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Gastric MUC5AC and MUC6 are large oligomeric mucins that differ in size, glycosylation and tissue distribution.

Nordman, Henrik LU ; Davies, Julia LU ; Lindell, Gert LU ; de Bolós, Carme; Real, Francisco and Carlstedt, Ingemar LU (2002) In Biochemical Journal 364(Pt 1). p.191-200
Abstract
Gastric MUC5AC and MUC6 mucins were studied using polyclonal antibodies. Immunohistochemistry showed MUC5AC to originate from the surface epithelium, whereas MUC6 was produced by the glands. Mucins from the surface epithelium or glands of corpus and antrum were purified using CsCl/4M guanidinium chloride density-gradient centrifugation. MUC5AC appeared as two distinct populations at 1.4 and 1.3 g/ml, whereas MUC6, which was enriched in the gland tissue, appeared at 1.45 g/ml. Reactivity with antibodies against the Le(b) structure (where Le represents the Lewis antigen) followed the MUC5AC distribution, whereas antibodies against the Le(y) structure and reactivity with the GlcNAc-selective Solanum tuberosum lectin coincided with MUC6,... (More)
Gastric MUC5AC and MUC6 mucins were studied using polyclonal antibodies. Immunohistochemistry showed MUC5AC to originate from the surface epithelium, whereas MUC6 was produced by the glands. Mucins from the surface epithelium or glands of corpus and antrum were purified using CsCl/4M guanidinium chloride density-gradient centrifugation. MUC5AC appeared as two distinct populations at 1.4 and 1.3 g/ml, whereas MUC6, which was enriched in the gland tissue, appeared at 1.45 g/ml. Reactivity with antibodies against the Le(b) structure (where Le represents the Lewis antigen) followed the MUC5AC distribution, whereas antibodies against the Le(y) structure and reactivity with the GlcNAc-selective Solanum tuberosum lectin coincided with MUC6, suggesting that the two mucins are glycosylated differently. Rate-zonal centrifugation of whole mucins and reduced subunits showed that both gastric MUC5AC and MUC6 are oligomeric glycoproteins composed of disulphide-bond linked subunits and that oligomeric MUC5AC was apparently smaller than MUC6. A heterogeneous population of 'low-density' MUC5AC mucins, which were smaller than the 'high-density' ones both before and after reduction, reacted with an antibody against a variable number tandem repeat sequence within MUC5AC, suggesting that they represent precursor forms of this mucin. Following ion-exchange HPLC, both MUC5AC and MUC6 appeared as several distinct populations, probably corresponding to 'glycoforms' of the mucins, the most highly charged of which were found in the gland tissue. (Less)
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subject
keywords
Chromatography, High Pressure Liquid, Enzyme-Linked Immunosorbent Assay, Epithelial Cells, Immunohistochemistry, Human, Glycosylation, Mucins : biosynthesis, Mucins : chemistry, Protein Isoforms, Stomach : metabolism, Tertiary, Protein Structure, Support, Non-U.S. Gov't, Density Gradient, Centrifugation
in
Biochemical Journal
volume
364
issue
Pt 1
pages
191 - 200
publisher
Portland Press Limited
external identifiers
  • pmid:11988092
  • wos:000175744200023
  • scopus:0037093409
ISSN
0264-6021
language
English
LU publication?
yes
id
731e781c-249d-4bc5-816c-0998fa3a268a (old id 107970)
alternative location
http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11988092&dopt=Abstract
date added to LUP
2007-07-18 13:28:25
date last changed
2017-10-01 04:44:20
@article{731e781c-249d-4bc5-816c-0998fa3a268a,
  abstract     = {Gastric MUC5AC and MUC6 mucins were studied using polyclonal antibodies. Immunohistochemistry showed MUC5AC to originate from the surface epithelium, whereas MUC6 was produced by the glands. Mucins from the surface epithelium or glands of corpus and antrum were purified using CsCl/4M guanidinium chloride density-gradient centrifugation. MUC5AC appeared as two distinct populations at 1.4 and 1.3 g/ml, whereas MUC6, which was enriched in the gland tissue, appeared at 1.45 g/ml. Reactivity with antibodies against the Le(b) structure (where Le represents the Lewis antigen) followed the MUC5AC distribution, whereas antibodies against the Le(y) structure and reactivity with the GlcNAc-selective Solanum tuberosum lectin coincided with MUC6, suggesting that the two mucins are glycosylated differently. Rate-zonal centrifugation of whole mucins and reduced subunits showed that both gastric MUC5AC and MUC6 are oligomeric glycoproteins composed of disulphide-bond linked subunits and that oligomeric MUC5AC was apparently smaller than MUC6. A heterogeneous population of 'low-density' MUC5AC mucins, which were smaller than the 'high-density' ones both before and after reduction, reacted with an antibody against a variable number tandem repeat sequence within MUC5AC, suggesting that they represent precursor forms of this mucin. Following ion-exchange HPLC, both MUC5AC and MUC6 appeared as several distinct populations, probably corresponding to 'glycoforms' of the mucins, the most highly charged of which were found in the gland tissue.},
  author       = {Nordman, Henrik and Davies, Julia and Lindell, Gert and de Bolós, Carme and Real, Francisco and Carlstedt, Ingemar},
  issn         = {0264-6021},
  keyword      = {Chromatography,High Pressure Liquid,Enzyme-Linked Immunosorbent Assay,Epithelial Cells,Immunohistochemistry,Human,Glycosylation,Mucins : biosynthesis,Mucins : chemistry,Protein Isoforms,Stomach : metabolism,Tertiary,Protein Structure,Support,Non-U.S. Gov't,Density Gradient,Centrifugation},
  language     = {eng},
  number       = {Pt 1},
  pages        = {191--200},
  publisher    = {Portland Press Limited},
  series       = {Biochemical Journal},
  title        = {Gastric MUC5AC and MUC6 are large oligomeric mucins that differ in size, glycosylation and tissue distribution.},
  volume       = {364},
  year         = {2002},
}