Open AccessProteomic Study of the Mucin Granulae in an Intestinal Goblet Cell Model
Author(s) -
Ana M. Rodríguez-Piñeiro,
Sjoerd van der Post,
Malin Johansson,
Kristina A. Thomsson,
Alexey I. Nesvizhskii,
Gunnar C. Hansson
Publication year - 2012
Publication title -
journal of proteome research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.644
H-Index - 161
eISSN - 1535-3907
pISSN - 1535-3893
DOI - 10.1021/pr2010988
Subject(s) - vesicle , mucin , mucin 2 , proteome , microbiology and biotechnology , secretion , secretory vesicle , mucus , goblet cell , proteomics , biology , secretory protein , biochemistry , chemistry , epithelium , membrane , gene expression , gene , ecology , genetics
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.