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  1. Article ; Online: Novel roles for O-linked glycans in protein folding.

    Vasudevan, Deepika / Haltiwanger, Robert S

    Glycoconjugate journal

    2014  Volume 31, Issue 6-7, Page(s) 417–426

    Abstract: ... in protein folding is not known. This article discusses past and recent advances made in novel roles ... N-Glycosylation has long been linked to protein folding and quality control ... also participate in this important function. Notably, Protein O-fucosyltransferase 1 (Ofut1/Pofut1 ...

    Abstract N-Glycosylation has long been linked to protein folding and quality control in the endoplasmic reticulum (ER). Recent work has shown that O-linked glycosylation and the corresponding glycosyltransferases also participate in this important function. Notably, Protein O-fucosyltransferase 1 (Ofut1/Pofut1), a soluble, ER localized enzyme that fucosylates Epidermal Growth Factor-like (EGF) repeats, functions as a chaperone involved in the proper localization of the Notch receptor in certain contexts. Pofut2, a related enzyme that modifies Thrombospondin type I repeats (TSRs), has also been hypothesized to play a role in the folding and quality control of TSR-containing proteins. Both enzymes only modify fully folded substrates suggesting that they are able to distinguish between folded and unfolded structures. Pofuts have known physiological relevance and are conserved across metazoans. Though consensus sequences for O-fucosylation have been established and structures of both Pofuts have been studied, the mechanism of how they participate in protein folding is not known. This article discusses past and recent advances made in novel roles for these protein O-glycosyltransferases.
    MeSH term(s) Animals ; Polysaccharides/chemistry ; Protein Folding ; Proteins/chemistry
    Chemical Substances Polysaccharides ; Proteins
    Language English
    Publishing date 2014-09-03
    Publishing country United States
    Document type Journal Article
    ZDB-ID 283770-5
    ISSN 1573-4986 ; 0282-0080
    ISSN (online) 1573-4986
    ISSN 0282-0080
    DOI 10.1007/s10719-014-9556-4
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2171: Show issues Location:
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    Jg. 1995 - 2021: Lesesall (1.OG)
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  2. Article: Retention of progenitor cell function in CD34+ cells purified using a novel O-sialoglycoprotease.

    Marsh, J C / Sutherland, D R / Davidson, J / Mellors, A / Keating, A

    Leukemia

    1992  Volume 6, Issue 9, Page(s) 926–934

    Abstract: ... linked glycans are not cleaved. Cleavage of the CD34 antigen results in the loss of epitopes detected ... This proteolytic enzyme specifically cleaves glycoproteins rich in O-sialoglycans. Glycoproteins containing only N ... by five of seven CD34-designated antibodies. In this study, we investigated the role of the P.h ...

    Abstract We previously showed that the sialoglycoprotein, CD34, which is expressed on primitive human hematopoietic progenitor cells, is cleaved by a unique glycoprotease from Pasteurella haemolytica (P.h. glycoprotease). This proteolytic enzyme specifically cleaves glycoproteins rich in O-sialoglycans. Glycoproteins containing only N-linked glycans are not cleaved. Cleavage of the CD34 antigen results in the loss of epitopes detected by five of seven CD34-designated antibodies. In this study, we investigated the role of the P.h. glycoprotease in isolating CD34+ cells from unfractionated normal human bone marrow mononuclear cells (MNCs), and determined the effect of the glycoprotease on the proliferative capacity of the progenitor-enriched fraction. CD34+ cells were isolated from MNCs using immunomagnetic beads attached via a CD34 antibody whose epitope is susceptible to removal by the cleavage with the glycoprotease. Subsequent cleavage with P.h. glycoprotease for 30 min at 37 degrees C released the CD34+ cells from the beads with a recovery of up to 78%. Using a CD34 antibody whose epitope was not removed by the glycoprotease, up to 95% of the recovered cells expressed CD34. Compared to unseparated MNCs, the CD34+ cells showed the following enrichment of committed hematopoietic progenitors, as assayed in semi-solid media: CFU-GM, 45-fold; CFU-M, 13-fold; BFU-E, 26-fold and CFU-GEMM, 81-fold. Hematopoiesis was also studied in two-stage long-term bone marrow cultures in which the CD34+ cells were co-cultured over irradiated, allogeneic adherent layers. Output of CFU-GM over a seven week period from these cultures was similar to that from control cultures with autologous adherent-cell-depleted marrow MNCs. These data suggest that the loss of O-sialo-glycosylated peptide moieties from P.h. glycoprotease-released CD34+ cells neither affects the functional capacity of committed progenitors, nor impairs the proliferation of long-term culture-generating cells. The P.h. glycoprotease can be used to facilitate the isolation and recovery of functionally competent CD34+ cells at high yield and purity, without prior removal of other adherent cells. The ability to rapidly purify CD34+ cells using this non-cytotoxic enzyme has important implications for bone marrow transplantation as well as for gene transfer studies in vitro.
    MeSH term(s) Antigens, CD/metabolism ; Antigens, CD34 ; Bone Marrow Cells ; Cell Division/drug effects ; Cell Separation/methods ; Cells, Cultured ; Colony-Forming Units Assay ; Hematopoietic Stem Cells/cytology ; Hematopoietic Stem Cells/drug effects ; Hematopoietic Stem Cells/immunology ; Humans ; Leukocytes, Mononuclear/cytology ; Leukocytes, Mononuclear/drug effects ; Leukocytes, Mononuclear/immunology ; Metalloendopeptidases/pharmacology
    Chemical Substances Antigens, CD ; Antigens, CD34 ; Metalloendopeptidases (EC 3.4.24.-) ; O-sialoglycoprotein endopeptidase (EC 3.4.24.57)
    Language English
    Publishing date 1992-09
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 807030-1
    ISSN 1476-5551 ; 0887-6924
    ISSN (online) 1476-5551
    ISSN 0887-6924
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2295: Show issues Location:
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