Disease relevance of DHX16

• The DBP2 gene was mapped by FISH to the MHC region on human chromosome 6p21.3, a region where many malignant, genetic and autoimmune disease genes are linked [1].

High impact information on DHX16

• A highly conserved protein, Prp8, is a component of the catalytic core [2].
• Transfection experiments demonstrated that the GFP-DBP2 gene product, transiently expressed in HeLa cells, was localized in the nucleus [1].
• We have cloned a new RNA helicase gene, designated DBP2 (DEAH-boxprotein), homologous to the Schizosaccaromyces pombe cdc28(+)/prp8(+) gene involved in pre-mRNA splicing and cell cycle progression [1].
• Lmpkac2 genes are located on chromosome 35 just downstream from the leishmanial prp8 gene [3].
• 100 mg atenolol and 10 and 20 mg bisoprolol reduced HR, SBP, and DBP 2 h postmedication [4].

Biological context of DHX16

• DBP1 and DBP2 both appeared to have one binding site for 25-hydroxyvitamin D3 per molecule of protein, with apparently similar association constants at 4 degrees C of 5--7 x 10(9) M-1 [5].
• Two outstanding publications on the amoeba Naegleria group I intron (Wikmark et al. BMC Evol Biol 2006, 6:39) and the PRP8 inteins in ascomycetes (Butler et al.BMC Evol Biol 2006, 6:42) provide important stepping stones towards integrated studies on how these parasitic elements evolve through time together with, or despite, their hosts [6].

Associations of DHX16 with chemical compounds

• In addition, they seem to be essential in this field the amino acid biosynthesis (cpcA and homoaconitase/lysF), the activation and expression of some genes at 37 degrees C (Hsp1/Asp f12, cgrA), some molecules and genes that maintain cellular viability (smcA, Prp8, anexins), etc [7].

Analytical, diagnostic and therapeutic context of DHX16

• Its m.w., charge microheterogeneity, and amino acid composition correspond closely with reported values for those properties of factor B. A radioimmunoassay was used to estimate the serum concentration of DBP-2 at 266 +/- 83 microgram/ml, which also corresponds with the level of factor B normally present in the serum [8].
• By means of DNA affinity chromatography of the fragments produced by trypsinization, the DNA-binding domain of DBP-2 was localized [8].
• On double immunodiffusion, anti-DBP2 antiserum produced precipitin lines of complete reaction-of-identity against the purified DBP1, the purified DBP2, and rat whole serum [5].
• The isoelectric points of DBP1 and DBP2 were estimated as 4.9 and 5.0, respectively, from the results of isoelectric focusing experiments [5].

References