The Balance Between Metalloproteinases and TIMPs
Progress in Molecular Biology and Translational Science, ISSN: 1877-1173, Vol: 147, Page: 101-131
2017
- 35Citations
- 51Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations35
- Citation Indexes35
- 35
- CrossRef23
- Captures51
- Readers51
- 43
Article Description
Endothelial cells (EC), especially the microvascular EC (MVEC), have critical functions in health and disease. For example, healthy MVEC provide a barrier between the fluid and protein found within the blood, and the surrounding tissue. Following tissue injury or infection, the microvascular barrier is often disrupted due to activation and dysfunction of the MVEC. Multiple mechanisms promote MVEC activation and dysfunction, including stimulation by cytokines, mechanical interaction with activated leukocytes, and exposure to harmful leukocyte-derived molecules, which collectively result in a loss of MVEC barrier function. However, MVEC activation is also critical to facilitate recruitment of inflammatory cells, such as neutrophils (PMNs) and monocytes, into the injured or infected tissue. Metalloproteinases, including the matrix metalloproteinases (MMPs) and the closely related, a disintegrin and metalloproteinases (ADAMs), have been implicated in regulating both MVEC barrier function, through cleavage of adherens and tight junctions proteins between adjacent MVEC and through degradation of the extracellular matrix, as well as PMN–MVEC interaction, through shedding of cell surface PMN receptors. Moreover, the tissue inhibitors of metalloproteinases (TIMPs), which collectively inhibit most MMPs and ADAMs, are critical regulators of MVEC activation and dysfunction through their ability to inhibit metalloproteinases and thereby promote MVEC stability. However, TIMPs have been also found to modulate MVEC function through metalloproteinase-independent mechanisms, such as regulation of vascular endothelial growth factor signaling. This chapter is focused on examining the role of the metalloproteinases and TIMPs in regulation of MVEC function in both health and disease.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S1877117317300121; http://dx.doi.org/10.1016/bs.pmbts.2017.01.001; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=85016185121&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/28413026; https://linkinghub.elsevier.com/retrieve/pii/S1877117317300121; https://doi.org/10.1016%2Fbs.pmbts.2017.01.001; https://dx.doi.org/10.1016/bs.pmbts.2017.01.001
Elsevier BV
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