Cell proliferation and migration on collagen substrata in vitro

1980 ◽  
Vol 41 (1) ◽  
pp. 159-175
Author(s):  
S.L. Schor
Keyword(s):  
Cell Proliferation ◽  
Cell Migration ◽  
Collagen Gel ◽  
Collagen Fibres ◽  
3 Dimensional ◽  
Cell Proliferation And Migration ◽  
Native Collagen ◽  
And Migration ◽  
Collagen Gel Matrix ◽  
Proliferation And Migration

Quantitative data are presented regarding cell proliferation and migration on (a) collagen films (b) the surface of 3-dimensional gels of native collagen fibres and (c) within the 3-dimensional collagen gel matrix, as part of a study of the effects of the extracellular matrix on cell behaviour. The nature of the collagen environment was found to influence the proliferation of certain cell types, but not of others. For example, HeLa cells proliferate at approximately the same rate and reach the same saturation cell densities on all of the collagen substrata, while human skin fibroblasts grow more slowly within the 3-dimensional collagen gel matrix compared with cells either on the gel surface or on collagen films. The 3-dimensional gels of native collagen fibres may also be used to study cell migration on the gel surface, as well as cell migration (or ‘infiltration’) from the gel surface into the 3-dimensional collagen matrix. Two methods have been used to obtain quantitative information concerning cell infiltration into the collagen gel, one involving the selective removal of cells from the gel surface, while the other relies on direct microscopic examination. Of the cells examined to date, epithelial cells (both normal and tumour) do not show infiltrative behaviour, while both normal and virally transformed fibroblasts, as well as tumour cells of non-epithelial origin (e.g. melanoma), do infiltrate into the collagen gel matrix, at rates which vary considerably according to cell type.

Abstract 451: Oxygen Regulation of Human Coronary Artery Smooth Muscle Cell Proliferation and Migration

2015 ◽  
Vol 35 (suppl_1) ◽  
Author(s):  
Mingming Yang ◽  
Tomoko Kamishima ◽  
Caroline Dart ◽  
John M Quayle
Keyword(s):  
Cell Proliferation ◽  
Smooth Muscle ◽  
Cell Migration ◽  
Coronary Artery ◽  
Cell Viability ◽  
Smooth Muscle Cell ◽  
Human Coronary Artery ◽  
Cell Proliferation And Migration ◽  
And Migration ◽  
Proliferation And Migration

Introduction: Intimal thickening of blood vessels, a hallmark of several vascular diseases including atherosclerosis and a potential point of therapeutic intervention, is caused by vascular smooth muscle cell proliferation and migration. It has been suggested that oxygen availability in vessels not only regulates behavior of smooth muscle cells but also serves as a trigger that may lead to pathological responses. In this study we determined whether hypoxia elicits proliferative and migratory responses in Human Coronary Artery SMCs (HCASMCs). Methods: Proliferation of HCASMCs was assessed using a 3-(4,5 dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) assay. SMCs were plated in 96-well plates (n=5), serum starved, and then placed under hypoxic or normoxic conditions for 2, 4 and 6 days (2D/4D/6D) before MTT was added to each well. Absorbance at the wavelength 570 nm was read on an ELISA plate reader, and percent change in cell viability was determined and normalized to control (cell viability under normoxia). Cell migration was characterized by scratch-wound assay. SMCs were seeded in 6 well plates overnight (n=3), then a ‘scratch’ on the cell monolayer was created for each well before putting into different oxygen levels for 4 hours, 12 hours and 24 hours. Images were captured at the beginning and at intervals during cell migration to close the scratch, and the degree of migration was determined by comparing the images. Results: Compared to normoxic condition, cell number changed to 118.1%±1.3% in 5% O 2 (p<0.05) and 98.2%%±1.9% in 1% O 2 after 2D; to 151.9% ±8.5% in 5% O 2 (p<0.001) and 119.4%±5.0% in 1% O 2 (p<0.05) after 4D; and to 163.0%±4.3% in 5% O 2 (p<0.001) and 120.3%±2.2% in 1% O 2 (p<0.05) after 6D. In the cell migration assay, the difference in migration rate between different groups after 4 hours was not obvious, but there was a significant difference after 12 hours (29.3%±1.3% closure in normoxia vs 39.8%±1.9% in 5% O 2 vs 40.9%±3.5% in 1% O 2 , p<0.05) and 24 hours (71.5%±4.4% in normoxia vs 87.2%±2.2% in 5% O 2 vs 87.5%±3.1% in 1% O 2 , p<0.05). Conclusion: Our studies reveal that hypoxia induces both proliferation and migration of HCASMCs.

scholarly journals Metformin Suppressed CXCL8 Expression and Cell Migration in HEK293/TLR4 Cell Line

2017 ◽  
Vol 2017 ◽  
pp. 1-11 ◽  
Author(s):  
Zhihui Xiao ◽  
Wenjun Wu ◽  
Vladimir Poltoratsky
Keyword(s):  
Cell Proliferation ◽  
Cell Migration ◽  
Tumor Cell ◽  
Nuclear Translocation ◽  
High Dose ◽  
Dependent Manner ◽  
Tumor Cell Proliferation ◽  
Cell Proliferation And Migration ◽  
And Migration ◽  
Proliferation And Migration

Chronic inflammation is associated with cancer. CXCL8 promotes tumor microenvironment construction through recruiting leukocytes and endothelial progenitor cells that are involved in angiogenesis. It also enhances tumor cell proliferation and migration. Metformin, type II diabetes medication, demonstrates anticancer properties via suppressing inflammation, tumor cell proliferation, angiogenesis, and metastasis. This study intended to address the role of metformin in regulation of CXCL8 expression and cell proliferation and migration. Our data indicated that metformin suppressed LPS-induced CXCL8 expression in a dose-dependent manner through inhibiting NF-κB, but not AP-1 and C/EBP, activities under the conditions we used. This inhibitory effect of metformin is achieved through dampening LPS-induced NF-κB nuclear translocation. Cell migration was inhibited by metformin under high dose (10 mM), but not cell proliferation.

Requirement of the epidermal growth factor receptor in renal epithelial cell proliferation and migration

2004 ◽  
Vol 287 (3) ◽  
pp. F365-F372 ◽  
Author(s):  
Shougang Zhuang ◽  
Yujing Dang ◽  
Rick G. Schnellmann
Keyword(s):  
Cell Proliferation ◽  
Epidermal Growth Factor Receptor ◽  
Cell Migration ◽  
Growth Factor ◽  
Growth Factor Receptor ◽  
Mechanical Injury ◽  
Cell Proliferation And Migration ◽  
Epidermal Growth ◽  
And Migration ◽  
Proliferation And Migration

We showed that renal proximal tubular cells (RPTC) can proliferate and migrate following plating and oxidant or mechanical injury in the absence of exogenous growth factors; however, the mechanisms of this response remain unclear. We examined whether epidermal growth factor receptor (EGFR) signaling is activated following plating and mechanical injury and mediates RPTC proliferation and migration. EGFR, Akt [a target of phosphoinositide-3-kinase (PI3K)], and ERK1/2 were activated after plating and mechanical injury, and their phosphorylation was further enhanced by addition of exogenous EGF. Inactivation of the EGFR with the selective inhibitor AG-1478 completely blocked phosphorylation of EGFR, Akt, and ERK1/2 and blocked cell proliferation and migration after plating and injury. Inhibition of PI3K with LY-294002 blocked Akt phosphorylation and proliferation, whereas U-0126 blocked ERK1/2 phosphorylation but had no effect on proliferation. Furthermore, p38 was phosphorylated following mechanical injury and the p38 inhibitor SB-203580 blocked p38 phosphorylation and cell migration. In contrast, neither PI3K nor ERK1/2 inhibition blocked cell migration. These results show that EGFR activation is required for RPTC proliferation and migration and that proliferation is mediated by PI3K, whereas migration is mediated by p38.

scholarly journals RAGE Up-Regulation Differently Affects Cell Proliferation and Migration in Pancreatic Cancer Cells

2020 ◽  
Vol 21 (20) ◽  
pp. 7723
Author(s):  
Priyanka Swami ◽  
Swetha Thiyagarajan ◽  
Arianna Vidger ◽  
Venkata S. K. Indurthi ◽  
Stefan W. Vetter ◽  
...  
Keyword(s):  
Pancreatic Cancer ◽  
Cell Proliferation ◽  
Cell Migration ◽  
Cancer Cells ◽  
Human Pancreatic Cancer ◽  
Mesenchymal Transition ◽  
Pancreatic Cancer Cells ◽  
Cell Proliferation And Migration ◽  
And Migration ◽  
Proliferation And Migration

The receptor for advanced glycation end products (RAGE) contributes to many cellular aspects of pancreatic cancer including cell proliferation, migration, and survival. Studies have shown that RAGE activation by its ligands promotes pancreatic tumor growth by stimulating both cell proliferation and migration. In this study, we investigated the effect of RAGE up-regulation on the proliferation and migration of the human pancreatic cancer Panc-1 cell-line. We show that moderate overexpression of RAGE in Panc-1 cells results in increased cell proliferation, but decreased cell migration. The observed cellular changes were confirmed to be RAGE-specific and reversible by using RAGE-specific siRNAs and the small molecule RAGE inhibitor FPS-ZM1. At the molecular level, we show that RAGE up-regulation was associated with decreased activity of FAK, Akt, Erk1/2, and NF-κB signaling pathways and greatly reduced levels of α2 and β1 integrin expression, which is in agreement with the observed decreases in cell migration. We also demonstrate that RAGE up-regulation changes the expression of key molecular markers of epithelial-to-mesenchymal transition (EMT). Our results suggest that in the absence of stimulation by external ligands, RAGE up-regulation can differently modulate cell proliferation and migration in pancreatic cancer cells and regulates partly EMT.

ARFGAP3 an androgen target gene promotes prostate cancer cell proliferation and migration.

2020 ◽  
Author(s):  
Lungwani Muungo
Keyword(s):  
Cell Proliferation ◽  
Cancer Cell ◽  
Cell Biology ◽  
Adaptor Protein ◽  
Cancer Cell Proliferation ◽  
Lncap Cells ◽  
Gtpase Activating Protein ◽  
Cell Proliferation And Migration ◽  
And Migration ◽  
Proliferation And Migration

ADP ribosylation factor GTPase-activating protein 3 (ARFGAP3) is a GTPase-activating protein that associates with the Golgiapparatus and regulates the vesicular trafficking pathway. In the present study, we examined the contribution of ARFGAP3 toprostate cancer cell biology. We showed that ARFGAP3 expression was induced by 100 nM of dihydrotestosterone (DHT) atboth the mRNA and protein levels in androgen-sensitive LNCaP cells. We generated stable transfectants of LNCaP cells withFLAG-tagged ARFGAP3 or a control empty vector and showed that ARFGAP3 overexpression promoted cell proliferation andmigration compared with control cells. We found that ARFGAP3 interacted with paxillin, a focal adhesion adaptor protein thatis important for cell mobility and migration. Small interfering RNA (siRNA)-mediated knockdown of ARFGAP3 showed thatARFGAP3 siRNA markedly reduced LNCaP cell growth. Androgen receptor (AR)-dependent transactivation activity on prostatespecificantigen (PSA) enhancer was synergistically promoted by exogenous ARFGAP3 and paxillin expression, as shown byluciferase assay in LNCaP cells. Thus, our results suggest that ARFGAP3 is a novel androgen-regulated gene that can promoteprostate cancer cell proliferation and migration in collaboration with paxillin.

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