Human HMOX2 blocking peptide

Studies have reported conflicting results about possible associations between variants in heme oxygenase (HMOX) genes and risk of Parkinson's disease (PD) in Caucasians, and little is known about these associations in Asians. We genotyped the single-nucleotide polymorphisms (SNPs) rs2071746 and rs2071747 in HMOX1 and rs1051308 in HMOX2 in 583 Han Chinese with PD and 627 healthy controls using a customized 2 x 48-Plex SNP Scan (TM) kit. Frequencies of genotypes and minor alleles were similar between patients and controls for rs2071746 and rs2071747, but different for rs1051308(P = 0.004, OR 1.705, 95%CI 1.191-2.442 for genotypes; P = 0.009, OR 1.249, 95%CI 1.037-1.476 for alleles). Our results suggest that rs1051308 is associated with risk of developing PD in Han Chinese, and further studies involving various ethnicities are needed to validate the association. (C) 2017 Published by Elsevier Ireland Ltd.

ATP1B4 genes represent a rare instance of orthologous vertebrate gene co-option that radically changed properties of the encoded BetaM proteins, which function as Na, K-ATPase subunits in lower vertebrates and birds. Eutherian BetaM has lost its ancestral function and became a muscle-specific resident of the inner nuclear membrane. Our earlier work implicated BetaM in regulation of gene expression through direct interaction with the transcriptional co-regulator SKIP. To gain insight into evolution of BetaM interactome we performed expanded screening of eutherian and avian cDNA libraries using yeast-two-hybrid and split-ubiquitin systems. The inventory of identified BetaM interactors includes lamina-associated protein LAP-1, myocyte nuclear envelope protein Syne1, BetaM itself, heme oxidases HMOX1 and HMOX2; transcription factor LZIP/CREB3, ERGIC3, PHF3, reticulocalbin-3, and beta-sarcoglycan. No new interactions were found for chicken BetaM and human Na, K-ATPase beta 1, beta 2 and beta 3 isoforms, indicating the uniqueness of eutherian BetaM interactome. Analysis of truncated forms of BetaM indicates that residues 72-98 adjacent to the membrane in nucleoplasmic domain are important for the interaction with SKIP. These findings demonstrate that evolutionary alterations in structural and functional properties of eutherian BetaM proteins are associated with the increase in its interactome complexity.