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Src protein kinase pp60c-src influences adhesion stabilization of HT-29 colon carcinoma cells to extracellular matrix components under dynamic conditions of laminar flow

Standard

Src protein kinase pp60c-src influences adhesion stabilization of HT-29 colon carcinoma cells to extracellular matrix components under dynamic conditions of laminar flow. / Haier, Jörg; Gallick, Garry E; Nicolson, Garth L.

in: THER ADV MED ONCOL, Jahrgang 2, Nr. 4, 06.11.2002, S. 237-45.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Haier, J, Gallick, GE & Nicolson, GL 2002, 'Src protein kinase pp60c-src influences adhesion stabilization of HT-29 colon carcinoma cells to extracellular matrix components under dynamic conditions of laminar flow', THER ADV MED ONCOL, Jg. 2, Nr. 4, S. 237-45.

APA

Haier, J., Gallick, G. E., & Nicolson, G. L. (2002). Src protein kinase pp60c-src influences adhesion stabilization of HT-29 colon carcinoma cells to extracellular matrix components under dynamic conditions of laminar flow. THER ADV MED ONCOL, 2(4), 237-45.

Vancouver

Haier J, Gallick GE, Nicolson GL. Src protein kinase pp60c-src influences adhesion stabilization of HT-29 colon carcinoma cells to extracellular matrix components under dynamic conditions of laminar flow. THER ADV MED ONCOL. 2002 Nov 6;2(4):237-45.

Bibtex

@article{cb2fb23badd34238ab5bedba7d597f8f,
title = "Src protein kinase pp60c-src influences adhesion stabilization of HT-29 colon carcinoma cells to extracellular matrix components under dynamic conditions of laminar flow",
abstract = "Tumor cell adhesion to extracellular matrix (ECM) and its stabilization are important determinants in metastasis formation, and they are mediated, in part, by integrins and regulated by a variety of protein kinases. Protein tyrosine kinase pp60c-src is found in adhesion-dependent focal adhesion plaques where it may regulate different integrin-mediated signaling cascades. Using human HT-29 colon carcinoma cells stably transfected with pp60c-src--specific antisense oligonucleotides (HT-29AS15), we investigated the role of pp60c-src in integrin-mediated adhesion and its stabilization to ECM components collagen I or IV under static and laminar fluid flow conditions. Under static adhesion conditions transfection of pp60c-src antisense oligonucleotides did not modify adhesive properties. Phosphorylation of focal adhesion kinase (FAK) and paxillin induced by static adhesion to collagen I or IV were similar in HT-29P and HT-29AS15 cells. However, using hydrodynamic conditions in a laminar flow chamber we found a slight reduction in early adhesion events and an even greater difference in adhesion stabilization rates (ASRs). The transfected cells showed a significant reduction in their ability to withstand shear forces and stabilize adhesive bounds. These changes correlated with the cellular expression levels of pp60c-src. Our results suggest that pp60c-src may be involved in stabilization of dynamic HT-29 cell adhesion to ECM components, and this kinase appears to be part of a mechanosensory protein complex during integrin-mediated cell adhesion.",
keywords = "Cell Adhesion, Collagen, Colorectal Neoplasms, Cytoskeletal Proteins, Extracellular Matrix, Focal Adhesion Kinase 1, Focal Adhesion Protein-Tyrosine Kinases, HT29 Cells, Humans, Paxillin, Phosphoproteins, Phosphorylation, Protein-Tyrosine Kinases, Proto-Oncogene Proteins pp60(c-src), Stress, Mechanical, Tumor Cells, Cultured",
author = "J{\"o}rg Haier and Gallick, {Garry E} and Nicolson, {Garth L}",
year = "2002",
month = nov,
day = "6",
language = "English",
volume = "2",
pages = "237--45",
journal = "THER ADV MED ONCOL",
issn = "1758-8340",
publisher = "Old City Publishing",
number = "4",

}

RIS

TY - JOUR

T1 - Src protein kinase pp60c-src influences adhesion stabilization of HT-29 colon carcinoma cells to extracellular matrix components under dynamic conditions of laminar flow

AU - Haier, Jörg

AU - Gallick, Garry E

AU - Nicolson, Garth L

PY - 2002/11/6

Y1 - 2002/11/6

N2 - Tumor cell adhesion to extracellular matrix (ECM) and its stabilization are important determinants in metastasis formation, and they are mediated, in part, by integrins and regulated by a variety of protein kinases. Protein tyrosine kinase pp60c-src is found in adhesion-dependent focal adhesion plaques where it may regulate different integrin-mediated signaling cascades. Using human HT-29 colon carcinoma cells stably transfected with pp60c-src--specific antisense oligonucleotides (HT-29AS15), we investigated the role of pp60c-src in integrin-mediated adhesion and its stabilization to ECM components collagen I or IV under static and laminar fluid flow conditions. Under static adhesion conditions transfection of pp60c-src antisense oligonucleotides did not modify adhesive properties. Phosphorylation of focal adhesion kinase (FAK) and paxillin induced by static adhesion to collagen I or IV were similar in HT-29P and HT-29AS15 cells. However, using hydrodynamic conditions in a laminar flow chamber we found a slight reduction in early adhesion events and an even greater difference in adhesion stabilization rates (ASRs). The transfected cells showed a significant reduction in their ability to withstand shear forces and stabilize adhesive bounds. These changes correlated with the cellular expression levels of pp60c-src. Our results suggest that pp60c-src may be involved in stabilization of dynamic HT-29 cell adhesion to ECM components, and this kinase appears to be part of a mechanosensory protein complex during integrin-mediated cell adhesion.

AB - Tumor cell adhesion to extracellular matrix (ECM) and its stabilization are important determinants in metastasis formation, and they are mediated, in part, by integrins and regulated by a variety of protein kinases. Protein tyrosine kinase pp60c-src is found in adhesion-dependent focal adhesion plaques where it may regulate different integrin-mediated signaling cascades. Using human HT-29 colon carcinoma cells stably transfected with pp60c-src--specific antisense oligonucleotides (HT-29AS15), we investigated the role of pp60c-src in integrin-mediated adhesion and its stabilization to ECM components collagen I or IV under static and laminar fluid flow conditions. Under static adhesion conditions transfection of pp60c-src antisense oligonucleotides did not modify adhesive properties. Phosphorylation of focal adhesion kinase (FAK) and paxillin induced by static adhesion to collagen I or IV were similar in HT-29P and HT-29AS15 cells. However, using hydrodynamic conditions in a laminar flow chamber we found a slight reduction in early adhesion events and an even greater difference in adhesion stabilization rates (ASRs). The transfected cells showed a significant reduction in their ability to withstand shear forces and stabilize adhesive bounds. These changes correlated with the cellular expression levels of pp60c-src. Our results suggest that pp60c-src may be involved in stabilization of dynamic HT-29 cell adhesion to ECM components, and this kinase appears to be part of a mechanosensory protein complex during integrin-mediated cell adhesion.

KW - Cell Adhesion

KW - Collagen

KW - Colorectal Neoplasms

KW - Cytoskeletal Proteins

KW - Extracellular Matrix

KW - Focal Adhesion Kinase 1

KW - Focal Adhesion Protein-Tyrosine Kinases

KW - HT29 Cells

KW - Humans

KW - Paxillin

KW - Phosphoproteins

KW - Phosphorylation

KW - Protein-Tyrosine Kinases

KW - Proto-Oncogene Proteins pp60(c-src)

KW - Stress, Mechanical

KW - Tumor Cells, Cultured

M3 - SCORING: Journal article

C2 - 12416028

VL - 2

SP - 237

EP - 245

JO - THER ADV MED ONCOL

JF - THER ADV MED ONCOL

SN - 1758-8340

IS - 4

ER -