・ Splicing variant α4B of cell adhesion receptor α4 integrin has been identified.

・ α4B was also expressed in α4 integrin expression tissue, and expression of both forms was high in inflammatory tissue.

・ Although binding of α4B itself to α4 integrin extracellular matrix components is partial, when co-expressed with α4 integrin, binding to the extracellular matrix components is inhibited.

・ α4B inhibited α4 integrin involved melanoma cancer cell metastasis.

・ By clarifying the interaction between α4 integrin and α4B, development of new anticancer drugs can be expected.

At this time, we have discovered splicing variant α4B of α4 integrin. α4B works as endogenous inhibitor of α4 integrin and has been found to suppress cell adhesion reaction of α4 integrin and α4 integrin involved cancer cell metastasis. If integrin function can be artificially suppressed as a result of understanding the details of interaction between α4 integrin and α4B, this could lead to development of a new cancer drug.

This study has been published under “Papers in Press” of the April 22, 2014 issue of the authoritative biology magazine, The Journal of Biological Chemistry.

Shigeyuki Kon, Assoc. Professor, Dept. of Immunology,

Faculty of Pharmaceutical Sciences, Hokkaido University

TEL: +81-11-706-3920 / FAX: +81-11-706-4990

E-mail: kon@pharm.hokudai.ac.jp

Tadashi Matsuda, Professor, Dept. of Immunology,

Faculty of Pharmaceutical Sciences, Hokkaido University

TEL: +81-11-706-3243 / FAX: +81-11-706-4990

E-mail: tmastuda@pharm.hokudai.ac.jp