Human serum amyloid A3 peptide enhances intestinal MUC3 expression and inhibits EPEC adherence

Marilynn A. Larson, Shu H. Wei, Annika Weber, David R. Mack, Thomas L. McDonald

Research output: Contribution to journalArticle

54 Scopus citations

Abstract

We previously determined that the N-terminal region of bovine mammary-associated serum amyloid A3 (M-SAA3) increased intestinal mucin MUC3 levels in HT29 human intestinal cells by ∼2.5-fold, relative to untreated cells. This study shows that the human M-SAA3 N-terminal peptide further enhances MUC3 transcript levels by ∼4.3-fold in these cells (p<0.02), implicating a species-specific interaction. Furthermore, immunofluorescence and immunoblot analysis using a MUC3-specific monoclonal antibody confirms that the human M-SAA3 peptide stimulates MUC3 protein expression and secretion by the HT29 cells. More importantly, pretreatment of the cells with the peptide causes a subsequent 73% decrease in the adherence of enteropathogenic Escherichia coli (EPEC) to these cells, relative to untreated cells (p<0.01). The intestinal mucin MUC3 has been shown to provide a protective barrier in the gut and inhibit adherence of pathogens to the gut wall. Therefore, a means to increase MUC3 protein expression by a colostrum-associated peptide or protein may be a highly effective prophylactic treatment for the prevention of gastrointestinal diseases such as necrotizing enterocolitis and infectious diarrhea.

Original languageEnglish (US)
Pages (from-to)531-540
Number of pages10
JournalBiochemical and Biophysical Research Communications
Volume300
Issue number2
DOIs
StatePublished - Jan 10 2003

Keywords

  • Colostrum
  • EPEC
  • Intestinal mucin
  • MUC3
  • Mammary-associated serum amyloid A3

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Human serum amyloid A3 peptide enhances intestinal MUC3 expression and inhibits EPEC adherence'. Together they form a unique fingerprint.

  • Cite this