Cell adhesion ability of artificial extracellular matrix proteins containing a long repetitive Arg-Gly-Asp sequence

2005 ◽  
Vol 100 (1) ◽  
pp. 82-87 ◽  
Author(s):  
Hiroyuki Kurihara ◽  
Teruyuki Nagamune
Keyword(s):  
Extracellular Matrix ◽  
Cell Adhesion ◽  
Extracellular Matrix Proteins ◽  
Matrix Proteins ◽  
Adhesion Ability ◽  
Artificial Extracellular Matrix

scholarly journals Human acute myeloid leukemia cells bind to bone marrow stroma via a combination of beta-1 and beta-2 integrin mechanisms

Blood ◽  
1993 ◽  
Vol 82 (10) ◽  
pp. 3125-3132 ◽  
Author(s):  
LJ Bendall ◽  
K Kortlepel ◽  
DJ Gottlieb
Keyword(s):  
Bone Marrow ◽  
Extracellular Matrix ◽  
Acute Myeloid Leukemia ◽  
Cell Adhesion ◽  
Myeloid Leukemia ◽  
Extracellular Matrix Proteins ◽  
Matrix Proteins ◽  
Leukemic Cells ◽  
Beta 2 ◽  
Acute Myeloid

Abstract Acute myeloid leukemia (AML) cells respond to exogenous stimulation from myeloid growth factors that may be secreted by cells of the bone marrow (BM) stroma and retained by glycosaminoglycans in the extracellular matrix. We have analyzed the capacity of malignant cells from patients with AML to maintain close proximity to sites of growth factor production and retention by binding to BM stromal elements, including fibroblasts and extracellular matrix proteins. Leukemic cells from all cases of AML adhered to BM fibroblast (BMF) monolayers (mean +/- standard error [SE] percentage binding, 30.9% +/- 2.5%; n = 23) and to fibronectin and laminin (mean +/- SE percentage binding, 28.0% +/- 4.1% [n = 11] and 21.5% +/- 2.3% [n = 8], respectively). Binding to bovine and human collagen type 1, vitronectin, hyaluronic acid, and albumin was minimal. Analysis of binding mechanisms indicated that very late antigen-4 (VLA-4) and VLA-5 were responsible for AML cell binding to fibronectin. Binding to laminin could be inhibited by antibody to the alpha chain of VLA-6. In contrast, AML cell adhesion to BMF monolayers was not impaired by blocking antibodies to either beta 1 or beta 2 integrins used alone, although the combination of anti-CD11/CD18 and anti-VLA-4 inhibited binding in more than 50% of cases. When anti- VLA-5 was added in these cases, mean +/- SE inhibition of binding of 45.5% +/- 9.1% (P < .001) was observed. Binding of AML cells to extracellular matrix proteins fibronectin and laminin is predominantly beta 1-integrin-dependent, but AML cell adhesion to BMF relies on the simultaneous involvement of beta 1 and beta 2 integrins as well as other currently unrecognized ligands.

scholarly journals Actin cytoskeleton polymerization in Dbl-transformed NIH3T3 fibroblasts is dependent on cell adhesion to specific extracellular matrix proteins

Oncogene ◽  
1997 ◽  
Vol 14 (16) ◽  
pp. 1933-1943 ◽  
Author(s):  
Paola Defilippi ◽  
Cristina Olivo ◽  
Guido Tarone ◽  
Patrizia Mancini ◽  
Maria Rosaria Torrisi ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Cell Adhesion ◽  
Actin Cytoskeleton ◽  
Extracellular Matrix Proteins ◽  
Matrix Proteins

scholarly journals ELMO1 increases expression of extracellular matrix proteins and inhibits cell adhesion to ECMs

2006 ◽  
Vol 70 (10) ◽  
pp. 1769-1776 ◽  
Author(s):  
A. Shimazaki ◽  
Y. Tanaka ◽  
T. Shinosaki ◽  
M. Ikeda ◽  
H. Watada ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Cell Adhesion ◽  
Extracellular Matrix Proteins ◽  
Matrix Proteins

Modulating Cell Adhesion Dynamics on Carbon Nanotube Monolayer Engineered with Extracellular Matrix Proteins

2010 ◽  
Vol 2 (4) ◽  
pp. 1038-1047 ◽  
Author(s):  
Ning Cai ◽  
Chee C. Wong ◽  
Ying X. Gong ◽  
Samuel C. W. Tan ◽  
Vincent Chan ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Cell Adhesion ◽  
Carbon Nanotube ◽  
Extracellular Matrix Proteins ◽  
Matrix Proteins
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