Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.23 (beta-galactosidase)
 14,648 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

RPE65 is essential for all-trans- to 11-cis-retinoid isomerization, the hallmark reaction of the retinal pigment epithelium (RPE). Here, we identify regulatory elements in the Rpe65 gene and demonstrate their functional relevance to Rpe65 gene expression. We show that the 5' flanking region of the mouse Rpe65 gene, like the human gene, lacks a canonical TATA box and consensus GC and CAAT boxes. The mouse and human genes do share several cis-acting elements, including an octamer, a nuclear factor one (NFI) site, and two E-box sites, suggesting a conserved mode of regulation. A mouse Rpe65 promoter/beta-galactosidase transgene containing bases -655 to +52 (TR4) of the mouse 5' flanking region was sufficient to direct high RPE-specific expression in transgenic mice, whereas shorter fragments (-297 to +52 or -188 to +52) generated only background activity. Furthermore, transient transfection of analogous TR4/luciferase constructs also directed high reporter activity in the human RPE cell line D407 but weak activity in the non-RPE cell lines HeLa, HepG2, and HS27. Functional binding of potential transcription factors to the octamer sequence, AP-4, and NFI sites was demonstrated by directed mutagenesis, electrophoretic mobility shift assay, and cross-linking. Mutations of these sites abolished binding and corresponding transcriptional activity and indicated that octamer and E-box transcription factors synergistically regulate the RPE65 promoter function. Thus, we have identified the regulatory region in the Rpe65 gene that accounts for tissue-specific expression in the RPE and found that octamer and E-box transcription factors play a critical role in the transcriptional regulation of the Rpe65 gene.
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PMID:The upstream region of the Rpe65 gene confers retinal pigment epithelium-specific expression in vivo and in vitro and contains critical octamer and E-box binding sites. 1089 39

This study investigated the activity of beta-N-acetyloglucosaminidase (beta-NAGASE), alpha-mannosidase, and beta-galactosidase in the uterine luminal fluid of cows after superovulation treatment, along with the possible associations between the activity of these 3 glycosidases and the superovulatory response. Embryos and a sample of fluid flushed from each uterine horn were collected on day 7 after artificial insemination (on estrus day 0) from 32 cows in which superovulation was induced with porcine follicle-stimulating hormone. Glycosidase activity was assayed colorimetrically. The cows were classified as to superovulatory response according to the number of corpora lutea per ovary (group 1, 1 to 4; group 2, > 4) and according to the total number of embryos per horn (T1, 0; T2, 1 to 2; T3, 3 to 4; T4, > 4) and the number of transferable embryos per horn (TR1, 0; TR2, 1 to 2; TR3, 3 to 4; TR4, > 4). The mean activity of beta-NAGASE was significantly lower (P < 0.05) in group 2 than in group 1, at 95.99 (standard error 20.43) versus 226.72 (46.77) IU/L. It was also significantly lower (P < 0.01) in group T4 compared with groups T1, T2, and T3, at 50.09 (8.21) versus 129.25 (34.60), 222.27 (62.62), and 290.26 (93.77) IU/L, respectively, as well as in group T1 compared with group T3. There was a positive relationship between beta-NAGASE activity and both the total number of embryos (P = 0.047) and the number of transferable embryos per horn (P = 0.013) when 1 to 4 corpora lutea developed per ipsilateral ovary. No difference in alpha-mannosidase or beta-galactosidase activity was detected among the groups.
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PMID:Activity of glycosidases (beta-N-acetyloglucosaminidase, alpha-mannosidase, and beta-galactosidase) in the uterine luminal fluid of cows after multiple ovulation. 1795 5