Med. (1981) [Pubmed]
  6. Arthritis associated with intestinal-bypass procedure for morbid obesity. Complement activation and characterization of circulating cryoproteins. Wands, J.R., LaMont, J.T., Mann, E., Isselbacher, K.J. N. Engl. J. Med. (1976) [Pubmed]
  7. Activation of the properdin pathway of complement in patients with gram-negative of bacteremia. Fearon, D.T., Ruddy, S., Schur, P.H., McCabe, W.R. N. Engl. J. Med. (1975) [Pubmed]
  8. A highly conserved amino-acid sequence in thrombospondin, properdin and in proteins from sporozoites and blood stages of a human malaria parasite. Robson, K.J., Hall, J.R., Jennings, M.W., Harris, T.J., Marsh, K., Newbold, C.I., Tate, V.E., Weatherall, D.J. Nature (1988) [Pubmed]
  9. Babesia rodhaini: requirement of complement for penetration of human erythrocytes. Chapman, W.E., Ward, P.A. Science (1977) [Pubmed]
  10. Analysis of the interactions between properdin, the third component of complement (C3), and its physiological activation products. Farries, T.C., Lachmann, P.J., Harrison, R.A. Biochem. J. (1988) [Pubmed]
  11. Genetic and physical mapping around the properdin P gene. Coleman, M.P., Murray, J.C., Willard, H.F., Nolan, K.F., Reid, K.B., Blake, D.J., Lindsay, S., Bhattacharya, S.S., Wright, A., Davies, K.E. Genomics (1991) [Pubmed]
  12. Activation of the alternative (properdin) pathway by divalent cations. Lew, F.T., Yukiyama, Y., Waks, H.S., Osler, A.G. J. Immunol. (1975) [Pubmed]
  13. Molecular characterization of properdin deficiency type III: dysfunction produced by a single point mutation in exon 9 of the structural gene causing a tyrosine to aspartic acid interchange. Fredrikson, G.N., Westberg, J., Kuijper, E.J., Tijssen, C.C., Sjöholm, A.G., Uhlén, M., Truedsson, L. J. Immunol. (1996) [Pubmed]
  14. Analysis of the interaction between properdin and factor B, components of the alternative-pathway C3 convertase of complement. Farries, T.C., Lachmann, P.J., Harrison, R.A. Biochem. J. (1988) [Pubmed]
  15. Inhibition of APP trafficking by tau protein does not increase the generation of amyloid-beta peptides. Goldsbury, C., Mocanu, M.M., Thies, E., Kaether, C., Haass, C., Keller, P., Biernat, J., Mandelkow, E., Mandelkow, E.M. Traffic (2006) [Pubmed]
  16. Properdin, a positive regulator of complement activation, is released from secondary granules of stimulated peripheral blood neutrophils. Wirthmueller, U., Dewald, B., Thelen, M., Schäfer, M.K., Stover, C., Whaley, K., North, J., Eggleton, P., Reid, K.B., Schwaeble, W.J. J. Immunol. (1997) [Pubmed]
  17. Depressed synovial fluid levels of properdin and properdin factor B in patients with rheumatoid arthritis. Ruddy, S., Fearon, D.T., Austen, K.F. Arthritis Rheum. (1975) [Pubmed]
  18. Cleavage of the third complement component (C3) and generation of the spasmogenic peptide, C3a, in human serum via the properdin pathway: demonstration of inhibitory as well as enhancing effects of epsilon-amino-caproic acid. Vogt, W., Schmidt, G., Lynen, R., Dieminger, L. J. Immunol. (1975) [Pubmed]
  19. Histidine-rich glycoprotein inhibits the antiangiogenic effect of thrombospondin-1. Simantov, R., Febbraio, M., Crombie, R., Asch, A.S., Nachman, R.L., Silverstein, R.L. J. Clin. Invest. (2001) [Pubmed]
  20. Surface-dependent modulation by H of C5 cleavage by the cell-bound alternative pathway C5 convertase of human complement. Fischer, E., Kazatchkine, M.D. J. Immunol. (1983) [Pubmed]
  21. Modulation of TNF-alpha secretion in peripheral blood mononuclear cells by cocoa flavanols and procyanidins. Mao, T.K., van de Water, J., Keen, C.L., Schmitz, H.H., Gershwin, M.E. Dev. Immunol. (2002) [Pubmed]
  22. Serum amyloid A, properdin, complement 3, and toll-like receptors are expressed locally in human sinonasal tissue. Lane, A.P., Truong-Tran, Q.A., Myers, A., Bickel, C., Schleimer, R.P. American journal of rhinology. (2006) [Pubmed]
  23. Glomerular deposition of mannose-binding lectin (MBL) indicates a novel mechanism of complement activation in IgA nephropathy. Endo, M., Ohi, H., Ohsawa, I., Fujita, T., Matsushita, M., Fujita, T. Nephrol. Dial. Transplant. (1998) [Pubmed]
  24. Development and application of an enzyme-linked immunosorbent assay for the quantitation of alternative complement pathway activation in human serum. Mayes, J.T., Schreiber, R.D., Cooper, N.R. J. Clin. Invest. (1984) [Pubmed]
  25. The role of properdin in the assembly of the alternative pathway C3 convertases of complement. Hourcade, D.E. J. Biol. Chem. (2006) [Pubmed]
  26. Molecular cloning of the cDNA coding for properdin, a positive regulator of the alternative pathway of human complement. Nolan, K.F., Schwaeble, W., Kaluz, S., Dierich, M.P., Reid, K.B. Eur. J. Immunol. (1991) [Pubmed]
 
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