Cloning of five human cadherins clarifies characteristic features of cadherin extracellular domain and provides further evidence for two structurally different types of cadherin

Hidenobu Tanihara, Kenji Sano, Ronald L. Heimark, Tom John, Shintaro Suzuki

Research output: Contribution to journalArticlepeer-review

136 Scopus citations

Abstract

The entire coding sequences for five possible human cadherins, named cadherin-4,-8,-11,-12 and-13, were determined. The deduced amino acid sequences of cadherin-4 and cadherin-13 showed high homology with those of chicken R-cadherin or chicken T-caciherin, suggesting that cadherin-4 and cadherin-13 are mammalian homologues of the chicken R-cadherin or T-cadherin. Comparison of the extracellular domain of these proteins with those of other cadherins and cadherin-related proteins clarifies characteristic structural features of this domain. The domain is subdivided into five subdomains, each of which contains a cadherin-specific motif characterized by well-conserved amino acid residues and short amino acid sequences. Moreover, each subdomain has unique features of its own. The comparison also provides additional evidence for two structurally different types of cadherins: the first type includes B-, E-, EP-, M, N-, P-and R-cadherins and cadherin-4; the second type includes cadherin-5 through cadherin-12. Cadherin-13 lacks the sequence corresponding to the cytoplasmic domain of typical cadherins, but the extracellular domain shares most of the features common to the extracellular domain of cadherins, especially those of the first type of cadherins, suggesting that cadherin-13 is a special type of cadherin. These results, and those of other recent cloning studies, indicate that many cadherins with different properties are expressed in various tissues of different organisms.

Original languageEnglish (US)
Pages (from-to)15-26
Number of pages12
JournalCell Communication and Adhesion
Volume2
Issue number1
DOIs
StatePublished - Jan 1 1994
Externally publishedYes

Keywords

  • Cadherins
  • EC-N
  • Extracellular domain
  • Homology
  • Motif
  • PCR
  • Polymerase chain reaction
  • The N-th subdomain of the extracellular domain of cadherins and cadherin-related proteins

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Cell Biology

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