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

The murine lymphocyte function-associated antigen 1 (LFA-1) is a glycoprotein heterodimer consisting of an Mr 180,000 alpha-chain and an Mr 95,000 beta-chain. Although LFA-1 has been studied extensively in the past few years due to its involvement in various antigen-specific T lymphocyte responses, virtually nothing is known about its glycosylation. In this report, we have analyzed the oligosaccharide moieties of the murine LFA-1 molecule. Utilizing a T lymphoma cell line, EL-4, it was found that [35S] sulfate, [3H]glucosamine, [3H]mannose, and [3H]fucose were incorporated into both the alpha- and beta-chains of LFA-1. Isolated alpha- and beta-chains from anti-LFA-1 immunoprecipitates of [3H]glucosamine-labeled NP-40 lysates were subjected to tryptic-chymotryptic digestion, and the resulting glycopeptides were fractionated by reverse-phase high performance liquid chromatography. Five major [3H]glucosamine-labeled glycopeptides were generated by this procedure from each of the two polypeptide chains. Treatment of the individual glycopeptides with almond emulsin peptide:N-glycosidase or Endo F demonstrated that the [3H]glucosamine label existed almost entirely in N-linked oligosaccharide structures (Mr 5000 to 10,000). By using similar techniques, the majority of the [35S]sulfate moieties were also found covalently bound to N-linked oligosaccharides. In addition, both [35S]sulfate-labeled alpha- and beta-chains were susceptible to Keratanase and endo-beta-galactosidase digestions, indicating the presence of sulfated N-acetyllactosamine sequences. The expression of [35S]sulfate-labeled LFA-1 on various cell types was also examined. LFA-1 was found to be sulfated only on thymocytes and splenic T cells, but not on macrophages, splenic B, or bone marrow cells.
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PMID:Lymphocyte function-associated antigen 1 (LFA-1) contains sulfated N-linked oligosaccharides. 388 93

The ER body is an endoplasmic reticulum (ER)-derived organelle. Because ER bodies are induced by wounding and methyl jasmonate (MeJA) treatment in rosette leaves, they might be responsible for defense systems. Recently, we isolated nai1 mutants that have no ER body and showed that the levels of PYK10 and PBP1 (PYK10-binding protein 1: At3g16420) were decreased in nai1 mutants. PYK10 is a beta-glucosidase that is localized in ER bodies. PBP1 consists of two repeated regions, each of which is highly homologous to the alpha-chain of jacalin, a carbohydrate-binding protein (lectin) of Artocarpus integriforia. We show in this study that PYK10 has two forms, an active form and an inactive form. The amount of active form increased during incubation of root homogenate. On the other hand, PYK10 separated into soluble and insoluble forms. Active PYK10 molecules mainly occurred as the insoluble form and inactive PYK10 molecules remain soluble. This suggests that the activation of PYK10 needs polymerization. In homogenates of both a pbp1 mutant and the wild type, PYK10 becomes insoluble, while PYK10 activity in pbp1 is only half of that in the wild type. PBP1 has an ability to interact with PYK10. Nonetheless, PBP1 does not bind active PYK10. These results suggest that PBP1 has some effect on the activation of PYK10. In addition, PBP1 was found to have a different subcellular distribution from PYK10. PBP1 may act like a molecular chaperone that facilitates the correct polymerization of PYK10, when tissues are damaged and subcellular structures are destroyed by pests.
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PMID:Activation of an ER-body-localized beta-glucosidase via a cytosolic binding partner in damaged tissues of Arabidopsis thaliana. 1591 74