Enhenced cell adhesion on collagen I treated parylene-C microplates

2021 ◽  
pp. 1-12
Author(s):  
Lijun Zhao ◽  
Weiwei Lan ◽  
Xiao Dong ◽  
Han Xu ◽  
Lili Wang ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Collagen I ◽  
Parylene C

Regulatory effects of stem cell factor and interleukin-4 on adhesion of human mast cells to extracellular matrix proteins

Blood ◽  
2002 ◽  
Vol 99 (3) ◽  
pp. 966-972 ◽  
Author(s):  
Axel Lorentz ◽  
Detlef Schuppan ◽  
Andreas Gebert ◽  
Michael P. Manns ◽  
Stephan C. Bischoff
Keyword(s):  
Extracellular Matrix ◽  
Mast Cell ◽  
Stem Cell ◽  
Cell Adhesion ◽  
Mast Cells ◽  
Stem Cell Factor ◽  
Collagen I ◽  
Interleukin 4 ◽  
Human Mast Cells ◽  
Ecm Proteins

Abstract Mast cells are inflammatory and immunoregulatory cells resident in tissues. They develop from bone marrow-derived progenitor cells that enter the tissue through the blood circulation. The specific localization and migration of mast cells in tissues is dependent on their interaction with extracellular matrix (ECM) proteins. Adhesion of human mast cells isolated from intestinal mucosa and cultured in the presence of stem cell factor (SCF) to ECM proteins is analyzed. It was observed that SCF is a unique cytokine enhancing mast cell adhesion to all tested ECM proteins (fibronectin, laminin, collagen I, III, IV, VI, XIV) up to 5-fold, particularly to fibronectin (54% ± 12% of mast cells) and to denatured collagens (40% ± 12% on cyanogen bromide-cleaved peptides of collagen I). Most noteworthy, preculture of mast cells with interleukin-4 (IL-4), in addition to SCF, reduced their potency to adhere to ECM proteins to one third compared to mast cells cultured with SCF alone. Mast cell adhesion was preferentially mediated by β1 integrins, and most cells expressed the ECM-binding integrins α2β1, α3β1, α4β1, α5β1, and αVβ3. SCF-induced mast cell adhesion was totally blocked by wortmannin and apigenin, indicating an involvement of phosphatidylinositol 3-kinase and mitogen-activated protein kinase, and it was related to an up-regulation of the HUTS-21 β1 epitope, which is associated with an activated conformation of β1. In conclusion, these data indicate that SCF induces the adhesion of cultured mast cells to ECM proteins, whereas IL-4 may promote detachment from the ECM.

scholarly journals Inhibition of platelets and tumor cell adhesion by the disintegrin domain of human ADAM9 to collagen I under dynamic flow conditions

Biochimie ◽  
2009 ◽  
Vol 91 (8) ◽  
pp. 1045-1052 ◽  
Author(s):  
Marcia R. Cominetti ◽  
Ana Carolina B.M. Martin ◽  
Juliana U. Ribeiro ◽  
Ibtissem Djaafri ◽  
Françoise Fauvel-Lafève ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Tumor Cell ◽  
Collagen I ◽  
Flow Conditions ◽  
Dynamic Flow ◽  
Tumor Cell Adhesion ◽  
Disintegrin Domain

scholarly journals CXCL12 Modulates Prostate Cancer Cell Adhesion by Altering the Levels or Activities ofβ1-Containing Integrins

2014 ◽  
Vol 2014 ◽  
pp. 1-11 ◽  
Author(s):  
Mehdi Dehghani ◽  
Sedigheh Kianpour ◽  
Ana Zangeneh ◽  
Zohreh Mostafavi-Pour
Keyword(s):  
Prostate Cancer ◽  
Cell Adhesion ◽  
Collagen I ◽  
Integrin Receptors ◽  
High Concentration ◽  
Kinase Activation ◽  
Potential Biomarker ◽  
Cell Adhesion And Migration ◽  
And Migration ◽  
Recombinant Fragments

The mechanisms by which prostate cancer (PCa) cell adhesion and migration are controlled during metastasis are not well understood. Here, we studied the effect of CXCL12 in PCa cell adhesion and spreading in DU145 and PC3 cell lines using as substrates collagen I, fibronectin (FN), and their recombinant fragments. CXCL12 treatment increasedβ1 integrin-dependent PC3 cell adhesion on FN which correlated with increased focal adhesion kinase activation. However neitherα5β1 norα4β1 subunits were involved in this adhesion. By contrast, CXCL12 decreased DU145 adhesion and spreading on FN by downregulatingα5 andβ1 integrin expression. To demonstrate the clinical relevance of CXCL12 in PCa, we measured CXCL12 levels in plasma by using ELISA and found that the chemokine is elevated in PCa patients when compared to controls. The high concentration of CXCL12 in patients suffering from PCa in comparison to those with benign disease or healthy individuals implicates CXCL12 as a potential biomarker for PCa. In addition these data show that CXCL12 may be crucial in controlling PCa cell adhesion on fibronectin and collagen I, possibly via crosstalk with integrin receptors and/or altering the expression levels of integrin subunits.

Collagen I-coated titanium surfaces: Mesenchymal cell adhesion andin vivo evaluation in trabecular bone implants

2006 ◽  
Vol 78A (3) ◽  
pp. 449-458 ◽  
Author(s):  
M. Morra ◽  
C. Cassinelli ◽  
G. Cascardo ◽  
L. Mazzucco ◽  
P. Borzini ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Trabecular Bone ◽  
Mesenchymal Cell ◽  
Collagen I ◽  
Bone Implants ◽  
Titanium Surfaces

scholarly journals The effect of collagen I mimetic peptides on mesenchymal stem cell adhesion and differentiation, and on bone formation at hydroxyapatite surfaces

Biomaterials ◽  
2009 ◽  
Vol 30 (10) ◽  
pp. 1898-1909 ◽  
Author(s):  
Kristin M. Hennessy ◽  
Beth E. Pollot ◽  
William C. Clem ◽  
Matthew C. Phipps ◽  
Amber A. Sawyer ◽  
...  
Keyword(s):  
Stem Cell ◽  
Cell Adhesion ◽  
Mesenchymal Stem Cell ◽  
Bone Formation ◽  
Collagen I ◽  
Mimetic Peptides

The Integrin α2 Dimorphism E534K Modulates Platelet Binding to Decorin but Not Collagen I,

Blood ◽  
2011 ◽  
Vol 118 (21) ◽  
pp. 3256-3256
Author(s):  
Thomas J Kunicki ◽  
Daniel Diaz ◽  
Shirley A Williams ◽  
Richard W. Farndale ◽  
Diane J. Nugent
Keyword(s):  
Cell Adhesion ◽  
Amino Acid ◽  
Binding Site ◽  
Cancer Biology ◽  
Conflicts Of Interest ◽  
Normal Subjects ◽  
Minor Allele ◽  
Collagen I ◽  
Functional Difference ◽  
Major Allele

Abstract Abstract 3256 Background. Integrin a2b1-mediated adhesion to collagens supports cellular attachment, while decorin binding by a2b1 often attenuates adhesion. Collagen I binds to the a2 I-domain via the triple-helical sequence GFOGER, but the decorin binding site is not within the a2 I-domain and has not yet been identified. A single nucleotide polymorphism in the a2 gene ITGA2 (rs1801106) (G1600A) resulting in the amino acid substitution glutamate-534 to lysine-534 (E534K) is the basis for one of the most important human platelet alloantigen (HPA) systems, HPA-5, yet HPA-5 alleles do not influence the binding of a2b1 to collagen I, and the effect of HPA-5 on platelet function, if any, has not been determined. We sought to determine whether the minor allele HPA-5b (534K) might influence the a2b1-mediated adhesion of platelets to a physiologically relevant ligand other than collagen I. One such alternative ligand is decorin, an extracellular matrix small leucine (Leu)-rich proteoglycan (SLRP). Methods/Results. Two groups of normal subjects were compared. The first group (GG) consisted of ten donors homozygous for the major allele rs1801106G. The second group (GA+AA) included one donor homozygous for the minor allele rs1801106A and nine donors heterozygous for these alleles. Aside from this, there were no significant differences between the two groups with respect to platelet count, mean platelet volume, surface expression of four selected platelet receptors, GPIba, GPVI, aIIbb3 or a2b1, or the allelic distribution of five receptor genes, ITGA2B rs5911, ITGB3 rs5918, GP1BA rs6065, GP6 rs1613662 and P2RY1 rs1065776. In direct platelet adhesion assays, we determined that platelets from GG donors bound more strongly to decorin than those from GA+AA donors (p < 0.01), while platelets from either group bound equally well to collagen I (p = 0.73). Using platelets from donors homozygous for the major allele rs1801106G, adhesion to decorin was significantly inhibited by human alloantibodies specific for HPA-5a but not by GFOGER or an a2-specific monoclonal antibody 6F1 known to inhibit cell adhesion to collagen I. Conversely, GFOGER and 6F1 inhibited adhesion to collagen I but not decorin. Conclusions. The simplest explanation of our findings is that 534E, located in the a2 b-propeller domain, is necessary for maximal binding of a2b1 to decorin but not collagen I. These results suggest that 534E contributes to the decorin binding site and that this amino acid represents a potential target for interventions that can modify cell adhesion to decorin and perhaps other proteoglycans. This also represents the first instance of a functional difference attributable to the HPA-5 alleles. These results expand our understanding of the decorin and collagen I interactions described in murine and human studies of cell adhesion and cancer biology, where decorin and collagen I often have opposite effects that are both mediated by a2b1. Decorin knockout (Dcn(−/−)) murine embryonic fibroblasts exhibit greater adhesion to collagen and greater migration on collagen substrates, while decorin attenuates the aggressiveness and metastasis of tumor cells with diverse histologic backgrounds. Further studies of the relationship between the collagen I and decorin binding sites on integrin a2 are warranted, particularly regarding its influence on thrombosis and hemostasis. Disclosures: No relevant conflicts of interest to declare.

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