Distinct modes of collagen type I proteolysis by matrix metalloproteinase (MMP) 2 and membrane type I MMP during the migration of a tip endothelial cell: Insights from a computational model

Karagiannis, Emmanouil D.; Popel, Aleksander S.

doi:10.1016/j.jtbi.2005.05.020

Cited by 61 publications

(79 citation statements)

References 53 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Invasion of endothelial cells into the ECM during capillary sprouting is mediated by different pericellular proteases, including MMPs (Ghajar et al 2008), ADAMs, and cathepsins (Cavallo-Medved et al 2009). MT1-MMP has been identified as the one of the most potent fibrinolytic and collagenolytic endothelial cell-derived MMPs during capillary sprouting (Hiraoka et al 1998;Karagiannis and Popel 2006), and its expression is largely confined to the sprouting tips of neocapillary structures through interaction of endothelial cells with vascular smooth muscle cells (Yana et al 2007). Proteolytic processing of ECM components leads to the exposure of ''matricryptic'' sites (Davis et al 2000) such as the RGD motif, which is present in collagens, vitronectin, and osteopontin (Ruoslahti 1996).…”

Section: Angiogenesismentioning

confidence: 99%

Pericellular proteolysis in cancer

2014

View full text Add to dashboard Cite

Pericellular proteases have long been associated with cancer invasion and metastasis due to their ability to degrade extracellular matrix components. Recent studies demonstrate that proteases also modulate tumor progression and metastasis through highly regulated and complex processes involving cleavage, processing, or shedding of cell adhesion molecules, growth factors, cytokines, and kinases. In this review, we address how cancer cells, together with their surrounding microenvironment, regulate pericellular proteolysis. We dissect the multitude of mechanisms by which pericellular proteases contribute to cancer progression and discuss how this knowledge can be integrated into therapeutic opportunities.

show abstract

Section: Angiogenesismentioning

confidence: 99%

Pericellular proteolysis in cancer

2014

View full text Add to dashboard Cite

show abstract

“…19 It should be noted, however, that MMPs are also involved in the proteolytic degradation of IGFBP3, which releases IGF-I from the IGF-I-IGFBP3 complex (Fig. 3) to stimulate IGF-I-mediated proliferation.…”

Section: Role Of Neural Stem Cellsmentioning

confidence: 99%

Growth factors, stem cells, and stroke

Kalluri

Dempsey

2008

FOC

View full text Add to dashboard Cite

✓ Postischemic neurogenesis has been identified as a compensatory mechanism to repair the damaged brain after stroke. Several factors are released by the ischemic tissue that are responsible for proliferation, differentiation, and migration of neural stem cells. An understanding of their roles may allow future therapies based on treatment with such factors. Although damaged cells release a variety of factors, some of them are stimulatory whereas some are inhibitory for neurogenesis. It is interesting to note that factors like insulin-like growth factor–I can induce proliferation in the presence of fibroblast growth factor–2 (FGF-2), and promote differentiation in the absence of FGF-2. Meanwhile, factors like transforming growth factor–β can induce the differentiation of neurons while inhibiting the proliferation of neural stem cells. Therefore, understanding the role of each factor in the process of neurogenesis will help physicians to enhance the endogenous response and improve the clinical outcome after stroke. In this article the authors discuss the role of growth factors and stem cells following stroke.

show abstract

“…Matrix metalloproteinases (MMPs) are a family of enzymes responsible for the proteolytic processing of extracellular matrix structural proteins, which regulate endothelial cell migration (Karagiannis and Popel, 2005;Segarra et al, 2005). Activated endothelial cells secrete MMP2 and MMP9 during angiogenesis (Arkell and Jackson, 2003).…”

Section: Introductionmentioning

confidence: 99%

Matrix Metalloproteinase 2 (MMP2) and MMP9 Secreted by Erythropoietin-Activated Endothelial Cells Promote Neural Progenitor Cell Migration

Zhang²,

et al. 2006

View full text Add to dashboard Cite

We investigated the hypothesis that endothelial cells activated by erythropoietin (EPO) promote the migration of neuroblasts. This hypothesis is based on observations in vivo that treatment of focal cerebral ischemia with EPO enhances the migration of neuroblasts to the ischemic boundary, a site containing activated endothelial cells and angiogenic microvasculature. To model the microenvironment within the ischemic boundary zone, we used a coculture system of mouse brain endothelial cells (

show abstract

Distinct modes of collagen type I proteolysis by matrix metalloproteinase (MMP) 2 and membrane type I MMP during the migration of a tip endothelial cell: Insights from a computational model

Cited by 61 publications

References 53 publications

Pericellular proteolysis in cancer

Pericellular proteolysis in cancer

Growth factors, stem cells, and stroke

Matrix Metalloproteinase 2 (MMP2) and MMP9 Secreted by Erythropoietin-Activated Endothelial Cells Promote Neural Progenitor Cell Migration

Contact Info

Product

Resources

About