ADAM 23/MDC3, a human disintegrin that promotes cell adhesion via interaction with the αvβ3 integrin through an RGD-independent mechanism

Santiago Cal, José M P Freije, José M. López, Yoshikazu Takada, Carlos López-Otín

Research output: Contribution to journalArticle

102 Scopus citations

Abstract

ADAM 23 (a disintegrin and metalloproteinase domain)/MDC3 (metalloprotease, disintegrin, and cysteine-rich domain) is a member of the disintegrin family of proteins expressed in fetal and adult brain. In this work we show that the disintegrin-like domain of ADAM 23 produced in Escherichia coli and immobilized on culture dishes promotes attachment of different human cells of neural origin, such as neuroblastoma cells (NB100 and SH-S(y)5(y)) or astrocytoma cells (U373 and U87 MG). Analysis of ADAM 23 binding to integrins revealed a specific interaction with αvβ3, mediated by a short amino acid sequence present in its putative disintegrin loop. This sequence lacks any RGD motif, which is a common structural determinant supporting αvβ3-mediated interactions of diverse proteins, including other disintegrins, αvβ3 also supported adhesion of HeLa cells transfected with a full-length cDNA for ADAM 23, extending the results obtained with the recombinant protein containing the disintegrin domain of ADAM 23. On the basis of these results, we propose that ADAM 23, through its disintegrin-like domain, may function as an adhesion molecule involved in αvβ3-mediated cell interactions occurring in normal and pathological processes, including progression of malignant tumors from neural origin.

Original languageEnglish (US)
Pages (from-to)1457-1469
Number of pages13
JournalMolecular Biology of the Cell
Volume11
Issue number4
StatePublished - Apr 2000
Externally publishedYes

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics
  • Cell Biology

Fingerprint Dive into the research topics of 'ADAM 23/MDC3, a human disintegrin that promotes cell adhesion via interaction with the αvβ3 integrin through an RGD-independent mechanism'. Together they form a unique fingerprint.

Cite this