PubMed · 5547065
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B Miles, T Pirkle, E K Lang. 1971. Double contrast study utilizing intraperitoneal gas.. https://pubmed.ncbi.nlm.nih.gov/5547065/
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The G12 subfamily of heterotrimeric G proteins, comprised of the alpha-subunits Galpha12 and Galpha13, has been implicated as a signaling component in cellular processes ranging from cytoskeletal changes to cell growth and oncogenesis. In an attempt to elucidate specific roles of this subfamily in cell regulation, we sought to identify molecular targets of Galpha12. Here we show a specific interaction between the G12 subfamily and the cytoplasmic tails of several members of the cadherin family of cell-surface adhesion proteins. Galpha12 or Galpha13 binding causes dissociation of the transcriptional activator beta-catenin from cadherins. Furthermore, in cells lacking the adenomatous polyposis coli protein required for beta-catenin degradation, expression of mutationally activated Galpha12 or Galpha13 causes an increase in beta-catenin-mediated transcriptional activation. These findings provide a potential molecular mechanism for the previously reported cellular transforming ability of the G12 subfamily and reveal a link between heterotrimeric G proteins and cellular processes controlling growth and differentiation.
OBJECTIVE: To report the development of metastatic prostate cancer in a heart transplant recipient without a primary focus in the recipient prostate gland; to present genetic evidence suggesting transplantation of the malignancy from the donor. DESIGN: Histological analysis of donor prostate and recipient prostate and rib. Molecular genetic analysis of prostate and kidney tissue from the donor and peripheral blood leukocytes and rib tissue from the transplant recipient. SETTING: University of Pennsylvania Medical Center. RESULTS: Multiple biopsies of recipient prostate were negative for malignancy but recipient rib contained prostatic adenocarcinoma with osteoblastic bone response. Molecular genetic analysis of recipient rib specimen, which contained both histologically normal and neoplastic cells, was shown to contain a combination of alleles from the donor and recipient at 4 loci. CONCLUSION: Although this is a single case report of an uncommon event, genotyping of polymorphic dinucleotide repeat elements from 4 different chromosomal regions provides strong evidence that the tumor cells arose from donor tissue and were transplanted along with the cardiac allograft.
Repair of oxidative damage to DNA bases is essential to prevent mutations and cell death. Endonuclease III is the major DNA glycosylase activity in Escherichia coli that catalyzes the excision of pyrimidines damaged by ring opening or ring saturation, and it also possesses an associated lyase activity that incises the DNA backbone adjacent to apurinic/apyrimidinic sites. During analysis of the area adjacent to the human tuberous sclerosis gene (TSC2) in chromosome region 16p13.3, we identified a gene, OCTS3, that encodes a 1-kb transcript. Analysis of OCTS3 cDNA clones revealed an open reading frame encoding a predicted protein of 34.3 kDa that shares extensive sequence similarity with E. coli endonuclease III and a related enzyme from Schizosaccharomyces pombe, including a conserved active site region and an iron/sulfur domain. The product of the OCTS3 gene was therefore designated hNTH1 (human endonuclease III homolog 1). The hNTH1 protein was overexpressed in E. coli and purified to apparent homogeneity. The recombinant protein had spectral properties indicative of the presence of an iron/sulfur cluster, and exhibited DNA glycosylase activity on double-stranded polydeoxyribonucleotides containing urea and thymine glycol residues, as well as an apurinic/apyrimidinic lyase activity. Our data indicate that hNTH1 is a structural and functional homolog of E. coli endonuclease III, and that this class of enzymes, for repair of oxidatively damaged pyrimidines in DNA, is highly conserved in evolution from microorganisms to human cells.