Disease relevance of CHN1

• Strikingly, microinjection of the full-length n-chimaerin into fibroblasts and neuroblastoma cells induces the simultaneous formation of lamellipodia and filopodia [1].
• In HIV-1, 5'-leader RNA/NC interactions appear to control these viral processes [2].
• We find that n-chimaerin expressed in the baculovirus system bound [3H]phorbol 12,13-dibutyrate with high affinity (0.17 +/- 0.01 nM) [3].
• Deletion analysis of the carboxy-terminal chimera revealed two small regions within the HIV NC protein that were sufficient for endowing mutant Bg-Bs with these properties [4].
• The inner core is formed by an outer shell of capsid protein molecules (CA protein) surrounding the dimeric RNA genome in close association with about 2000 molecules of nucleocapsid protein (NC protein) and molecules of reverse transcriptase (RT) and integrase (IN) [5].

High impact information on CHN1

• We have previously shown that there is a diversity of GAPs that recognize this subfamily, including n-chimaerin, which is enriched in the hippocampus; we also detected proteins that bind these p21 proteins and seem to inhibit GTP hydrolysis [6].
• Taken together, these results suggest that n-chimaerin acts synergistically with Rac1 and Cdc42Hs to induce actin-based morphological changes and that this action involves Rac1 and Cdc42Hs binding but not GAP activity [1].
• The effects of n-chimaerin on formation of lamellipodia and filopodia were inhibited by dominant negative Rac1(T17N) and Cdc42Hs(T17N), respectively. n-Chimaerin's effects were also inhibited by coinjection with Rho GDP dissociation inhibitor or by treatment with phorbol ester [1].
• The single human n-chimerin gene was mapped to chromosome 2q31-q32.1, colocalizing with the CRE-BP1 transcription factor gene (2q32) [7].
• n-Chimerin (alpha 1-chimerin) is a brain GTPase-activating protein (GAP) for the ras-related p21rac [7].

Chemical compound and disease context of CHN1

• The HIV-1 NC binds to the HIV-1 LTR and results in a mobility shift in polyacrylamide gel electrophoresis [8].

Biological context of CHN1

• Alpha 2-chimerin, an SH2-containing GTPase-activating protein for the ras-related protein p21rac derived by alternate splicing of the human n-chimerin gene, is selectively expressed in brain regions and testes [7].
• A novel human brain complementary DNA sequence encodes n-chimaerin, a 34,000 Mr protein [9].
• Retroviruses, including HIV-1 encode a major nucleic acid binding protein (NC protein) found within the virus where 2000 NC protein molecules coat the dimeric genome [2].
• While both of the two Zn finger motifs found within NC7 were essential for efficient elongation, NC protein that contained a point mutation in the first Zn finger or that was devoid of both Zn fingers yielded primer-template complexes that could still be initiated in 1-base-extension assays [10].
• Therefore, compensatory mutations within the p2 and NC proteins, distal from deletions within the DIS region of the HIV genome, can restore HIV replication, viral gene expression, and viral RNA packaging to control levels [11].

Anatomical context of CHN1

• RNA transcription directed by the adenovirus major late promoter, however, is not significantly affected by NC in the cell-free system [8].
• Moreover, transfection of HIV-1 provirus containing mutations in NC zinc-finger domains dramatically decreases the enhancement activity in human T cells, in which HIV-1 LTR is stably integrated into the cellular genome [8].
• NC injection to the animals with necrosis was followed by Ca2+ release from all the studied organelles [12].
• Neurohormone C (NC) is a glycopeptide isolated from bovine hypothalamus, which inhibits Ca-calmodulin (CaM)-dependent cAMP and cGMP phosphodiesterase (PDE) and is a regulator of Ca in the cell [12].

Associations of CHN1 with chemical compounds

• The sequence identity of n-chimaerin with PKC includes the cysteine-rich motif CX2CX13CX2CX7CX7C, and amino acids upstream of the first cysteine residue, but not the kinase domain [13].
• A novel functional target for tumor-promoting phorbol esters and lysophosphatidic acid. The p21rac-GTPase activating protein n-chimaerin [14].
• We now show that the rac-GAP activity of n-chimaerin is stimulated by phosphatidylserine (PS) and phosphatidic acid (PA) and that phorbol esters can synergize with PS and PA [14].
• In response to the V82A drug-resistant protease mutation, the P2 alanine of NC-p1 mutates to valine (AP2V) [15].
• All of the complexes have been characterized by (1)H NMR spectroscopy, elemental analysis (CHN), and X-ray crystallography [16].

Other interactions of CHN1

• The similarity of two separate regions of n-chimaerin to domains of protein kinase C and BCR has intriguing implications with respect to its evolutionary origins, its function in the brain and potential phorbol-ester-binding properties [9].
• Eight patients (CHN1) with a S beta 2m < 5 mg/liter had various abnormalities of their urinary protein pattern [17].

Analytical, diagnostic and therapeutic context of CHN1

• We present here the sequence analysis of m1.7 and its putative product, rnprot1.7, and show that rnprot1.7 is similar to the product of the human n-chimaerin gene, which is expressed in brain and testes [18].
• Thus, RT-PCR detection of EWS-CHN or TAF2N-CHN fusion gene using archival paraffin-embedded tissue is a feasible and useful ancillary technique for the diagnosis of EMCS [19].
• Four different methods were evaluated including elemental analysis (CHN), quantitative amino acid analysis (AAA), high-performance liquid chromatography (HPLC), and Kjeldahl [20].
• Isomers of astaxanthin produced by Thraustochytrium sp. CHN-1 are identified as (3S,3S')-trans-astaxanthin, (3R,3R')-trans-astaxanthin and (3S,3S')-cis-astaxanthin by chirality column HPLC, and 1H and 13C NMR [21].
• The Child Health Network for the Greater Toronto Area (CHN), a network of 20 hospitals and 9 community care access centres, assessed one component of its early progress in building a regionalized system of perinatal care [22].

References