Disease relevance of OPN1LW

• Adenovirus E1A proteins prepare the host cell for viral replication, stimulating cell cycling and viral transcription through interactions with critical cellular regulatory proteins such as RB and CBP [1].
• APF/CBP, an anionic polypeptide in bile and gallstones that may regulate calcium salt and cholesterol precipitation from bile [2].
• For the CBP pancreatic cancer line, CHS treatment increased tumor immunogenicity significantly, as demonstrated by diminished tumor growth rate and by increased duration of survival after challenge [3].
• Tax stimulates HTLV-I transcription through high affinity binding to the KIX domain of CBP, a pleiotropic coactivator [4].
• Mutations in transcription factors have recently been identified in a number of genetic diseases (for example, Denys-Drash syndrome, WT1 [19]; pituitary dwarfism, PIT1 [16]; Rubinstein-Taybi syndrome, CBP [20] [5].

High impact information on OPN1LW

• Finally, our studies implicate recruitment by KLF2 of the transcriptional coactivator cyclic AMP response element-binding protein (CBP/p300) as a unifying mechanism for these various effects [6].
• We now demonstrate that the p300 and CBP acetyltransferases play a major role in the in vivo acetylation of RelA, principally targeting lysines 218, 221 and 310 for modification [7].
• In search of the underlying mechanism, we have found that CD44ICD potentiates transactivation mediated by the transcriptional coactivator CBP/p300 [8].
• We recently identified and enriched a protein (CBP) from HeLa cells with binding specificity for cruciform-containing DNA [9].
• We have now studied the interaction of CBP with stable cruciform DNA molecules containing the 27 bp palindrome of SV40 on one strand and an unrelated 26 bp palindrome on the other strand by hydroxyl radical footprinting [9].

Chemical compound and disease context of OPN1LW

• We propose that the NADH glycerol phosphate shuttle participates in generating a pool of ATP that serves either as a co-factor or a modulator of the kinases involved in the phosphorylation of p300/CBP during hypoxia [10].
• Furthermore, inhibition of CBP and p300 function in neurodegenerative diseases caused by polyglutamine expansion may be an underlying cause for cytotoxicity [11].
• We examined the effect of an alpha-adrenergic blocker (doxazosin) on BP measurements taken by HBP after awakening and during clinic visits (CBP) in 50 patients with type-2 diabetes and morning hypertension [12].
• Two transplantable solid tumors (CBP and PDP) and two continuous cultured cell lines (CBP-TC and PDP-TC) were established from nitrosamine-induced pancreatic ductal adenocarcinomas in inbred Syrian hamsters [13].
• Eighty-nine patients with multiple myeloma resistant to melphalan were randomized to receive cyclophosphamide plus prednisone (CP) (47 patients) or cyclophosphamide plus BCNU plus prednisone (CBP) (42 patients) [14].

Biological context of OPN1LW

• This places L1CAM between this marker and the color vision genes (RCP, GCP), a region very dense in CpG islands, expected to contain a large fraction of the disease genes assigned to the Xq28 region [15].
• The current study presents nucleotide sequence analyses and tests of neutrality for a 5.5-kb region of the X-linked long-wave "red" opsin gene (OPN1LW) in 236 individuals from ethnically diverse human populations [16].
• Our analysis of the recombination landscape across OPN1LW reveals an unusual haplotype structure associated with amino acid replacement variation in exon 3 that is consistent with gene conversion [16].
• BglII RFLP in DXS 498 between the pigment gene repeat unit, RCP and GCP [17].
• The sequence homology reflects, at least partly, the conservation of common binding sites for the RB and CBP/p300 proteins, which are preserved in the same relative order along E2F1 and E1A [18].

Anatomical context of OPN1LW

• CBP, with an apparent molecular weight of 245,000, co-migrated with the upper band of human and dogfish erythrocyte spectrin [19].
• The competition between Tax and cellular transcription factors for CBP represents a novel pathway for HTLV-I dependent deregulation of gene expression, and may have significant implications for cellular homeostasis and transformation in the HTLV-I infected T-cell [4].
• E1A represses apolipoprotein AI enhancer activity in liver cells through a pRb- and CBP-independent pathway [20].
• Chimerism in granulocytes and PBMC subsets did show great intra-individual differences in the subsets and these data correlated well with RCP and CYT data with the exception of the NK cells [21].
• Using red cell phenotyping (RCP) and/or cytogenetics (CYT) we identified 19 patients with persisting mixed chimerism (MC) among 231 patients transplanted with partially T cell-depleted stem cell grafts from HLA-identical siblings [21].

Associations of OPN1LW with chemical compounds

• Transplantable pancreatic carcinoma lines CBP and LSP-1 grown in inbred hamsters were tested for immunogenicity after CHS treatment [3].
• In order to investigate the role of CBP in the regulation of endogenous genes, we isolated stable transformants that express Gal4-CBP(1-451) in response to added doxycycline [22].
• CBP is required for sterol-regulated and sterol regulatory element-binding protein-regulated transcription [22].
• Physical association between the histone acetyl transferase CBP and a histone methyl transferase [23].
• TBK and RCP were measured before treatment to establish baseline values, after which all subjects received 6 mg piretanide a day for 14 days [24].

Other interactions of OPN1LW

• The red (RCP) and green (GCP) color pigment genes are located in Xq28, a chromosomal region implicated in many genetic disorders [17].

Analytical, diagnostic and therapeutic context of OPN1LW

• Immunizations were performed using both syngeneic and allogeneic cells and supernatants for both the CBP and LSP-1 systems for specificity experiments [3].
• Mobility shift assays performed with the HLA-A2 ISRE revealed the presence of a constitutive binding protein (ISRE/CBP) [25].
• Here, the in vivo association of CBP/14-3-3 with mammalian origins of DNA replication was analyzed by studying its association with the monkey replication origins ors8 and ors12, as assayed by a chromatin immunoprecipitation assay and quantitative PCR analysis [26].
• Tertiary structure prediction of the KIX domain of CBP using Monte Carlo simulations driven by restraints derived from multiple sequence alignments [27].
• CONCLUSION: In this study, CBP/Cat.II patients had significantly lower flowmetry parameters compared to matched age normals [28].

References