Calreticulin is directly involved in anti-alpha3 integrin antibody-mediated secretion and activation of matrix metalloprotease-2

Biochemical and Biophysical Research Communications
H ItoS Kubota

Abstract

Matrix metalloprotease-2 (MMP-2) plays a pivotal role in cancer invasion and metastasis. Invasive human rhabdomyosarcoma cells (RD) secrete proMMP-2. We recently reported that anti-alpha3 integrin antibody induced the activated form of MMP-2 and enhanced proMMP-2 secretion by RD cells with concomitant enhancement of RD cell invasion. Since recent studies showed that calreticulin interacts with integrin alpha subunit, we hypothesized that calreticulin may be involved in signal transduction of anti-alpha3 integrin antibody-mediated MMP-2 secretion and activation. Here we demonstrate that anti-alpha3 integrin antibody induced a transient enhanced interaction of calreticulin with alpha3 integrin. Transfection of antisense oligonucleotides of calreticulin in RD cells abrogated the interaction between calreticulin and alpha3 integrin, and completely suppressed activation of MMP-2 and enhanced secretion of proMMP-2 induced by anti-alpha3 integrin antibody. Transient overexpression of calreticulin cDNA in RD cells significantly increased secretion of proMMP-2. The results demonstrate for the first time that calreticulin is directly involved in MMP-2 secretion and activation.

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Citations

Dec 4, 2008·Annals of Surgical Oncology·Chiung-Nien ChenKing-Jen Chang
Mar 10, 2016·Expert Opinion on Therapeutic Targets·Paul EggletonMarek Michalak
Apr 22, 2003·Journal of Cellular Biochemistry·Gisela BrünagelRobert H Getzenberg
Jan 1, 2005·The Journal of Membrane Biology·Tsutomu Tsuji
Apr 1, 2019·Apoptosis : an International Journal on Programmed Cell Death·Alejandro Schcolnik-CabreraFela Mendlovic
Feb 1, 2006·Molecular Cancer Research : MCR·Jean SpenceDan Mercola
Jul 20, 2006·Cancer Research·Sabine GesierichMargot Zöller
Mar 15, 2006·Differentiation; Research in Biological Diversity·Edyta BrzóskaJerzy Moraczewski

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