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  • Venkatakrishnan, Vignesh,1987Gothenburg University,Göteborgs universitet,Institutionen för medicin, avdelningen för reumatologi och inflammationsforskning,Institute of Medicine, Department of Rheumatology and Inflammation Research,University of Gothenburg (author)

Glycan analysis of human neutrophil granules implicates a maturation-dependent glycosylation machinery

  • Article/chapterEnglish2020

Publisher, publication year, extent ...

  • 2020

Numbers

  • LIBRIS-ID:oai:gup.ub.gu.se/297269
  • https://gup.ub.gu.se/publication/297269URI
  • https://doi.org/10.1074/jbc.RA120.014011DOI
  • https://research.chalmers.se/publication/519881URI
  • https://research.chalmers.se/publication/519586URI

Supplementary language notes

  • Language:English

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  • Subject category:ref swepub-contenttype
  • Subject category:art swepub-publicationtype

Notes

  • Protein glycosylation is essential to trafficking and immune functions of human neutrophils. During granulopoiesis in the bone marrow, distinct neutrophil granules are successively formed. Distinct receptors and effector proteins, many of which are glycosylated, are targeted to each type of granule according to their time of expression, a process called "targeting by timing." Therefore, these granules are time capsules reflecting different times of maturation that can be used to understand the glycosylation process during granulopoiesis. Herein, neutrophil subcellular granules were fractionated by Percoll density gradient centrifugation, andN- andO-glycans present in each compartment were analyzed by LC-MS. We found abundant paucimannosidicN-glycans and lack ofO-glycans in the early-formed azurophil granules, whereas the later-formed specific and gelatinase granules and secretory vesicles contained complexN-andO-glycans with remarkably elongatedN-acetyllactosamine repeats with Lewis epitopes. Immunoblotting and histochemical analysis confirmed the expression of Lewis X and sialyl-Lewis X in the intracellular granules and on the cell surface, respectively. Many glycans identified are unique to neutrophils, and their complexity increased progressively from azurophil granules to specific granules and then to gelatinase granules, suggesting temporal changes in the glycosylation machinery indicative of "glycosylation by timing" during granulopoiesis. In summary, this comprehensive neutrophil granule glycome map, the first of its kind, highlights novel granule-specific glycosylation features and is a crucial first step toward a better understanding of the mechanisms regulating protein glycosylation during neutrophil granulopoiesis and a more detailed understanding of neutrophil biology and function.

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  • Dieckmann, RegisGothenburg University,Göteborgs universitet,Institutionen för medicin, avdelningen för reumatologi och inflammationsforskning,Institute of Medicine, Department of Rheumatology and Inflammation Research,University of Gothenburg (author)
  • Loke, I.Macquarie University,Cordlife Group (author)
  • Tjondro, H. C.Macquarie University (author)
  • Chatterjee, S.Macquarie University (author)
  • Bylund, Johan,1975Gothenburg University,Göteborgs universitet,Institutionen för odontologi, sektion 3,Institute of Odontology, Section 3,University of Gothenburg(Swepub:gu)xbyljo (author)
  • Thaysen-Andersen, M.Macquarie University (author)
  • Karlsson, Niclas G.,1966Gothenburg University,Göteborgs universitet,Institutionen för biomedicin, avdelningen för medicinsk kemi och cellbiologi,Institute of Biomedicine, Department of Medical Biochemistry and Cell Biology,University of Gothenburg(Swepub:gu)xkanic (author)
  • Karlsson-Bengtsson, AnnaGothenburg University,Göteborgs universitet,Institutionen för medicin, avdelningen för reumatologi och inflammationsforskning,Institute of Medicine, Department of Rheumatology and Inflammation Research,University of Gothenburg,Chalmers tekniska högskola,Chalmers University of Technology(Swepub:cth)ankarls (author)
  • Göteborgs universitetInstitutionen för medicin, avdelningen för reumatologi och inflammationsforskning (creator_code:org_t)

Related titles

  • In:Journal of Biological Chemistry295:36, s. 12648-126600021-92581083-351X

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