Matrix Metalloproteinases -14, -9 and -2 are Localized to the Podosome and Involved in Podosome Development in the A7r5 Smooth Muscle Cell
Journal Title: Journal of Cardiobiology - Year 2017, Vol 5, Issue 1
Abstract
Aim: The purpose of the study was to localize matrix metalloproteinase (MMP)-14, -9, and -2 in the A7r5 smooth musclecell nd to understand the interaction between these MMPs and the cytoskeleton. This interaction was observed under non- timulating and phorbol 12, 13-dibutyrate (PDBu)-stimulating conditions. Methods: Confocal microscopy was utilized to define he localizations of MMPs and tissue inhibitor of matrix metalloproteinases(TIMPs) in the A7r5 cell and to determine nteraction between MMPs and the cytoskeleton. Under PDBu-stimulating conditions, the presence of MMP active forms and ctivity by gel zymography was evaluated in the A7r5 cell. Actin and microtubule-polymerization inhibitors were used to valuate MMP interaction with the cytoskeleton and the cytoskeleton was observed on matrix and within a Type I collagen el. Results: MMP-14, -9, and -2 were localized to the podosome in the A7r5 smooth muscle cell and interactions were seen with hese MMPs and the actin cytoskeleton. PDBu-stimulation induced increases in the protein abundance of the active forms of he MMPs and MMP- 2 activity was increased. MMPs also interact with α-actin and not β-tubulin in the A7r5 cell. Galardin, also nown as GM-6001, was shown to inhibit podosome formation and prevented MMP localization to the podosome. This broad pectrum MMP inhibitor also prevented collagen gel contraction and prevented cell adhesion and spreading of A7r5 cells ithin this collagen matrix. Conclusion: MMPs are important in the formation and function of podosomes in the A7r5 smooth uscle cell. MMPs interact with α-actin and not β-tubulin in the A7r5 cell. Podosomes play an important role in cell migration nd understanding the function of podosomes can lead to insights into cancer metastasis and cardiovascular disease.
Authors and Affiliations
Sean Thatcher
Keywords
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- EP ID EP240026
- DOI 10.13188/2332-3671.1000020
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