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Gel-forming mucins appeared early in metazoan evolution.

Artikel i vetenskaplig tidskrift
Författare Tiange Lang
Gunnar C. Hansson
Tore Samuelsson
Publicerad i Proceedings of the National Academy of Sciences of the United States of America
Volym 104
Nummer/häfte 41
Sidor 16209-14
ISSN 0027-8424
Publiceringsår 2007
Publicerad vid Institutionen för biomedicin, avdelningen för medicinsk kemi och cellbiologi
Sidor 16209-14
Språk en
Länkar dx.doi.org/10.1073/pnas.0705984104
Ämnesord Animals, Chordata, Nonvertebrate, genetics, Evolution, Molecular, Gels, Humans, Membrane Glycoproteins, chemistry, genetics, Mucins, chemistry, genetics, Phylogeny, Protein Structure, Tertiary, Strongylocentrotus purpuratus, genetics, Xenopus, genetics, Xenopus Proteins, chemistry, genetics, von Willebrand Factor, chemistry, genetics
Ämneskategorier Medicin och Hälsovetenskap


Mucins are proteins that cover and protect epithelial cells and are characterized by domains rich in proline, threonine, and serine that are heavily glycosylated (PTS or mucin domains). Because of their sequence polymorphism, these domains cannot be used for evolutionary analysis. Instead, we have made use of the von Willebrand D (VWD) and SEA domains, typical for mucins. A number of animal genomes were examined for these domains to identify mucin homologues, and domains of the resulting proteins were used in phylogenetic studies. The frog Xenopus tropicalis stands out because the number of gel-forming mucins has markedly increased to at least 25 as compared with 5 for higher animals. Furthermore, the frog Muc2 homologues contain unique PTS domains where cysteines are abundant. This animal also has a unique family of secreted mucin-like proteins with alternating PTS and SEA domains, a type of protein also identified in the fishes. The evolution of the Muc4 mucin seems to have occurred by recruitment of a PTS domain to AMOP, NIDO, and VWD domains from a sushi domain-containing family of proteins present in lower animals, and Xenopus is the most deeply branching animal where a protein similar to the mammalian Muc4 was identified. All transmembrane mucins seem to have appeared in the vertebrate lineage, and the MUC1 mucin is restricted to mammals. In contrast, proteins with properties of the gel-forming mucins were identified also in the starlet sea anemone Nematostella vectensis, demonstrating an early origin of this group of mucins.

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