Anti-EHD2 (aa 529-542) polyclonal antibody

BACKGROUND. Deletions of 19q have been associated with gliomas, especially oligodendrogliomas. In addition, cases with oligodendrogliomas with the 19q deletion have been observed to have a better survival compared with cases without the 19q deletion. The authors have previously described a 150-kilobase minimal deletion region in gliomas that maps to 19q13.33 and contains 3 novel candidate genes (GLTSCR1, EHD2, and GLTSCR2). METHODS. The authors performed an association study using 141 cases with gliomas (61 cases with astrocytomas, 40 cases with oligodendrogliomas, 40 cases with mixed oligoastrocytomas) and 108 general controls. They evaluated 7 single nucleotide polymorphisms (SNPs) in 6 genes within and nearby the minimal 19q deletion region (ERCC2, RA1, ASE-1, ERCC1, GLTSCR1, and LIG1). RESULTS. The prevalence of a germline GLTSCRI-exon-1 T allele (SNP rs1035938) was 40% in cases with oligodendrogliomas compared with 27% in controls (P = 0.029), and the prevalence of an ERCC2-exon-22 T allele (SNP rs1052555) was 35% in cases with oligodendrogliomas compared with 18% in controls (P = 0.043). One high-risk and 1 low-risk haplotype were associated with oligodendroglioma development (P = 0.003 and 0.026, respectively). Cases with oligodendrogliomas with the 19q deletion had a significantly higher frequency of the GLTSCRl-exon-1 T allele compared with cases without the 19q deletion (P = 0.01). It was noteworthy that cases with gliomas who were homozygous for the GLTSCRI-exon-1 T allele had a significantly better survival: 77% and 68% survival at 2 and 5 years compared with 56% and 34% for other genotypes (P = 0.02, log-rank test). Multivariable to analysis identified grade, age, and the GLTSCRI-exon-1 and ERCC2-exon-22 genotypes as independent predictors for survival. CONCLUSIONS. These results suggested that alterations in GLTSCR1 (or a closely linked gene) were associated with the development and progression of oligoden droglioma. (c) 2005 American Cancer Society.

The change of myoblast shape from fibroblast-like to elongate, which is essential for adhesion and fusion, results from re- modeling of actin cytoskeleton. The process involves an array of factors, for example the action of latrunculin B or cytochalasin D, which interfere with F-actin remodeling. It is also suggested that the conservative gene Napl regulates cytoskeleton re-modeling during mammalian myoblast fusion. Non-muscular myosin 2A and its interaction with submembrane F-actin is responsible for the bipolar shape of myoblasts. Treatment with alpha-cytodextrin (a-CD) removes lipids from the cell membrane and leads to myotube growth. Transciption factor NFATC2 (Nuclear Factor of Activivated T Cells 2) is responsible for regulation of myotube growth. Its activators are IL-4 and prostaglandin (PGF2a). Transcription factor Mitf (microphthalmia-associated transcription factor) is also required for the myotube growth. Receptors of trans-membrane protein: N- and M-cadherins, combined with receptors of IgSF (immunoglobulin superfamily), Cdo and neogenins, initiate signal pathways which lead from the cell surface to the nucleus. As a result, they trigger expression of muscle-specific genes and myoblast-myotube fusion. Myoferlin and the associated EHD2 are included in the endocytosis of membrane proteins which then undergo recycling. A new concept assumes that cytoplasmic vesicles, which are present in fusing myoblasts, represent particular symptom of endocytosis. Weakening of the endocytic vesicle recycling process is associated with defect myoblast fusion and myoblast-myotube fusion. Integrin subunit alpha 3 has an effect on myoblast adhesion and fusion, while blocking the function of gene Itg beta 1, which codes for integrin subunit beta 1, weakens the fusion. Transmebrane protein ADAM12 is required for adhesion and myon blast fusion. PRMT (protein arginine methyltransferase) shows the highest activity during myoblast fusion. Kalponin 3 (CNN3) regulates the process of myoblast fusion and expression of muscle-specific genes. Kirrel gene in Brachydanio rerio, a homologue of Kirre gene in Drosophila Melanogaster, is responsible for myoblast fusion. The protein encoded by the gene myoblast city (mbc) in Drosophila is Dockl 80. Protein 180 has a homologue in vertebrates. In Brachydanio inhibition of two subgroups of Dock180, Dock1 and Dock5 disturb the fusion of myoblasts. In mouse Dockl-/- mutants muscle fibers are thinner and shorter, compared to Dockl+/+. Proteins Raci and Cdc42 regulate actin dynamics in Drosophila. In mouse mutants deficit of Racl and Cdc42 decreases the dynamics of actin and vinculin fibers, and as result weaken myoblast fusion.