Molecular Cloning of Human Gastric Mucin MUC5AC Reveals Conserved Cysteine-Rich D-Domains and a Putative Leucine Zipper Motif

• Published in: Biochemical and biophysical research communications 1998-04, Vol.245 (3), p.853-859
• Main Authors: van de Bovenkamp, Jeroen H.B., Hau, Chi M., Strous, Ger J.A.M., Büller, Hans A., Dekker, Jan, Einerhand, Alexandra W.C.
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Blotting, Southern; Cloning, Molecular; Cysteine - analysis; DNA, Complementary - analysis; Gene Library; Humans; Leucine Zippers; Models, Molecular; Molecular Sequence Data; Mucin 5AC; Mucins - chemistry; Mucins - genetics; Polymerase Chain Reaction; Structure-Activity Relationship
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1006/bbrc.1998.8535

To further clone the human gastric mucin MUC5AC cDNA, we screened a human gastric cDNA library with previously identified MUC5AC sequences. We obtained 32 independent clones encoding newly identified sequences comprising the entire N-terminal sequence of MUC5AC, up to 3024 bp upstream of the previously identified MUC5AC sequences. The N-terminus of MUC5AC shows high homology (43% identity) with the N-terminus of MUC2 and contains three domains homologous to the D-domains found in the pro-von Willebrand factor. Furthermore, the N-terminus of MUC5AC contains a putative leucine zipper motif not found in any other mucin identified so far. Moreover, a large central repetitive sequence was identified encoding approximately 2500 amino acids (7.5 kb). We were able to establish that the MUC5AC cDNA together with the previously identified 6.1 kb of MUC5AC cDNA sequence is about 16.6 kb, encoding 5525 amino acids. A model of the domain structure of MUC5AC is presented.