An emerging role of degrading proteinases in hypertension and the metabolic syndrome: Autodigestion and receptor cleavage
Current Hypertension Reports, ISSN: 1522-6417, Vol: 14, Issue: 1, Page: 88-96
2012
- 15Citations
- 18Captures
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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
- Citations15
- Citation Indexes15
- 15
- CrossRef13
- Captures18
- Readers18
- 18
Article Description
One of the major challenges for hypertension research is to identify the mechanisms that cause the comorbidities encountered in many hypertensive patients, as seen in the metabolic syndrome. An emerging body of evidence suggests that human and experimental hypertensives may exhibit uncontrolled activity of proteinases, including the family of matrix metalloproteinases, recognized for their ability to restructure the extracellular matrix proteins and to play a role in hypertrophy. We propose a new hypothesis that provides a molecular framework for the comorbidities of hypertension, diabetes, capillary rarefaction, immune suppression, and other cell and organ dysfunctions due to early and uncontrolled extracellular receptor cleavage by active proteinases. The proteinase and signaling activity in hypertensives requires further detailed analysis of the proteinase expression, the mechanisms causing proenzyme activation, and identification of the proteinase substrate. This work may open the opportunity for reassessment of old interventions and development of new interventions to manage hypertension and its comorbidities. © 2011 Springer Science+Business Media, LLC.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84857635793&origin=inward; http://dx.doi.org/10.1007/s11906-011-0240-9; http://www.ncbi.nlm.nih.gov/pubmed/22081429; http://link.springer.com/10.1007/s11906-011-0240-9; https://dx.doi.org/10.1007/s11906-011-0240-9; https://link.springer.com/article/10.1007/s11906-011-0240-9; http://www.springerlink.com/index/10.1007/s11906-011-0240-9; http://www.springerlink.com/index/pdf/10.1007/s11906-011-0240-9
Springer Science and Business Media LLC
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