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Proteomic study of the mucin granulae in an intestinal goblet cell model.

Journal article
Authors Ana María Rodríguez-Piñeiro
Sjoerd van der Post
Malin E V Johansson
Kristina A Thomsson
Alexey I Nesvizhskii
Gunnar C. Hansson
Published in Journal of proteome research
Volume 11
Issue 3
Pages 1879-90
ISSN 1535-3907
Publication year 2012
Published at Institute of Biomedicine, Department of Medical Biochemistry and Cell Biology
Pages 1879-90
Language en
Links dx.doi.org/10.1021/pr2010988
Keywords Cells, Cultured, Centrifugation, Density Gradient, Colon, Sigmoid, cytology, metabolism, secretion, Goblet Cells, metabolism, secretion, Humans, Mucin-2, chemistry, isolation & purification, metabolism, secretion, Peptide Fragments, chemistry, Principal Component Analysis, Protein Binding, Protein Interaction Mapping, Protein Transport, Proteomics, R-SNARE Proteins, metabolism, Receptors, Cell Surface, chemistry, metabolism, Secretory Vesicles, metabolism, Synaptotagmins, chemistry, metabolism, Vacuolar Proton-Translocating ATPases, chemistry, metabolism, rab3A GTP-Binding Protein, metabolism
Subject categories Basic Medicine, Cell and Molecular Biology

Abstract

Goblet cells specialize in producing and secreting mucus with its main component, mucins. An inducible goblet-like cell line was used for the purification of the mucus vesicles stored in these cells by density gradient ultracentrifugation, and their proteome was analyzed by nanoLC-MS and MS/MS. Although the density of these vesicles coincides with others, it was possible to reveal a number of proteins that after immunolocalization on colon tissue and functional analyses were likely to be linked to the MUC2 vesicles. Most of the proteins were associated with the vesicle membrane or their outer surface. The ATP6AP2, previously suggested to be associated with vesicular proton pumps, was colocalized with MUC2 without other V-ATPase proteins and, thus, probably has roles in mucin vesicle function yet to be discovered. FAM62B, known to be a calcium-sensitive protein involved in vesicle fusion, also colocalized with the MUC2 vesicles and is probably involved in unknown ways in the later events of the MUC2 vesicles and their secretion.

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