ADAM12-mediated focal adhesion formation is differently regulated by β1 and β3 integrins

Charles Kumar Thodeti; Camilla Fröhlich; Christian Kamp Nielsen; Yoshikazu Takada; Reinhard Fässler; Reidar Albrechtsen; Ulla M. Wewer

doi:10.1016/j.febslet.2005.09.024

ADAM12-mediated focal adhesion formation is differently regulated by β1 and β3 integrins

Charles Kumar Thodeti, Camilla Fröhlich, Christian Kamp Nielsen, Yoshikazu Takada, Reinhard Fässler, Reidar Albrechtsen, Ulla M. Wewer

研究成果: 雜誌貢獻 › 文章 › 同行評審

24 引文斯高帕斯（Scopus）

摘要

ADAM12, a disintegrin and metalloprotease, has been demonstrated to be upregulated in human malignant tumors and to accelerate the malignant phenotype in a mouse model for breast cancer. ADAM12 is a substrate for β1 integrins and may affect tumor and stromal cell behavior through its binding to β1 integrins. Here, we report that cells deficient in β1 integrin or overexpressing β3 integrin can bind to recombinant full-length human ADAM12 via β3 integrin. Furthermore, cell binding to ADAM12 via β3 integrin results in the formation of focal adhesions, which are not formed upon β1 integrin-mediated cell attachment. We also show that RhoA is involved in β3 integrin-mediated focal adhesion formation.

原文	英語
頁（從 - 到）	5589-5595
頁數	7
期刊	FEBS Letters
卷	579
發行號	25
DOIs	https://doi.org/10.1016/j.febslet.2005.09.024
出版狀態	已發佈 - 10月 24 2005
對外發佈	是

ASJC Scopus subject areas

生物物理學
結構生物學
生物化學
分子生物學
遺傳學
細胞生物學

UN SDG

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10.1016/j.febslet.2005.09.024

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title = "ADAM12-mediated focal adhesion formation is differently regulated by β1 and β3 integrins",

abstract = "ADAM12, a disintegrin and metalloprotease, has been demonstrated to be upregulated in human malignant tumors and to accelerate the malignant phenotype in a mouse model for breast cancer. ADAM12 is a substrate for β1 integrins and may affect tumor and stromal cell behavior through its binding to β1 integrins. Here, we report that cells deficient in β1 integrin or overexpressing β3 integrin can bind to recombinant full-length human ADAM12 via β3 integrin. Furthermore, cell binding to ADAM12 via β3 integrin results in the formation of focal adhesions, which are not formed upon β1 integrin-mediated cell attachment. We also show that RhoA is involved in β3 integrin-mediated focal adhesion formation.",

keywords = "ADAM12 integrin, Cancer, Cell adhesion, Focal adhesion, RhoA",

author = "Thodeti, {Charles Kumar} and Camilla Fr{\"o}hlich and Nielsen, {Christian Kamp} and Yoshikazu Takada and Reinhard F{\"a}ssler and Reidar Albrechtsen and Wewer, {Ulla M.}",

note = "Funding Information: The study was supported by grants from the Danish Cancer Society, the Danish Medical Research Council, and the Dansk Kr{\ae}ftforskningsfond, Lundbeck, Novo Nordisk, Munksholm, and Friis Foundations. We thank Eva Engvall for helpful comments on the manuscript and Linda Raab and Dana Beitner-Johnson for editorial assistance.",

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AU - Thodeti, Charles Kumar

AU - Fröhlich, Camilla

AU - Nielsen, Christian Kamp

AU - Takada, Yoshikazu

AU - Fässler, Reinhard

AU - Albrechtsen, Reidar

AU - Wewer, Ulla M.

N1 - Funding Information: The study was supported by grants from the Danish Cancer Society, the Danish Medical Research Council, and the Dansk Kræftforskningsfond, Lundbeck, Novo Nordisk, Munksholm, and Friis Foundations. We thank Eva Engvall for helpful comments on the manuscript and Linda Raab and Dana Beitner-Johnson for editorial assistance.

PY - 2005/10/24

Y1 - 2005/10/24

N2 - ADAM12, a disintegrin and metalloprotease, has been demonstrated to be upregulated in human malignant tumors and to accelerate the malignant phenotype in a mouse model for breast cancer. ADAM12 is a substrate for β1 integrins and may affect tumor and stromal cell behavior through its binding to β1 integrins. Here, we report that cells deficient in β1 integrin or overexpressing β3 integrin can bind to recombinant full-length human ADAM12 via β3 integrin. Furthermore, cell binding to ADAM12 via β3 integrin results in the formation of focal adhesions, which are not formed upon β1 integrin-mediated cell attachment. We also show that RhoA is involved in β3 integrin-mediated focal adhesion formation.

AB - ADAM12, a disintegrin and metalloprotease, has been demonstrated to be upregulated in human malignant tumors and to accelerate the malignant phenotype in a mouse model for breast cancer. ADAM12 is a substrate for β1 integrins and may affect tumor and stromal cell behavior through its binding to β1 integrins. Here, we report that cells deficient in β1 integrin or overexpressing β3 integrin can bind to recombinant full-length human ADAM12 via β3 integrin. Furthermore, cell binding to ADAM12 via β3 integrin results in the formation of focal adhesions, which are not formed upon β1 integrin-mediated cell attachment. We also show that RhoA is involved in β3 integrin-mediated focal adhesion formation.

KW - ADAM12 integrin

KW - Cancer

KW - Cell adhesion

KW - Focal adhesion

KW - RhoA

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JO - FEBS Letters

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ADAM12-mediated focal adhesion formation is differently regulated by β1 and β3 integrins

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