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KCP  -  kielin/chordin-like protein

Homo sapiens

Synonyms: CRIM-2, CRIM2, Cysteine-rich BMP regulator 2, Cysteine-rich motor neuron 2 protein, FLJ33365, ...
 
 
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Disease relevance of CRIM2

  • KCP would enhance virus pathogenesis through evading complement attack, opsonization, and anaphylaxis but may also aid in targeting KSHV to one of its host reservoirs since C3d is a ligand for complement receptor 2 on B-cells [1].
  • KCP additionally enhances virion binding to permissive cells through a heparin/heparan sulfate-binding site located at the N-terminus of the protein [2].
  • This result confirms previous reports that recombinant KCP is twice as efficient in inhibiting the classic pathway-mediated lysis of erythrocytes than is the vaccinia virus complement control protein, which also contains four sushi domains [3].
 

High impact information on CRIM2

  • The fourth open reading frame of the KSHV genome encodes a protein (KSHV complement control protein (KCP, previously termed ORF4)) predicted to have complement-regulating activity [1].
  • Dentin was conditioned either with 37% H3PO4 for 20 seconds, or an air-abrasion unit (KCP 1000, ADT) was used with 120 and 160 psi pressure and two different particle sizes, 50 and 27 microns [4].
  • The conventional Ortholux curing light (OCL) and the Plasma Arc Curing (PAC) light attached to the KCP air abrasion unit of American Dental Technologies were utilized to polymerize sealants and resin restorations on extracted third molars and premolars [5].
  • In group 3, 24 teeth were prepared by high-speed (160 PSI) microabrasion using 50 mu alpha alumina particles in a KCP 2000 machine [6].
 

Analytical, diagnostic and therapeutic context of CRIM2

  • The equilibrium affinity constant (KD) of KCP for C3b and C4b was determined by surface plasmon resonance analysis to range between 0.47-10 microM and 0.025-6.1 microM, respectively, depending on NaCl concentration and cation presence [1].
  • The enamel surface was treated as follows for each group: (1) group 1 (control group); (2) group 2 (acid etch group); (3) group 3 (KCP [Kinetic Cavity Preparation System] group); and (4) group 4 (KCP and acid etch group) [7].

References

  1. Functional activity of the complement regulator encoded by Kaposi's sarcoma-associated herpesvirus. Spiller, O.B., Blackbourn, D.J., Mark, L., Proctor, D.G., Blom, A.M. J. Biol. Chem. (2003) [Pubmed]
  2. Kaposi's sarcoma-associated herpes virus complement control protein: KCP--complement inhibition and more. Mark, L., Spiller, O.B., Villoutreix, B.O., Blom, A.M. Mol. Immunol. (2007) [Pubmed]
  3. Cloning and Expression of a Functionally Active Truncated N-Glycosylated KSHV ORF4/KCP/Kaposica in the Methylotrophic Yeast Pichia pastoris. Gomes Pereira, N.A., Juliano, M.A., Carmona, A.K., Sturrock, E.D., Kotwal, G.J. Ann. N. Y. Acad. Sci. (2005) [Pubmed]
  4. Bond strength of composite to dentin treated by air abrasion. Manhart, J., Mehl, A., Schroeter, R., Obster, B., Hickel, R. Operative dentistry. (1999) [Pubmed]
  5. An in vitro study of microleakage of occlusal composite restorations polymerized by a conventional curing light and a PAC curing light. Stritikus, J., Owens, B. The Journal of clinical pediatric dentistry. (2000) [Pubmed]
  6. Microleakage of sealants after conventional, bur, and air-abrasion preparation of pits and fissures. Hatibovic-Kofman, S., Wright, G.Z., Braverman, I. Pediatric dentistry. (1998) [Pubmed]
  7. Microleakage and bond strength of sealant to primary enamel comparing air abrasion and acid etch techniques. Knobloch, L.A., Meyer, T., Kerby, R.E., Johnston, W. Pediatric dentistry. (2005) [Pubmed]
 
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