Disease relevance of ARID1B

• Immunoprecipitation of membrane protein isolated from LM cells and TE-85 cells with the MoAbs OSA1 and OSA2 conjugated with Staphylococcus aureus yielded a molecule with molecular weight of approximately 92,000 [1].
• RESULTS: Medieval uroscopists recognized proteinuria, and in 1827 Richard Bright first linked proteinuria to both dropsy (edema) and the autopsy finding of chronically diseased, scarred kidneys [2].
• Whilst these changing concepts were debated, it was noted in parallel that diabetics might show coagulable urine containing albumin, even before Bright and others had established this as a sign of kidney disease [3].
• The description of end-stage kidney disease by Richard Bright (1789-1858) in 1827 launched studies of the vasculature, which were to lead to the recognition of hypertension and subsequent identification of the lesions of arteriosclerosis (1833) and atherosclerosis (1904) as diseases of the vasculature [4].

Psychiatry related information on ARID1B

• BACKGROUND: We developed a standardised case-based educational exercise on the topic of childhood learning disorders, and a multimedia computerised adaptation of this exercise, as part of a national curriculum project based on the Bright Futures guidelines [5].

High impact information on ARID1B

• ARID1 is an E3 Ubiquitin Ligase that taget Histone H2B (Ref) [6]
• Five hybrid clones were established and designated as OSA1, OSA2, OSA3, OSA4, and OSA5 [1].
• The glucocorticoid receptor-mediated activation is not observed with the C-terminal domain or with the hOsa2 polypeptide lacking the ARID DNA binding domain [7].
• Mass spectrometric analysis, and immunoblotting with antibodies specific to hOsa1 or hOsa2 demonstrate the presence of both proteins in SWI/SNF-A but not in the related polybromo-BRG1-associated factors complex purified from HeLa cells [7].
• These results suggest that hOsa1 and hOsa2 participate in promoting transcriptional activation by the steroid hormone receptors [7].
• In cultured mammalian cells, hOsa1 and hOsa2 stimulate transcription by the glucocorticoid, estrogen, and androgen receptors [7].

Biological context of ARID1B

• ARID1B is an independent gene product with an open reading frame that is more than 60% identical with p270 [8].
• Analysis of the panels of cell lines indicates that ARID1B, similar to p270, has a broad tissue distribution [8].
• We report accurate Brownian simulation results for the kinetics of the pseudo-first-order diffusion-influenced excited-state reversible transfer reaction A(*) + Bright harpoon over left harpoonC(*) + D with two different lifetimes using two different propagation algorithms [9].

Anatomical context of ARID1B

• Identification, Structural, and Functional Characterization of a New Early Gene (6A3-5, 7 kb): Implication in the Proliferation and Differentiation of Smooth Muscle Cells [10].

Associations of ARID1B with chemical compounds

• This difference could all be accounted for by increased accident rate in OSA patients with the highest AHI (OSA3) (MVA/yr: 0.11+/-0.15, 0.08+/-0.12, 0.06+/-0.14 for OSA groups 3,2,1 respectively) as there was no differences among Control, OSA1 and OSA2 accident rates [11].
• Solvent-Dependent Photophysics of 1-Cyclohexyluracil: Ultrafast Branching in the Initial Bright State Leads Nonradiatively to the Electronic Ground State and a Long-Lived (1)npi State [12].

Other interactions of ARID1B

• The ratio of p270/ARID1B in typical cells is approx. 3.5:1, and BRG1 is distributed proportionally between the two ARID subunits [8].
• Here we report the isolation of two related but distinct cDNA clones, hOsa1 and hOsa2, that encode the largest subunits of human SWI/SNF. hOsa1 is identical to previously reported BAF250, and hOsa2 shares a high degree of sequence similarity with hOsa1 [7].
• The SYT protein has a unique QPGY domain, which is also present in the largest subunits, p250 and the newly identified homolog p250R, of the corresponding SNF/SWI complexes [13].
• One was 1,002 kb in size and contained PACRG and QKI, while the second was 199 kb and harbours a single gene, ARID1B [14].

References