Lone Tjener Pallesen

Characterization of human mucin (MUC15) and identification of ovine and caprine orthologs.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

  • Lone Tjener Pallesen
  • Lise Refstrup Linnebjerg Pedersen, Aarhus Universitet, Department of Molecular Biology, Denmark
  • Torben Ellebæk Petersen, Aarhus University, Department of Molecular Biology, Denmark
  • Charlotte Rhode Knudsen, Aarhus University, Department of Molecular Biology, Denmark
  • Jan Trige Rasmussen, Aarhus University, Department of Molecular Biology, Denmark

The glycoprotein MUC15 (mucin 15) was initially isolated from the bovine milk fat globule membrane. The present work demonstrates the existence of immunologically similar proteins ( approximately 130 kDa) in ovine, caprine, porcine, and buffalo milk samples. Purification and N-terminal amino acid sequencing confirmed the presence of ovine and caprine MUC15 orthologs in milk fat globule membranes. Expression of MUC15 in human milk was demonstrated by immunostaining ( approximately 150 kDa) as well as by mass spectrometry. Screening of a human multiple tissue expression array showed abundant MUC15 gene expression in placenta, salivary gland, thyroid gland, trachea, esophagus, kidney, testis, and the leukemia K-562 cell line. Furthermore, moderate expression was seen in the pancreas, adult and fetal lung, fetal kidney, lymph node, adult and fetal thymus, and parietal lobe. Structural motifs for interactions (epidermal growth factor receptor and Src homology 2 domains) are identified in the intracellular region. Implication of the mucin in signal transduction and the potential physiological function of MUC15 are discussed.

Original languageEnglish
JournalJournal of Dairy Science
Volume91
Issue12
Pages (from-to)4477-4483
Number of pages8
ISSN0022-0302
Publication statusPublished - 2008
Externally publishedYes

See relations at Aarhus University Citationformats

ID: 19433420