Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.26.9 (ribonuclease)
 6,589 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Using the cDNA coding for the human interferon alpha/beta receptor (IFNAR), the IFNAR gene has been physically mapped relative to the other loci of the chromosome 21q22.1 region. 32,906 base pairs covering the IFNAR gene have been cloned and sequenced. Primer extension and solution hybridization-ribonuclease protection have been used to determine that the transcription of the gene is initiated in a broad region of 20 base pairs. Some aspects of the polymorphism of the gene, including noncoding sequences, have been analyzed; some are allelic differences in the coding sequence that induce amino acid variations in the resulting protein. The exon structure of the IFNAR gene and of that of the available genes for the receptors of the cytokine/growth hormone/prolactin/interferon receptor family have been compared with the predictions for the secondary structure of those receptors. From this analysis, we postulate a common origin and propose an hypothesis for the divergence from the immunoglobulin superfamily.
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PMID:The structure of the human interferon alpha/beta receptor gene. 137 Aug 33

The gene encoding the human pregnancy-specific glycoprotein (PSG) belongs to a gene subfamily, comprised of the carcinoembryonic antigen (CEA) and PSG subgroups, within the immunoglobulin superfamily. To study the functional roles of PSG during development in an animal model, we isolated and characterized a near full-length cDNA (rnCGM6) encoding a PSG-related protein from a rat placental cDNA library. rnCGM6 is 2,068 bp in length and contains an open reading frame that encodes a 475-amino-acid polypeptide with a predicted molecular mass of 53 kD. The 5' noncoding sequence is 173 nucleotides, and primer-extension experiments demonstrate that the transcriptional initiation site is located 22-24 nucleotides further upstream. The 3' noncoding sequence contains 470 nucleotides which is followed by a poly(A) tail. In contrast to human PSGs, which contain one immunoglobulin variable-like and two to three immunoglobulin constant-like protein domains, rnCGM6 contains three immunoglobulin variable-like domains and one immunoglobulin constant-like domain. rnCGM6 contains six potential N-linked glycosylation sites and, in its carboxyl-terminal domain, a tyrosine protein kinase phosphorylation site. The tyrosine phosphorylation site is conserved among all rat and human PSG members. rnCGM6 hybridized with a major 2.5-kb and two minor 3.0- and 3.5-kb mRNAs, all primarily expressed in the rat placenta. Ribonuclease protection analysis, using probes specific to the 5', middle, and 3' regions of rnCGM6, and the 5' region of a previously identified cDNA, rnCGM1, mainly yielded fully-protected fragments indicating relatively low sequence similarity among rat PSG-related proteins. Northern hybridization and ribonuclease protection assays also suggest that rnCGM6 may be the major PSG member in rat.
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PMID:Characterization of a major member of the rat pregnancy-specific glycoprotein family. 154 19

Human chorionic gonadotrophin (hCG), placental alkaline phosphatase (PLAP), and pregnancy-specific glycoprotein (PSG) are three major proteins produced by the trophoblast of the human placenta. Immunocytochemical studies suggest that PSG and hCG are also present in the human amnion. In this study, we examined whether amniotic and chorionic membranes were capable of expressing trophoblastic-specific genes. As previously reported, trophoblasts express high levels of hCG beta, hCG alpha, PLAP, and PSG. Both amnion and chorion were found to express PLAP and hCG beta mRNA. However, the hCG alpha transcript was expressed only by the amnion, but not by the chorion in the term placenta. Recent molecular cloning studies indicate that human PSGs are a group of closely related placental proteins that, together with the carcinoembryonic antigen family members, comprise a subfamily within the immunoglobulin superfamily. To demonstrate that amnion and chorion also express PSG transcripts, we employed ribonuclease protection analysis using probes specific to the 5' and 3' region of PSG mRNAs. Our data indicate that while amniotic as well as chorionic membrane expressed low levels of the PSG genes, only a certain subpopulation of PSG transcripts were expressed. Furthermore, the amnion and chorion demonstrated differences in PSG species expression from each other and from trophoblastic tissue. Thus, human amnion, chorion and trophoblast selectively express several placental genes.
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PMID:Differential gene expression in the amnion, chorion, and trophoblast of the human placenta. 836 11

Glycoproteins generally exist as populations of glycosylated variants (glycoforms) of a single polypeptide. Although the same glycosylation machinery is available to all proteins that enter the secretory pathway in a given cell, most glycoproteins emerge with characteristic glycosylation patterns and heterogeneous populations of glycans at each glycosylation site. The factors that control the composition of the glycoform populations and the role that heterogeneity plays in the function of glycoproteins are important questions for glycobiology. A full understanding of the implications of glycosylation for the structure and function of a protein can only be reached when a glycoprotein is viewed as a single entity. Individual glycoproteins, by virtue of their unique structures, can selectively control their own glycosylation by modulating interactions with the glycosylating enzymes in the cell. Examples include protein-specific glycosylation within the immunoglobulins and immunoglobulin superfamily and site-specific processing in ribonuclease, Thy-1, IgG, tissue plasminogen activator, and influenza A hemagglutinin. General roles for the range of sugars on glycoproteins such as the leukocyte antigens include orientating the molecules on the cell surface. A major role for specific sugars is in recognition by lectins, including chaperones involved in protein folding. In addition, the recognition of identical motifs in different glycans allows a heterogeneous population of glycoforms to participate in specific biological interactions.
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PMID:Glycosylation: heterogeneity and the 3D structure of proteins. 906 19