Thomas B. Shows
Roswell Park Cancer Institute
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Neuron | 1993
Mengqing Xiang; Lijuan Zhou; Y.-W. Peng; Roger L. Eddy; Thomas B. Shows; Jeremy Nathans
A search for POU domain transcription factors in human retina cDNA has led to the identification of Brn-3b, a class IV POU domain protein. Immunohistochemical experiments show that chicken, mouse, rabbit, monkey, and human retinas contain Brn-3b exclusively within a subpopulation of ganglion cells. In the adult mouse brain, Brn-3b is found only within cells in the deep layers of the superior colliculus, in the dorsal periaqueductal gray, and in a small cluster of cells in the brain stem near the area postrema. During the immediate postnatal period, cells containing Brn-3b are distributed in a number of regions within the brain stem and cerebellum. These data suggest that Brn-3b plays a role in determining and/or maintaining the identities of a small number of neurons, including a subset of visual system neurons.
Nature | 1985
Cornelis Murre; Richard A. Waldmann; Cynthia C. Morton; Kathleen F. Bongiovanni; Thomas A. Waldmann; Thomas B. Shows; Jonathan G. Seidman
Three gene families that rearrange during the somatic development of T cells have been identified in the murine genome. Two of these gene families (α and β) encode subunits of the antigen-specific T-cell receptor and are also present in the human genome1–5. The third gene family, designated here as the γ-chain gene family, is rearranged in murine cytolytic T cells but not in most helper T cells6–8. Here we present evidence that the human genome also contains γ-chain genes that undergo somatic rearrangement in leukaemia-derived T cells. Murine γ-chain genes appear to be encoded in gene segments that are analogous to the immunoglobulin gene variable, constant and joining segments8. There are two closely related constant-region gene segments in the human genome. One of the constant-region genes is deleted in all three T-cell leukaemias that we have studied. The two constant-region γ-chain genes reside on the short arm of chromosome 7 (7p15); this region is involved in chromosomal rearrangements identified in T cells from individuals with the immunodeficiency syndrome ataxia telangiectasia9–12 and observed only rarely in routine cytogenetic analyses of normal individuals13–16. This region is also a secondary site of β-chain gene hybridization17.
Genomics | 1992
Lu Bao; Norma P. Gerard; Roger L. Eddy; Thomas B. Shows; Craig Gerard
The genes encoding receptors for the chemotactic ligands C5a (C5AR) and FMLP (FPR) were mapped using a panel of somatic cell hybrids to chromosome 19. Because the hybridization pattern on Southern analysis suggested an intron structure or related genes in the case of FPR, genomic clones were characterized. Two structural homologues of the FMLP receptor, clones 81 (FPRH1) and 82 (FPRH2), were identified, which similarly map to chromosome 19. The structural homologues do not recognize the ligand FMLP, but are likely chemotactic receptors.
Advances in human genetics | 1982
Thomas B. Shows; Alan Y. Sakaguchi; Susan L. Naylor
It is estimated that the human haploid genome is composed of 3 × 109 nucleotides and that only 10% of it consists of coding and regulatory sequences.14 If a gene is approximately 104 nucleotides in length, which includes the coding region and the intervening and flanking sequences, this estimate would predict that there are about 3–10 × 104 human genes coding for different protein products. Since gene clustering in humans has become evident (for example, the hemoglobin, immunoglobin, and HLA clusters), these estimated gene products may be grouped in from 3000 to 15,000 clusters.15 Further, based upon genetic and molecular studies of microorganisms, Drosophila, and the mouse, there are perhaps 5 × 104 structural genes estimated in humans,14,106,183 which is in agreement with the number of estimated protein products in the human genome. Mapping the human genome involves partitioning the total number of genes into individual maps representing the 24 different human nuclear chromosomes and linearly ordering them on each chromosome. A similar exercise has mapped the 37 genes encoded in the DNA of the mitochondrial genome.2
Genomics | 1992
Timo Hautala; M.G. Byers; Roger L. Eddy; Thomas B. Shows; Kari I. Kivirikko; Raili Myllylä
Lysyl hydroxylase (EC 1.14.11.4), an alpha 2 dimer, catalyzes the formation of hydroxylysine in collagens by the hydroxylation of lysine residues in peptide linkages. A deficiency in this enzyme activity is known to exist in patients with the type VI variant of the Ehlers-Danlos syndrome, but no amino acid sequence data have been available for the wildtype or mutated human enzyme from any source. We report the isolation and characterization of cDNA clones for lysyl hydroxylase from a human placenta lambda gt11 cDNA library. The cDNA clones cover almost all of the 3.2-kb mRNA, including all the coding sequences. These clones encode a polypeptide of 709 amino acid residues and a signal peptide of 18 amino acids. The human coding sequences are 72% identical to the recently reported chick sequences at the nucleotide level and 76% identical at the amino acid level. The C-terminal region is especially well conserved, a 139-amino-acid region, residues 588-727 (C-terminus), being 94% identical between the two species and a 76-amino-acid region, residues 639-715, 99% identical. These comparisons, together with other recent data, suggest that lysyl hydroxylase may contain functionally significant sequences especially in its C-terminal region. The human lysyl hydroxylase gene (PLOD) was mapped to chromosome 1 by Southern blot analysis of human-mouse somatic cell hybrids, to the 1p34----1pter region by using cell hybrids that contain various translocations of human chromosome 1, and by in situ hybridization to 1p36.2----1p36.3. This gene is thus not physically linked to those for the alpha and beta subunits of prolyl 4-hydroxylase, which are located on chromosomes 10 and 17, respectively.
Biochemical Genetics | 1970
Thomas B. Shows; Verne M. Chapman; Frank H. Ruddle
Malate dehydrogenase and malic enzyme each possess supernatant and mitochondrial molecular forms which are structurally and genetically independent. We describe electrophoretic variants of the mitochondrial enzymes of malate dehydrogenase and malic enzyme in mice. Progeny testing from genetic crosses indicated that the genes which code for mitochondrial malate dehydrogenase and malic enzyme were not inherited maternally but as independent unlinked nuclear autosomal genes. The locus for mitochondrial malic enzyme was located on linkage group I. Linkage analysis with a third mitochondrial enzyme marker, glutamic oxaloacetic transaminase, showed that the nuclear genes which code for the three mitochondrial enzymes were not closely linked to each other. This evidence suggests that clusters of nuclear genes coding for mitochondrial function are unlikely in mice.
Genomics | 1991
Kenneth D. Bloch; Charles C. Hong; Roger L. Eddy; Thomas B. Shows; Thomas Quertermous
Four members of the endothelin family of vasoactive and mitogenic peptides have been identified: human endothelins 1, 2, and 3 (ET1, ET2, and ET3, respectively) and mouse vasoactive intestinal contractor (VIC). To characterize the mRNA encoding ET2, a 192-bp fragment of the ET2 gene, amplified by the polymerase chain reaction from human genomic DNA, was used to screen cell lines and tissues for ET2 gene expression. ET2 mRNA was detected in a cell line (HTB119) derived from a human lung small cell carcinoma, and an ET2 cDNA was cloned from a cDNA library prepared from HTB119 mRNA. DNA prepared from human-mouse somatic hybrid cell lines was used to assign the gene encoding ET2 (EDN2) to the 1p21----1pter region of chromosome 1, demonstrating that EDN2 is not linked to genes encoding ET1 (EDN1; chromosome 6) and ET3 (EDN3; chromosome 20). Southern blot hybridization revealed a single gene in human and rat genomes that hybridized with the ET2 gene fragment, and the rat gene was cloned. The endothelin peptide encoded by the rat gene differed from ET2 at 1 of 21 residues and was identical to mouse VIC. We conclude that VIC is the mouse and rat analogue of the human ET2 gene.
Genomics | 1991
Glenn I. Fishman; Roger L. Eddy; Thomas B. Shows; Lawrence Rosenthal; Leslie A. Leinwand
Connexins are protein subunits that constitute gap junction channels. Two members of this gene family, connexin43 (Cx43) and connexin32 (Cx32), are abundantly expressed in the heart and liver, respectively. Human genomic DNA analysis revealed the presence of two loci for Cx43: an expressed gene and a processed pseudogene. The expressed gene (GJA1) was mapped to human chromosome 6 and the pseudogene (GJA1P) to chromosome 5. To determine whether Cx32 was linked to Cx43, somatic cell hybrids were analyzed by polymerase chain reaction and hybridization, resulting in the assignment of the gene for Cx32 (GJB1) to the X chromosome at Xp11----q22. Comparison of the structures of connexin genes suggests that members of this multigene family arose from a single precursor, but evolved to distinct chromosomal locations.
Journal of Leukocyte Biology | 1996
Carol J. Raport; Vicki L. Schweickart; David Chantry; Roger L. Eddy; Thomas B. Shows; Ronald Godiska; Patrick W. Gray
Chemokines are relatively small peptides with potent chemoattractant and activation activities for leukocytes. Several chemokine receptors have been cloned and characterized and all are members of the G protein‐coupled receptor superfamily. Using degenerate oligonucleotides and polymerase chain reaction, we have identified seven novel receptors with significant homology to chemokine receptors. Two of these sequences are presented here for the first time. We have shown, with gene mapping studies, that receptors with the highest sequence similarity are closely linked on human chromosomes. This close genetic association suggests a functional relationship as well.
Gene | 1995
Carol J. Raport; Vicki L. Schweickart; Roger L. Eddy; Thomas B. Shows; Patrick W. Gray
A polymerase chain reaction (PCR) strategy with degenerate primers was used to identify novel G-protein-coupled receptor-encoding genes from human genomic DNA. One of the isolated clones, termed V28, showed high sequence similarity to the genes encoding human chemokine receptors for monocyte chemoattractant protein 1 (MCP-1) and macrophage inflammatory protein 1 alpha (MIP-1 alpha)/RANTES, and to the rat orphan receptor-encoding gene RBS11. When RNA was analyzed by Northern blot, V28 was found to be most highly expressed in neural and lymphoid tissues. Myeloid cell lines, particularly THP.1 cells, showed especially high expression of V28. We have mapped V28 to human chromosome 3p21-3pter, near the MIP-1 alpha/RANTES receptor-encoding gene.
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University of Texas Health Science Center at San Antonio
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