Disease relevance of C6

• In the absence of C6, perivascular mononuclear infiltrates of ED1(+) macrophages and CD8(+) T lymphocytes were present 7 days after transplantation, but vascular endothelial cells were quiescent, with minimal von Willebrand factor release and no evidence of alveolar hemorrhage or edema [1].
• Characterization of a membrane-bound metalloendoprotease of rat C6 glioblastoma cells [2].
• In conclusion, we have demonstrated that extrahepatic, but not renal synthesis of, C6 is sufficient to contribute to glomerular injury during anti-Thy1.1 nephritis [3].
• Effect of measles virus antibodies on a measles SSPE virus persistently infected C6 rat glioma cell line [4].
• Although all modulated cell clones were more susceptible to homologous virus infection than control C6 cells, it was not possible to rescue any defective measles virus which may have been maintained in the culture [4].

High impact information on C6

• Microtubule protein preparations from C6 glial cells and their spontaneous polymer formation [5].
• C6 rat glioblastoma cells are able to attach to and to spread on culture dishes which are coated with purified central nervous system myelin, in contrast to normal astrocytes, fibroblasts or neurons which adhere poorly and are unable to spread on this substrate [2].
• The metalloprotease blockers o-phenanthroline and a newly developed oligopeptide could specifically inhibit C6 cell spreading on central nervous system myelin, suggesting a crucial role for a metalloprotease [2].
• Gel filtration chromatography using the Triton X-114-solubilized proteins or the proteins removed by a short trypsin treatment revealed a molecular weight range for the C6 enzyme of 60,000-100,000 [2].
• Purified, salt-washed C6 plasma membranes cleaved the peptide between alanine and phenylalanine, an effect which is strongly inhibited by o-phenanthroline, but not by thiol-blocking agents or aspartic and serine protease inhibitors [2].

Biological context of C6

• No significant apoptosis was detected in either cultures treated with C6-deficient serum or in control cultures [6].
• Complement component C6 is a part of the lytic membrane attack complex formed during complement activation [7].
• Sequence analysis confirmed that the derived amino acid sequence for rat C6 is highly homologous to human and mouse [7].
• Further, adenosine diphosphate induced platelet aggregation were markedly reduced in C6 deficient rats [7].
• In addition, we identified four point mutations in the mouse C6 gene that may result in C6 deficiency observed in the Peru-Coppock mouse strain [7].

Anatomical context of C6

• Lungs transplanted from C6(+) donors to C6(-) recipients had increased alveolar macrophages and capillary injury [1].
• C6 microtubule preparations exhibit few rings at 0 degrees C, have low polymerization yield, and have a low content of accessory proteins [5].
• Assay of cytokine mRNA by RT-PCR in the spinal cords showed no differences in the profile of Th1 or Th2 cytokines between PVG/C and PVG/C6(-) rats [8].
• PVG/C rats also had a greater increase in peripheral blood white blood cell, neutrophil, and basophil counts than was observed in the PVG/C6(-) [8].
• RNA isolated from C6 cells was shown to direct the synthesis of the activity following microinjection into Xenopus oocytes and one-step fractionation of Xenopus extract [9].

Associations of C6 with chemical compounds

• In conclusion, it was demonstrated in vivo that not only C6 but also C2 is synthesized extrahepatically in PVG/c rats [10].
• Skeletal muscle F-actin stimulates the C-6 myosin adenosine triphosphatase 2- to 3-fold in the presence of KCl and Mg2+ [11].
• When assayed in the presence of 0.6 M KCl and 1 mM EDTA the skeletal muscle myocin ATPase demonstrates substrate saturation while the C-6 myosin enzyme activity is stimulated by ATP concentrations above 2.5 mM [11].

Regulatory relationships of C6

• C6 cells expressed less than 0.2% of the proteolipid mRNA that was expressed in primary oligodendrocytes [12].

Other interactions of C6

• Following immunization with myelin basic protein, PVG/C6(-) rats developed significantly milder EAE than PVG/C rats [8].

Analytical, diagnostic and therapeutic context of C6

• C6 production by lung allografts was demonstrated at the mRNA and protein levels [1].
• Polymerase chain reaction with primers corresponding to endopeptidase 24.11 or to the highly conserved motif of the "astacin family" showed that both enzymes were not detectable in the C6 glioblastoma cells [2].

References