Mutated E-cadherin: Genomic and functional characterization in thyroid cells from the KAT family

• Type: Article in International Scientific Journal
• Date: 2004

Authors

Rocha, AS (Author) Other; De Wever, O (Author) Other; Moreira, S (Author) Other; Costa, MJ (Author) Other; Vandekerckhove, J (Author) Other; Mareel, M (Author) Other; Soares, P (Author) FMUP

Journal

Title: Thyroid

Vol. 14

Pages: 902-909

ISSN: 1050-7256

Publisher: Mary Ann Liebert

Indexing

ISI Web of Knowledge - 7 Citations

Scopus - 7 Citations

Scientific classification

FOS: Medical and Health sciences > Clinical medicine

Other information

Authenticus ID: P-000-81H

DOI: 10.1089/thy.2004.14.902

Abstract (EN): Members of a family of thyroid cell lines (KAT) were analyzed because they expressed a higher molecular weight (135 kd) form of E-cadherin at their surface. We found that this aberrant E-cadherin is the result of a point mutation in the exon 9 donor splice site causing a skipping of exon 9 with consequent deletion of the corresponding aminoacids on E-cadherin protein. As a spin-off, we report that the various members of the KAT family share this mutation as well as the genetic background. Furthermore we found that this mutated protein leads to disturbed cell-cell adhesion although E-cadherin is still able to mediate the formation of the cadherin/catenin complex. We also demonstrate the presence of another cell-cell adhesion complex, formed by P-cadherin and the catenins. The latter is also not able to mediate cell-cell adhesion. Although these cells lack cell-cell adhesion they are not invasive without exogenous stimulus.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 8