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

Research output: Contribution to journal › Article › peer-review

24 Citations (Scopus)

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.

Original language	English
Pages (from-to)	5589-5595
Number of pages	7
Journal	FEBS Letters
Volume	579
Issue number	25
DOIs	https://doi.org/10.1016/j.febslet.2005.09.024
Publication status	Published - Oct 24 2005
Externally published	Yes

Keywords

ADAM12 integrin
Cancer
Cell adhesion
Focal adhesion
RhoA

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/j.febslet.2005.09.024

Cite this

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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.",

year = "2005",

month = oct,

day = "24",

doi = "10.1016/j.febslet.2005.09.024",

language = "English",

volume = "579",

pages = "5589--5595",

journal = "FEBS Letters",

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T1 - ADAM12-mediated focal adhesion formation is differently regulated by β1 and β3 integrins

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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U2 - 10.1016/j.febslet.2005.09.024

DO - 10.1016/j.febslet.2005.09.024

M3 - Article

C2 - 16213489

AN - SCOPUS:26844465553

SN - 0014-5793

VL - 579

SP - 5589

EP - 5595

JO - FEBS Letters

JF - FEBS Letters

IS - 25

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

UN SDGs

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