Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.21 (beta-glucosidase)
 3,280 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

3'5'-cGMP activated beta-glucuronidase, beta-galactosidase, beta-glucosidase and N-acetyl-beta-glucosaminidase in blood platelets, while 2'3'-cGMP, 3,5'-cGMP, N2O2'-dipalmitoyl and 5'-GMP did not affect the activity of these glycosidases. The guanylate cyclase system appears to be involved in activation of blood platelets glycosidases since it is well known that 3'5'-cGMP activates the thrombocyte protein kinase.
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PMID:[The role of the modification of cyclic purine nucleotide molecule in the regulation of platelet acid glycosidase activity]. 282 26

A 60 kDa protein (P60) co-purified with phytochrome was identified as avenacosidase, a beta-glucosidase which is part of the defense system of Avena sativa. An antiserum raised against P60 was used to isolate a cDNA clone coding for the complete amino acid sequence of P60. The cDNA-derived amino acid sequence contained the partial sequences described before for a protein kinase [(1989) Planta 178, 199-206] and for a TCP1-related molecular chaperone [(1993) Nature 363, 644-647] co-purified with phytochrome. We conclude that these activities were related to minor contaminants and that only sequences of avenacosidase had been obtained.
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PMID:The amino acid sequence previously attributed to a protein kinase or a TCP1-related molecular chaperone and co-purified with phytochrome is a beta-glucosidase. 801 61

Sulfate transport was examined in rat liver lysosomes that were isolated from thyroid hormone-treated, thyroidectomized, and control animals. Sulfate uptake was significantly decreased in lysosomes from animals that had received intraperitoneal T3 (3,5,3'-triiodothyronine) at a dose of 20 micrograms/100 g body weight. The effect of T3 was maximal by 24 h post-injection and resulted in marked decreases in both Vmax (control: 155 +/- 33 pmol/unit of beta-hexosaminidase/30 s versus T3 treated: 24 +/- 7 pmol/unit of beta-hexosaminidase/30 s) and Km (control: 213 +/- 34 microM versus T3 treated: 92 +/- 6 microM). Thyroidectomy was associated with a significant increase in Vmax (control: 250 pmol/unit of beta-hexosaminidase/30 s versus thyroidectomized: 564 pmol/unit of beta-hexosaminidase/30 s), while Km was not significantly affected. The effect of thyroid hormone on lysosomal sulfate transport appeared to be relatively specific. In contrast to its effect on sulfate transport, T3 treatment had no effect on the uptake of either glucose or N-acetylglucosamine by rat liver lysosomes. Lysosomal pH, acidification in response to Mg/ATP, and the specific activities of alpha-L-iduronidase, beta-hexosaminidase, beta-D-glucosidase, and acid phosphatase were unaffected by T3 administration. Incubation of T3 with lysosomes from control animals had little or no effect on sulfate transport. Treatment of isolated lysosomes with either protein kinase A or alkaline phosphatase resulted in modest stimulation of transport. Thus, T3 does not appear to regulate transport by either direct interaction with the lysosomal transporter or protein kinase A-mediated phosphorylation. The exact mechanism for the inhibitory effect of T3 on lysosomal sulfate transport remains to be determined.
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PMID:Regulation of lysosomal sulfate transport by thyroid hormone. 808 19

We used two-dimensional electrophoresis (2-DE) and other proteomic approaches to identify proteins expressed in suspension-cultured rice cells in response to the rice blast fungus, Magnaporthe grisea. Proteins were extracted from suspension-cultured cells at 24 and 48 h after rice blast fungus inoculation or treatment with elicitor or other signal molecules such as jasmonic acid (JA), salicylic acid, and H(2)O(2). The proteins were then polyethylene glycol fractionated before separation by 2-DE. Fourteen protein spots were induced or increased by the treatments, which we analyzed by N-terminal or internal amino acid sequencing. Twelve proteins from six different genes were identified. Rice pathogen-related protein class 10 (OsPR-10), isoflavone reductase like protein, beta-glucosidase, and putative receptor-like protein kinase were among those induced by rice blast fungus; these have not previously been reported in suspension-cultured rice cells. Six isoforms of probenazole-inducible protein (PBZ1) and two isoforms of salt-induced protein (SalT) that responded to blast fungus, elicitor, and JA were also resolved on a 2-DE gel and identified by proteome analysis. The expression level of these induced proteins both in suspension-cultured cells and in leaves of whole plants was analyzed by Western blot. PBZ1, OsPR-10, and SalT proteins from incompatible reactions were induced earlier and to a greater extent than those in compatible reactions. Proteome analysis can thus distinguish differences in the timing and amount of protein expression induced by pathogens and other signal molecules in incompatible and compatible interactions.
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PMID:Proteomic analysis of differentially expressed proteins induced by rice blast fungus and elicitor in suspension-cultured rice cells. 1467 87

Sporothrix schenckii induced sporotrichosis has gained importance in recent years because of its worldwide prevalence. The dimorphic switching process is required for the pathogenesis of S. schenckii. Previously, we found that STE20-like protein kinase (SsSte20) was overexpressed in the early yeast stage, but not in the mycelial stage of S. schenckii, which suggested its involvement in morphogenesis of this fungal pathogen. It remains unclear, however, whether SsSte20 is essential for dimorphic switching of S. schenckii and what are its related genes. In this study, the function of SsSte20 was investigated using double-stranded RNA interference (dsRNAi) mediated by Agrobacterium tumefaciens. We evaluated its effects on normal asexual development, yeast-phase cell formation, and cell wall composition and integrity. In addition, by transcriptome analysis of the SsSte20 knockdown (SsSte20-i) mutant and the standard S. schenckii strain, we further investigated the genes and pathways that were affected by SsSte20. Our results showed that inactivation of SsSte20 significantly affected the growth and internal components of S. schenckii conidia and impaired the dimorphic switching process. RNA transcriptome analysis of the standard S. schenckii strain and the SsSte20-i mutant revealed that SsSte20 inhibition affected the genes that were not only involved in the biological process, but also in the cellular component, and the molecular functions of S. schenckii. It mainly affected the expression of iron/ion-binding transporter genes, oxidation-reduction-related genes, 1, 3-beta-glucosidase, and methylsterol monooxygenase, which are highly associated with environmental information processing and the biosynthesis of cell wall components. Overall, our research supports the claim that SsSte20 plays an essential role in the dimorphism of S. schenckii and affects its global transcriptome.
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PMID:Ste20 is crucial for dimorphic switching of sporothrix schenckii and affects its global transcriptome. 3226 78