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Aortic aneurysms, chronic kidney disease and metalloproteinases

Authors :
Giuseppe Filiberto Serraino
Pasquale Mastroroberto
Teresa Faga
Ashour Michael
Gemma Patella
Umberto Bracale
Michele Andreucci
Nicola Ielapi
Raffaele Serra
Michele Provenzano
Andreucci, M.
Provenzano, M.
Faga, T.
Michael, A.
Patella, G.
Mastroroberto, P.
Serraino, G. F.
Bracale, U. M.
Ielapi, N.
Serra, R.
Source :
Biomolecules, Vol 11, Iss 194, p 194 (2021), Biomolecules
Publication Year :
2021

Abstract

Metalloproteinases (MPs) are proteolytic enzymes involved in extracellular matrix deposition, regulation of cellular signals of inflammation, proliferation, and apoptosis. Metalloproteinases are classified into three families: Matrix-MPs (MMPs), A-Disintegrin-and-Metalloprotease (ADAMs), and the A-Disintegrin-and-Metalloproteinase-with-Thrombospondin-1-like-Domains (ADAMTS). Previous studies showed that MPs are involved in the development of aortic aneurysms (AA) and, concomitantly, in the onset of chronic kidney disease (CKD). CKD has been, per se, associated with an increased risk for AA. The aim of this review is to examine the pathways that may associate MPs with CKD and AA. Several MMPs, such as MMP-2, -8, -9, and TIMP-1 have been shown to damage the AA wall and to have a toxic effect on renal tubular cells, leading to fibrosis. Similarly, ADAM10 and 17 have been shown to degrade collagen in the AA wall and to worsen kidney function via pro-inflammatory stimuli, the impairment of the Renin-Angiotensin-Aldosterone System, and the degradation of structural proteins. Moreover, MMP-2 and -9 inhibitors reduced aneurysm growth and albuminuria in experimental and human studies. It would be important, in the future, to expand research on MPs from both a prognostic, namely, to refine risk stratification in CKD patients, and a predictive perspective, likely to improve prognosis in response to targeted treatments.

Details

Language :
English
Database :
OpenAIRE
Journal :
Biomolecules, Vol 11, Iss 194, p 194 (2021), Biomolecules
Accession number :
edsair.doi.dedup.....25e2a01fb4f7beaa290ea2ff751c4bcd