Disease relevance of Commd3

• Antiserum raised against the electrophoretically purified endo B protein immunoprecipitated endo B from [35S]methionine-labeled cell lysates of three parietal endodermal cell lines, a presumptive visceral endodermal cell line, and a mouse hepatoma line [1].
• Mycobacterium tuberculosis (strain H37Rv) and bacillus Calmette-Guérin (BCG) vaccine inhibit phagosome maturation in macrophages and their effect on processing, and presentation of a secreted Ag85 complex B protein, Ag85B, by mouse macrophages was analyzed [2].
• sigma B is a secondary sigma factor that controls the general stress response in Bacillus subtilis. sigma B-dependent genes are activated when sigma B is released from an inhibitory complex with an anti-sigma B protein (RsbW) and becomes free to associate with RNA polymerase [3].
• Here we have examined the effects of ethanol on hepatitis B protein X (HBX)- or hepatitis C core protein (HCV core protein)-mediated activation of NF-kappaB, a critical signal in hepatic injury, regeneration, and tumor transformation [4].

High impact information on Commd3

• Overexpression of p65 increases endogenous I kappa B protein in both carcinoma and lymphoid cells by two mechanisms: protein stabilization and increased transcription of I kappa B mRNA [5].
• The proto-oncogene bcl-3 encodes an I kappa B protein [6].
• To assess whether Spi-B is required for pDC development we used an RNA interference knock down approach to specifically silence Spi-B protein synthesis in CD34(+) precursor cells [7].
• Most importantly, differentiating mouse erythroblasts exhibited a stage-specific activation of the E16 splicing switch in concert with a dramatic and specific down-regulation of hnRNP A/B protein expression [8].
• In vitro translated Spi-B protein can bind to PU.1 binding sites in myeloid promoters and transactivate these promoters in nonmyeloid cells [9].

Biological context of Commd3

• Apo B-38.9 was the sole apo B protein in homozygote (apob(38.9/38.9)) plasma [10].
• On the other hand, cAMP derivatives are not effective in inducing the fos and jun genes, except for fra-2 mRNA, JUN D protein, and to some extent JUN B protein [11].
• A difference in jun B protein overall phosphorylation was observed in the two cell lines [12].
• Using an anti-sigma B monoclonal antibody to monitor the levels of sigma B protein, PSPAC to control the expression of the sigB operon, and a ctc-lacZ reporter system to monitor sigma B activity, we observed that the rsbV and rsbW products control sigma B activity at the ctc promoter independently of their effects on sigma B levels [13].
• Slow component B protein kinetics in optic nerve and tract windows [14].

Anatomical context of Commd3

• These results indicate that the monocyte/B-cell-specific transcription factor PU.1 and the Mono A and Mono B protein complexes act in concert to regulate monocyte-specific transcription of the CSF-1 receptor [15].
• The cytoskeletal B protein isolated from extraembryonic endodermal cells (Endo B) is a 50-kDa subunit of intermediate filaments that is expressed in trophoblast and extraembryonic endoderm of early mouse embryos [16].
• Binding of NF-kappa B protein was demonstrated by oligonucleotide competition, induction of binding upon 70Z/3 pre-B- to B-cell differentiation, response to GTP in the binding reaction, reduction of binding upon addition of I kappa B protein and uv cross-linking analysis [17].
• Structural analysis of chicken oviduct progesterone receptor using monoclonal antibodies to the subunit B protein [18].
• Supershift and Western blotting analyses revealed relatively high constitutive expression of Fos-B protein in neocortex and hippocampus, but not in medulla-pons and spinal cord [19].

Associations of Commd3 with chemical compounds

• Kinetic studies, using the Sm antiserum to immunoprecipitate the methionine-labeled snRNP proteins, suggest that the B protein has a half-life of 90 to 120 min in the cytoplasm [20].
• These results suggest that expression of Fos-B protein may be required for modulation of nuclear gene transcription by both SPD and SPN through stimulation DNA-binding activity of AP1 complex in murine central structures [19].
• The identity of the former protein was confirmed by its reaction with goat anti-mouse serum albumin in an immunodiffusion procedure, and the latter protein by its B protein activity in the lactose synthetase assay [21].
• Our results suggest that minimally-oxidized LDL is not recognized by the macrophage scavenger receptors unless the lipid hydroperoxide groups are decomposed to products able to derivatize the apo B protein [22].

Other interactions of Commd3

• Our experiments suggest that decreased jun B protein levels may be a mechanism that results in elevated AP-1 activity in malignant 10Gy5 cells [12].

Analytical, diagnostic and therapeutic context of Commd3

• In keeping with this, Jun-B protein is not detectable in cytosol or nuclear extracts from resting B lymphocytes, as determined by immunoblotting with Jun-B antisera [23].

References