Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.2.1.23 (beta-galactosidase)
14,648 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Several neurological diseases which affect the corpus striatum are candidates for gene therapy. We have developed a defective Herpes Simplex Virus (HSV-1) vector system to introduce genes into postmitotic cells, such as neurons. The prototype vector, pHSVlac, contains a transcription unit which places the E. coli Lac Z gene under the control of the HSV-1 immediate early (IE) 4/5 promoter, a constitutive promoter. We now demonstrate that a HSV-1 vector can deliver a gene into striatal neurons. Infection of cultured rat striatal neurons with pHSVlac virus resulted in stable expression of beta-galactosidase for at least two weeks, without cell death. The potential to replace the Lac Z gene with other genes of interest, such as the gene responsible for Huntington's Disease, once it is isolated, may lead to insights about the pathogenesis of this genetic neurodegenerative disease, and may provide a method for performing gene therapy on this disease. Similarly, introduction of the tyrosine hydroxylase gene, which encodes the rate-limiting enzyme in the conversion of tyrosine to dopamine, into striatal neurons might provide a novel gene therapy approach towards treating Parkinson's Disease.
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PMID:Infection of cultured striatal neurons with a defective HSV-1 vector: implications for gene therapy. 166 13

The 3'-terminal regions of the human T-cell leukemia virus I (HTLV-I) and HTLV-II genomes encode a novel gene product. We showed that expression of this region fused to the beta-galactosidase gene in bacteria produces a protein recognized by adult T-cell leukemia-lymphoma patient sera. Rabbit antibodies raised against this protein specifically precipitated the 42-kilodalton x-lor gene protein from HTLV-I-infected cells.
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PMID:Expression of the x-lor gene of human T-cell leukemia virus I in Escherichia coli. 299 73

The gene YAT1 from Saccharomyces cerevisiae encodes a protein of 688 amino acids which displays significant sequence similarity to vertebrate L-carnitine acyltransferases and yeast inner mitochondrial L-carnitine acetyltransferase. Steady state levels of the respective mRNA are low during growth on glucose or galactose, derepressed on glycerol, and significantly induced when ethanol or acetate are the only carbon sources. The YAT1 promotor region confers the identical carbon source dependence also on the expression of beta-galactosidase when cloned 5' to the Escherichia coli lacZ-coding region. An antiserum directed against a beta-galactosidase/Yat1p fusion protein recognizes a protein of 78-kDa molecular mass in the mitochondrial fraction from yeast. In vitro translated Yat1p, which lacks a cleavable presequence, binds to mitochondria in a protease-sensitive location in a standard in vitro import assay. Deletion of the single copy gene in a haploid yeast strain yields no obvious phenotype with any carbon source. Carnitine acetyltransferase activities of intact mitochondria from a YAT1 deletion mutant are slightly lower than wild type, but are approximately alike in lysed mitochondria from mutant and control cells. Thus, the novel gene is nonessential and likely to code for a minor mitochondrial outer carnitine acetyltransferase.
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PMID:The ethanol-inducible YAT1 gene from yeast encodes a presumptive mitochondrial outer carnitine acetyltransferase. 826 85

In a previous study a novel gene designated as US8.5 was identified in the unique short component of the herpes simplex virus type 1 (HSV1) genome. Epitope tagging experiments suggested the existence of a protein encoded by this gene in HSV1 infected cells. To further analyze the US8.5 gene product and function, a rabbit polyclonal antiserum was raised against a recombinant beta-galactosidase-US8.5 fusion protein expressed in E. coli. This antiserum reacted specifically with a 19 kDa protein in HSV1(F) infected cells as shown by immunoblotting and immunoprecipitation experiments. In addition, using the same antiserum a 21 kDa protein was detected in lysates from cells infected with HSV2(G), which was most likely the HSV2 homolog of US8.5. Kinetic studies indicated that US8.5 is expressed as gamma 1 gene. In addition, the US8.5 protein was immunoprecipitated with the anti-US8.5 serum from 32P-labeled lysates of Vero cells infected with HSV1, demonstrating that the protein is phosphorylated. Immunofluorescence studies localized the US8.5 protein to the nucleoli of HSV1 infected cells.
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PMID:Characterization of the US8.5 protein of herpes simplex virus. 857 43

We have devised a strategy to rapidly screen gene traps in mouse embryonic stem (ES) cells based on DNA sequence information and an in vitro analysis of gene expression. After the initial identification of ES cell clones expressing beta-galactosidase, tagged RNA transcripts were immediately cloned and sequenced in order to determine their identities. Novel gene sequences found were used to probe northern blots to examine the expression patterns of their cognate genes. Our initial characterization of 30 cDNA clones indicated that more than half of the tagged sequences were novel mouse genes and of these 40% showed a restricted pattern of expression in adult mouse tissues. This molecular characterization of gene traps is quick, reliable and well suited for the large-scale screening of mammalian developmental genes. Furthermore, since gene trap insertion frequently disrupts the tagged host gene, the ES cells can be used to produce transgenic animals for a genetic analysis of gene function.
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PMID:A molecular strategy designed for the rapid screening of gene traps based on sequence identity and gene expression pattern in adult mice. 903 82

A novel beta-galactosidase (beta-gal) gene was cloned from Bacillus circulans ATCC 31382. The coding region was 1,758 bp and encoded a polypeptide of 586 amino acids with a deduced molecular mass of 66,888. Active staining for beta-gal showed that B. circulans ATCC 31382 produced three beta-gal isozymes. Two of these were detected in Biolacta N5 (Daiwakasei Co.), but the product of this novel gene corresponded to the one not contained in Biolacta N5. The novel beta-gal showed the highest amino acid sequence identity (43.3%) with a beta 1-->3 > 1-->4 galactosidase from Xanthomonas manihotis and was also highly similar to beta-gals from animals, plants, and fungi. This suggests an evolutionary relationship between this novel gene and those of eukaryotic origins. One of the two B. circulans beta-gals, the nucleotide sequences of which are available in the GenBank, was 20% identical to the novel beta-gal. Other bacterial beta-gals showed little or no similarity. We propose that this novel beta-gal be called B. circulans beta-gal-3, and the gene be called bgaC.
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PMID:Cloning and characterization of the gene encoding a novel beta-galactosidase from Bacillus circulans. 930 Nov 6

A gene trap screen designed to isolate novel mouse genes involved in nervous system development was performed. Here, we describe the isolation and characterization of a novel gene, bodenin, which is expressed in restricted areas of the brain. beta-Galactosidase marker gene activity was detected in the embryo at the start of organogenesis (embryonic day 8.5; E8.5). Staining gradually became stronger until E12.5, when embryos exhibited widespread expression. In brains of newborn and adult mice, beta-galactosidase staining was confined predominantly to forebrain structures. Transcriptional activity was also observed in kidney, liver, lung, heart, skeletal muscle, and testes. Part of the trapped gene was isolated by 5'-rapid amplification of cDNA ends (5'-RACE). Isolation and sequencing of the complete cDNA revealed an unknown gene encoding a 200 amino acid protein. Comparison with published sequences showed 94% amino acid identity to a human integrin cytoplasmic domain-associated protein. Mice homozygous for the mutation were viable and did not exhibit any obvious abnormal phenotype. However, concealed phenotypic abnormalities cannot be excluded. The lack of readily visible abnormalities may also be due to functional compensation or to the production of low levels of wild-type protein in mice homozygous for the gene trap vector insertion. Nevertheless, the restricted expression of bodenin in the brain of newborn and adult mice suggests a role for this novel gene in the developing and mature central nervous system.
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PMID:Bodenin: a novel murine gene expressed in restricted areas of the brain. 962 4

We have cloned a novel gene encoding a human ubiquitin-specific protease (USP1). The product, which consists of 785 amino acids with a deduced molecular mass of 88.2 kDa, possesses His and Cys domains that are highly conserved in all members of the ubiquitin-specific processing (UBP) family of proteases. Recombinant USP1 protein showed genuine UBP activity, correctly cleaving Ub-beta-galactosidase to produce ubiquitin and beta-galactosidase. Chromosomal mapping by fluorescence in situ hybridization and radiation hybrid analyses localized the USP1 gene to the p31.3-p32.1 band of chromosome 1. As losses of heterozygosity or amplifications have been observed in the distal region of the short arm of chromosome 1 in some neuroblastomas, breast cancers, and pancreatic adenocarcinomas, the USP1 gene may be a candidate for either the tumor-suppressive or the oncogenic activities associated with that chromosomal region.
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PMID:Identification and chromosomal assignment of USP1, a novel gene encoding a human ubiquitin-specific protease. 980 42

The "Fab immunogene" is a novel gene transfer vehicle in which the Fab fragment of anti-human epidermal growth factor (EGF) receptor antibody B4G7 is conjugated with poly-L-lysine to form an affinity complex with DNA. It was developed to target delivery of therapeutic genes into EGF receptor-hyperproducing tumor cells. Various characteristic features of the immunogene have been documented (Chen et al., 1998). Here we add further evidence to prove that in vitro transfer of beta-galactosidase/Fab immunogene is exclusively to EGF receptor-positive cells and that the herpes simplex virus thymidine kinase (TK)/Fab immunogene induces substantial suicide effects on A431 tumor cells when treated together with ganciclovir. The in vivo specificity of the immunogene transfer was examined using A431 tumor-bearing nude mice. When these nude mice were injected intraperitoneally with the chloramphenicol acetyltransferase (CAT)/Fab immunogene, CAT DNA was detected in the tumors as well as in liver and kidney but not brain, whereas CAT mRNA and enzyme activity were detected only in the tumors. Local and intraperitoneal injection of the TK/Fab immunogene and subsequent administration of ganciclovir effectively suppressed the growth of A431 tumors transplanted on the backs of nude mice. These observations suggest a possible application of the Fab immunogene system in cancer gene therapy.
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PMID:Targeted in vivo delivery of therapeutic gene into experimental squamous cell carcinomas using anti-epidermal growth factor receptor antibody: immunogene approach. 987 65

We have identified a novel gene, USP15, encoding a human ubiquitin-specific protease (USP). The USP15 protein consists of 952 amino acids with a predicted molecular mass of 109.2 kDa and contains the highly conserved Cys and His boxes present in all members of the UBP family of deubiquitinating enzymes. USP15 shares 60.5% sequence identity and 76% sequence similarity with the human homolog (UNP/Unph/USP4) of the mouse Unp proto-oncogene. Recombinant USP15 demonstrated ubiquitin-specific protease activity against engineered linear fusions of ubiquitin to beta-galactosidase and glutathione S-transferase. USP15 can also cleave the ubiquitin-proline bond, a property previously unique to Unp/UNP. Chromosomal mapping by fluorescence in situ hybridization and radiation hybrid analyses localized the USP15 gene to chromosome band 12q14, a different location than that of UNP (3p21.3). Analysis of expressed sequence tag databases reveals evidence of alternate polyadenylation sites in the USP15 gene and also indicates that the gene may possess an exon/intron structure similar to that of the Unp gene, suggesting they have descended from a common ancestor. A systematic nomenclature for the human USPs is proposed.
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PMID:Identification, functional characterization, and chromosomal localization of USP15, a novel human ubiquitin-specific protease related to the UNP oncoprotein, and a systematic nomenclature for human ubiquitin-specific proteases. 1044 27


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