Differente Integrin-vermittelte Adhäsion von hoch hepatisch metastasierenden und gering metastasierenden Kolon-Karzinom-Zellen an extrazellulärer Matrix

Standard

Differente Integrin-vermittelte Adhäsion von hoch hepatisch metastasierenden und gering metastasierenden Kolon-Karzinom-Zellen an extrazellulärer Matrix. / Haier, J; Nasralla, M; Buhr, H J; Nicolson, G L.

In: Langenbecks Arch Chir Suppl Kongressbd, Vol. 115, No. Suppl I, 1998, p. 307-13.

Research output: SCORING: Contribution to journalSCORING: Journal articleResearchpeer-review

Harvard

Haier, J, Nasralla, M, Buhr, HJ & Nicolson, GL 1998, 'Differente Integrin-vermittelte Adhäsion von hoch hepatisch metastasierenden und gering metastasierenden Kolon-Karzinom-Zellen an extrazellulärer Matrix', Langenbecks Arch Chir Suppl Kongressbd, vol. 115, no. Suppl I, pp. 307-13.

APA

Haier, J., Nasralla, M., Buhr, H. J., & Nicolson, G. L. (1998). Differente Integrin-vermittelte Adhäsion von hoch hepatisch metastasierenden und gering metastasierenden Kolon-Karzinom-Zellen an extrazellulärer Matrix. Langenbecks Arch Chir Suppl Kongressbd, 115(Suppl I), 307-13.

Vancouver

Haier J, Nasralla M, Buhr HJ, Nicolson GL. Differente Integrin-vermittelte Adhäsion von hoch hepatisch metastasierenden und gering metastasierenden Kolon-Karzinom-Zellen an extrazellulärer Matrix. Langenbecks Arch Chir Suppl Kongressbd. 1998;115(Suppl I):307-13.

Bibtex

@article{9fb251f543c549f3987dc53a1394b8fd,
title = "Differente Integrin-vermittelte Adh{\"a}sion von hoch hepatisch metastasierenden und gering metastasierenden Kolon-Karzinom-Zellen an extrazellul{\"a}rer Matrix",
abstract = "Poorly and highly liver metastatic colon carcinoma cell lines have different integrin-mediated adhesion to extracellular matrix. Specific integrin-mediated interactions between tumor cells and extracellular matrix (ECM) in the host organs are important for organ-specific metastasis. In colon carcinoma integrin expression differs depending on the metastatic potential of the tumor. Integrin-mediated adhesion of poorly (HT-29P) and highly liver-metastatic (HT-29LMM) colon carcinoma to extracellular matrix (ECM; Collagen I-C I, Collagen IV-C IV, Laminin LN, Fibronectin FN, Vitronectin VN) was investigated. HT-29LMM showed significant better adhesion to LN (45% vs. 26%; p < 0.001) and FN 20% vs. 1%; p < 0.001). No adhesion was found to VN. RGD-oligopeptides completely inhibited adhesion to FN. Using inhibition with anti-integrin-mAB it was shown, that adhesion to C I and C IV is mediated by alpha 2 beta 1-integrin, adhesion to LN by alpha 6 beta 1 and adhesion to FN by alpha v beta 1. These results have shown that adhesion of HT-29 cells is mediated by different integrins depending on ECM components. Poorly and highly metastatic cells possessed different patterns of adhesion to various substrates.",
keywords = "Cell Adhesion, Colonic Neoplasms, Extracellular Matrix, Gene Expression Regulation, Neoplastic, Humans, Integrins, Liver, Liver Neoplasms, Prognosis, Tumor Cells, Cultured",
author = "J Haier and M Nasralla and Buhr, {H J} and Nicolson, {G L}",
year = "1998",
language = "Deutsch",
volume = "115",
pages = "307--13",
number = "Suppl I",

}

RIS

TY - JOUR

T1 - Differente Integrin-vermittelte Adhäsion von hoch hepatisch metastasierenden und gering metastasierenden Kolon-Karzinom-Zellen an extrazellulärer Matrix

AU - Haier, J

AU - Nasralla, M

AU - Buhr, H J

AU - Nicolson, G L

PY - 1998

Y1 - 1998

N2 - Poorly and highly liver metastatic colon carcinoma cell lines have different integrin-mediated adhesion to extracellular matrix. Specific integrin-mediated interactions between tumor cells and extracellular matrix (ECM) in the host organs are important for organ-specific metastasis. In colon carcinoma integrin expression differs depending on the metastatic potential of the tumor. Integrin-mediated adhesion of poorly (HT-29P) and highly liver-metastatic (HT-29LMM) colon carcinoma to extracellular matrix (ECM; Collagen I-C I, Collagen IV-C IV, Laminin LN, Fibronectin FN, Vitronectin VN) was investigated. HT-29LMM showed significant better adhesion to LN (45% vs. 26%; p < 0.001) and FN 20% vs. 1%; p < 0.001). No adhesion was found to VN. RGD-oligopeptides completely inhibited adhesion to FN. Using inhibition with anti-integrin-mAB it was shown, that adhesion to C I and C IV is mediated by alpha 2 beta 1-integrin, adhesion to LN by alpha 6 beta 1 and adhesion to FN by alpha v beta 1. These results have shown that adhesion of HT-29 cells is mediated by different integrins depending on ECM components. Poorly and highly metastatic cells possessed different patterns of adhesion to various substrates.

AB - Poorly and highly liver metastatic colon carcinoma cell lines have different integrin-mediated adhesion to extracellular matrix. Specific integrin-mediated interactions between tumor cells and extracellular matrix (ECM) in the host organs are important for organ-specific metastasis. In colon carcinoma integrin expression differs depending on the metastatic potential of the tumor. Integrin-mediated adhesion of poorly (HT-29P) and highly liver-metastatic (HT-29LMM) colon carcinoma to extracellular matrix (ECM; Collagen I-C I, Collagen IV-C IV, Laminin LN, Fibronectin FN, Vitronectin VN) was investigated. HT-29LMM showed significant better adhesion to LN (45% vs. 26%; p < 0.001) and FN 20% vs. 1%; p < 0.001). No adhesion was found to VN. RGD-oligopeptides completely inhibited adhesion to FN. Using inhibition with anti-integrin-mAB it was shown, that adhesion to C I and C IV is mediated by alpha 2 beta 1-integrin, adhesion to LN by alpha 6 beta 1 and adhesion to FN by alpha v beta 1. These results have shown that adhesion of HT-29 cells is mediated by different integrins depending on ECM components. Poorly and highly metastatic cells possessed different patterns of adhesion to various substrates.

KW - Cell Adhesion

KW - Colonic Neoplasms

KW - Extracellular Matrix

KW - Gene Expression Regulation, Neoplastic

KW - Humans

KW - Integrins

KW - Liver

KW - Liver Neoplasms

KW - Prognosis

KW - Tumor Cells, Cultured

M3 - SCORING: Zeitschriftenaufsatz

C2 - 14518266

VL - 115

SP - 307

EP - 313

IS - Suppl I

ER -