ADAM12-mediated focal adhesion formation is differently regulated by beta1 and beta3 integrins.

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Standard

ADAM12-mediated focal adhesion formation is differently regulated by beta1 and beta3 integrins. / Thodeti, Charles Kumar; Frohlich, Camilla; Nielsen, Christian Kamp; Takada, Yoshikazu; Fässler, Reinhard; Albrechtsen, Reidar; Wewer, Ulla M.

I: FEBS Letters, Bind 579, Nr. 25, 2005, s. 5589-95.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Thodeti, CK, Frohlich, C, Nielsen, CK, Takada, Y, Fässler, R, Albrechtsen, R & Wewer, UM 2005, 'ADAM12-mediated focal adhesion formation is differently regulated by beta1 and beta3 integrins.', FEBS Letters, bind 579, nr. 25, s. 5589-95. https://doi.org/10.1016/j.febslet.2005.09.024

APA

Thodeti, C. K., Frohlich, C., Nielsen, C. K., Takada, Y., Fässler, R., Albrechtsen, R., & Wewer, U. M. (2005). ADAM12-mediated focal adhesion formation is differently regulated by beta1 and beta3 integrins. FEBS Letters, 579(25), 5589-95. https://doi.org/10.1016/j.febslet.2005.09.024

Vancouver

Thodeti CK, Frohlich C, Nielsen CK, Takada Y, Fässler R, Albrechtsen R o.a. ADAM12-mediated focal adhesion formation is differently regulated by beta1 and beta3 integrins. FEBS Letters. 2005;579(25):5589-95. https://doi.org/10.1016/j.febslet.2005.09.024

Author

Thodeti, Charles Kumar ; Frohlich, Camilla ; Nielsen, Christian Kamp ; Takada, Yoshikazu ; Fässler, Reinhard ; Albrechtsen, Reidar ; Wewer, Ulla M. / ADAM12-mediated focal adhesion formation is differently regulated by beta1 and beta3 integrins. I: FEBS Letters. 2005 ; Bind 579, Nr. 25. s. 5589-95.

Bibtex

@article{8b7882f05a4f11dd8d9f000ea68e967b,
title = "ADAM12-mediated focal adhesion formation is differently regulated by beta1 and beta3 integrins.",
abstract = "ADAM12, adisintegrin 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 beta1 integrins and may affect tumor and stromal cell behavior through its binding to beta1 integrins. Here, we report that cells deficient in beta1 integrin or overexpressing beta3 integrin can bind to recombinant full-length human ADAM12 via beta3 integrin. Furthermore, cell binding to ADAM12 via beta3 integrin results in the formation of focal adhesions, which are not formed upon beta1 integrin-mediated cell attachment. We also show that RhoA is involved in beta3 integrin-mediated focal adhesion formation.",
author = "Thodeti, {Charles Kumar} and Camilla Frohlich and Nielsen, {Christian Kamp} and Yoshikazu Takada and Reinhard F{\"a}ssler and Reidar Albrechtsen and Wewer, {Ulla M}",
note = "Keywords: ADAM Proteins; Antigens, CD29; Cell Line, Tumor; Focal Adhesions; Humans; Integrin beta3; Membrane Proteins; Recombinant Proteins; Up-Regulation; rhoA GTP-Binding Protein",
year = "2005",
doi = "10.1016/j.febslet.2005.09.024",
language = "English",
volume = "579",
pages = "5589--95",
journal = "F E B S Letters",
issn = "0014-5793",
publisher = "JohnWiley & Sons Ltd",
number = "25",

}

RIS

TY - JOUR

T1 - ADAM12-mediated focal adhesion formation is differently regulated by beta1 and beta3 integrins.

AU - Thodeti, Charles Kumar

AU - Frohlich, Camilla

AU - Nielsen, Christian Kamp

AU - Takada, Yoshikazu

AU - Fässler, Reinhard

AU - Albrechtsen, Reidar

AU - Wewer, Ulla M

N1 - Keywords: ADAM Proteins; Antigens, CD29; Cell Line, Tumor; Focal Adhesions; Humans; Integrin beta3; Membrane Proteins; Recombinant Proteins; Up-Regulation; rhoA GTP-Binding Protein

PY - 2005

Y1 - 2005

N2 - ADAM12, adisintegrin 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 beta1 integrins and may affect tumor and stromal cell behavior through its binding to beta1 integrins. Here, we report that cells deficient in beta1 integrin or overexpressing beta3 integrin can bind to recombinant full-length human ADAM12 via beta3 integrin. Furthermore, cell binding to ADAM12 via beta3 integrin results in the formation of focal adhesions, which are not formed upon beta1 integrin-mediated cell attachment. We also show that RhoA is involved in beta3 integrin-mediated focal adhesion formation.

AB - ADAM12, adisintegrin 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 beta1 integrins and may affect tumor and stromal cell behavior through its binding to beta1 integrins. Here, we report that cells deficient in beta1 integrin or overexpressing beta3 integrin can bind to recombinant full-length human ADAM12 via beta3 integrin. Furthermore, cell binding to ADAM12 via beta3 integrin results in the formation of focal adhesions, which are not formed upon beta1 integrin-mediated cell attachment. We also show that RhoA is involved in beta3 integrin-mediated focal adhesion formation.

U2 - 10.1016/j.febslet.2005.09.024

DO - 10.1016/j.febslet.2005.09.024

M3 - Journal article

C2 - 16213489

VL - 579

SP - 5589

EP - 5595

JO - F E B S Letters

JF - F E B S Letters

SN - 0014-5793

IS - 25

ER -

ID: 5185949