Characterization of cadherin-4 and cadherin-5 reveals new aspects of cadherins

Hidenobu Tanihara, Mitsuru Kido, Shuichi Obata, Ronald L Heimark, Mari Davidson, Tom St John, Shintaro Suzuki

Research output: Contribution to journalArticle

68 Citations (Scopus)

Abstract

Several properties of cadherin-4 and cadherin-5 were characterized by using the cDNA transfection approach. The proteins of both cadherins had a relative molecular mass of about 130 kDa and were present at the cell periphery, especially at cell-cell contact sites. These cadherins were easily digested with trypsin, and Ca2+ protected cadherin-4, but not cadherin-5, from the digestion. In immunoprecipitation, cadherin-4 co-precipitated with two major proteins of 105 kDa and 95 kDa, respectively. The 105 kDa and the 95 kDa proteins are likely to correspond to α- and β-catenins. Cadherin-5 co-precipitated with only one major protein of 95 kDa, but seems to associate with the 105 kDa protein. On the other hand, plakoglobin or γ-catenin did not co-precipitate well with either cadherin-4 or cadherin-5 in immunoprecipitation, but plakoglobin also appears to associate weakly with these cadherins. Cadherin-4 transfectants aggregated within 30 minutes in a cell aggregation assay, but cadherin-5 transfectants did not aggregate under the same conditions. Furthermore, the transfectants of chimeric cadherin 4 with cadherin-5 cytoplasmic domain showed cell aggregation activity comparable to that of wild-type cadherin-4 transfectants, whereas the transfectants of chimeric cadherin-5 with cadherin-4 cytoplasmic domain did not show appreciable cell aggregation, suggesting that the extracellular domains of cadherins, in conjunction with their cytoplasmic domains, play an important role in cell aggregation activity. These results show that cadherin-4 is very similar to the classical cadherins, whereas cadherin-5 is functionally as well as structurally distinct from classical cadherins.

Original languageEnglish (US)
Pages (from-to)1697-1704
Number of pages8
JournalJournal of Cell Science
Volume107
Issue number6
StatePublished - Jun 1994

Fingerprint

Cadherins
Cell Aggregation
gamma Catenin
Catenins
Proteins
Immunoprecipitation
R-cadherin
cadherin 5
Trypsin
Transfection
Digestion
Complementary DNA

Keywords

  • Cadherin
  • Catenin
  • Cell adhesion
  • Cytoplasmic domain
  • Extracellular domain
  • Motif

ASJC Scopus subject areas

  • Cell Biology

Cite this

Tanihara, H., Kido, M., Obata, S., Heimark, R. L., Davidson, M., St John, T., & Suzuki, S. (1994). Characterization of cadherin-4 and cadherin-5 reveals new aspects of cadherins. Journal of Cell Science, 107(6), 1697-1704.

Characterization of cadherin-4 and cadherin-5 reveals new aspects of cadherins. / Tanihara, Hidenobu; Kido, Mitsuru; Obata, Shuichi; Heimark, Ronald L; Davidson, Mari; St John, Tom; Suzuki, Shintaro.

In: Journal of Cell Science, Vol. 107, No. 6, 06.1994, p. 1697-1704.

Research output: Contribution to journalArticle

Tanihara, H, Kido, M, Obata, S, Heimark, RL, Davidson, M, St John, T & Suzuki, S 1994, 'Characterization of cadherin-4 and cadherin-5 reveals new aspects of cadherins', Journal of Cell Science, vol. 107, no. 6, pp. 1697-1704.
Tanihara H, Kido M, Obata S, Heimark RL, Davidson M, St John T et al. Characterization of cadherin-4 and cadherin-5 reveals new aspects of cadherins. Journal of Cell Science. 1994 Jun;107(6):1697-1704.
Tanihara, Hidenobu ; Kido, Mitsuru ; Obata, Shuichi ; Heimark, Ronald L ; Davidson, Mari ; St John, Tom ; Suzuki, Shintaro. / Characterization of cadherin-4 and cadherin-5 reveals new aspects of cadherins. In: Journal of Cell Science. 1994 ; Vol. 107, No. 6. pp. 1697-1704.
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