Webbläsaren som du använder stöds inte av denna webbplats. Alla versioner av Internet Explorer stöds inte längre, av oss eller Microsoft (läs mer här: * https://www.microsoft.com/en-us/microsoft-365/windows/end-of-ie-support).

Var god och använd en modern webbläsare för att ta del av denna webbplats, som t.ex. nyaste versioner av Edge, Chrome, Firefox eller Safari osv.

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

Författare

  • Henrik Nordman
  • Julia Davies
  • Gert Lindell
  • Carme de Bolós
  • Francisco Real
  • Ingemar Carlstedt

Summary, in English

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.

Publiceringsår

2002

Språk

Engelska

Sidor

191-200

Publikation/Tidskrift/Serie

Biochemical Journal

Volym

364

Issue

Pt 1

Dokumenttyp

Artikel i tidskrift

Förlag

Portland Press

Ämne

  • Biochemistry and Molecular Biology

Nyckelord

  • 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

Status

Published

Forskningsgrupp

  • Diabetic Complications

ISBN/ISSN/Övrigt

  • ISSN: 0264-6021