Disease relevance of Brd8

• Comparison of the tryptic peptides of p80 with those of the p120 gag-fusion protein of Abelson murine leukemia virus demonstrated that p80 and p120 did not share tryptic peptides [1].
• The p80 and p120 immunobands were observed in Novikoff hepatoma and in hypertrophic rat liver, but were not detected in normal liver under the same conditions [2].
• Two tyrosine phosphoproteins in phorbol ester-sensitive EL4 (S-EL4) mouse thymoma cells have been identified as the p120 c-Cbl protooncogene product and the p85 subunit of phosphatidylinositol 3-kinase [3].
• Mycoplasma hyorhinis GDL surface protein antigen p120 defined by monoclonal antibody [4].
• Efficacy of p120 antisense-mediated therapy for pancreatic cancer [5].

High impact information on Brd8

• L12 are Ab-MuLV-transformed cells that express the abl p120 oncogene product but lack the cellularly encoded p53 [6].
• We have attempted to identify a 120-kD tyrosine-phosphorylated protein (p120) that associates with Zap-70 in activated T lymphocytes [7].
• Role of p120 Ras-GAP in directed cell movement [8].
• This sequence is also required for E-cadherin binding of protein p120, a known regulator of cadherin-mediated cell adhesion [9].
• This observation, coupled with the fact that the p120 protein encoded by this virus has been shown to undergo an apparent autophosphorylation to yield phosphotyrosine in vitro, suggests that Abelson virus encodes a protein kinase that phosphorylates tyrosine in transformed cells [10].

Chemical compound and disease context of Brd8

• The pharmacokinetics, tissue distribution, stability, and cellular uptake by LOX ascites tumor of p120 antisense phosphorothioate oligonucleotide, ISIS 3466, were studied in vivo [11].

Biological context of Brd8

• TCR-zeta/CD3 induced activation of T cells augmented the tyrosine phosphorylation of p120/130 in vivo as detected by antibody and GST:fyn-SH2 fusion proteins. p120/130 represents the first identified p59fyn(T):SH2 binding substrate in T cells, and as such is likely to play a key role in the early events of T cell activation [12].
• These GAPs possess a common catalytic domain but contain distinct regulatory elements that may couple different external signals to control of the Ras pathway. p120-Gap, for example, has two N-terminal SH2 domains that directly recognize phosphotyrosine motifs on activated growth factor receptors and cytoplasmic phosphoproteins [13].
• Recently, betaglycan and inhibin binding protein (InhBP/p120, also known as the product of immunoglobulin superfamily gene 1 [IGSF1]) were identified as candidate inhibin coreceptors, shedding light on the molecular basis of how inhibins may affect target cells [14].
• Overexpression of the noncatalytic domains of p120 GAP may modulate Ras signal transduction pathways [15].
• In addition, expression of full-length kinesin reduced the nuclear accumulation of p120 and blocked the branching phenotype associated with p120 overexpression [16].

Anatomical context of Brd8

• Further, based on the results of in vitro kinase assays, p120/130 appears to be preferentially associated with p59fyn(T) in T cells, and not with p56lck [12].
• To better understand the in vivo functions of InhBP/p120, we characterized the InhBP/p120 mRNAs and gene in mice and generated InhBP/p120 mutant mice by gene targeting in embryonic stem cells [14].
• In addition, cFKBP/SMAP-induced smooth muscle differentiation was inhibited by FK506 [17].
• Moreover, overexpression of cFKBP/SMAP in lung and gizzard mesenchymal cells induced smooth muscle differentiation [17].
• This product showed identical mobility to p120 induced in intact activated macrophages radiolabeled with [35S]methionine [18].

Associations of Brd8 with chemical compounds

• The phosphotyrosine is found at two sites in the protein. p120 therefore may be a protein kinase that undergoes autophosphorylation in vivo [10].
• Metabolically labeled p120 was found to include methionine-containing tryptic peptides of p73 plus additional peptides consistent with its larger size [19].
• Accumulation of translatable p120 mRNA was blocked by treatment with cycloheximide, indicating that active protein synthesis was required during the induction period [18].
• Perturbing the p120-microtubule interaction with nocodazole or taxol markedly affected both the tubulin interaction and the balance between cytoplasmic and nuclear p120 [16].
• Macrophages obtained from mice chronically infected with bacillus Calmette-Guerin constitutively expressed both p120 and cytolytic activity [20].

Analytical, diagnostic and therapeutic context of Brd8

• Immunoblotting with antibodies to p120 and the ras GTPase activating protein, GAP, suggests that p120 and GAP are unrelated [21].
• Protein blots of mycoplasmas derived from BW5147 cell cultures were stained with antibody to p120, revealing a component identical to that observed with broth-grown organisms [4].
• By using indirect immunofluorescence and immunoferritin techniques, mycoplasmas colonizing the surface of chronically infected BW5147 murine T-lymphoblastoid cells were selectively stained with antibody to p120, indicating the localization of the corresponding epitope at the mycoplasma surface [4].
• Among them, two proteins, p43 and p120, were identified as mitogen-activated protein kinase (MAP-kinase) and focal adhesion kinase (FAK), respectively, by immunoprecipitation and immunoblot analysis [22].
• Western blotting analysis indicated expression of alpha- and beta-catenins and p120-catenin (or p120 cas) in BMMC, whereas PMC showed less intense expression of alpha- and beta-catenins with high levels of p120 expression [23].

References