MT1-MMP evaluation in neointimal hyperplasia in the late follow-up after prosthesis implantation.
Aorta
/ surgery
Arterial Occlusive Diseases
/ surgery
Blood Vessel Prosthesis Implantation
/ adverse effects
Femoral Artery
/ enzymology
Graft Occlusion, Vascular
/ enzymology
Humans
Hyperplasia
/ enzymology
Iliac Artery
/ surgery
Leg
/ blood supply
Matrix Metalloproteinase 14
/ metabolism
Matrix Metalloproteinase 2
/ metabolism
Neointima
/ enzymology
Reoperation
Tissue Inhibitor of Metalloproteinase-2
/ metabolism
extracellular matrix
matrix metalloproteinases
neointimal hyperplasia
vascular anastomoses
Journal
International journal of experimental pathology
ISSN: 1365-2613
Titre abrégé: Int J Exp Pathol
Pays: England
ID NLM: 9014042
Informations de publication
Date de publication:
04 2019
04 2019
Historique:
received:
21
11
2017
revised:
30
01
2019
accepted:
06
02
2019
pubmed:
7
5
2019
medline:
14
8
2019
entrez:
7
5
2019
Statut:
ppublish
Résumé
Vascular surgical interventions are often burdened with late complications, including thrombosis or restenosis. The latter is generally caused by neointimal hyperplasia. Although extracellular matrix (ECM) remodelling is an important part of neointima formation, this process is not clearly understood. The aim of the study was to assess the content and activity of membrane-type 1 matrix metalloproteinase in human neointima in the late stages of its development. Matrix metalloproteinase-2 and tissue inhibitor of matrix metalloproteinase-2 were also evaluated. The research was performed on neointima samples collected during secondary vascular interventions from patients with chronic limb ischaemia who developed vascular occlusion at 6-18 months after aorto/ilio-femoral bypass grafting. The control material consisted of segments of femoral arteries collected from organ donors. Western blot and/or ELISA were used for the determination of MT1-MMP and TIMP-2 expression. The activity of MT1-MMP was measured by fluorometric assay and that of MMP-2 by zymography. We demonstrated significantly increased MT1-MMP protein content in neointima when compared to normal arteries. However, the activity of MT1-MMP was significantly lower in neointima than in control samples. The decreased MT1-MMP activity was concomitant with reduced activity of MMP-2. The TIMP-2 protein levels in neointima and normal arteries were not significantly different. The results of our study suggest that the reduced activity of MT1-MMP and consequently MMP-2 in human neointima may play a role in decreased degradation of ECM components and thus promote neointimal overgrowth.
Identifiants
pubmed: 31058412
doi: 10.1111/iep.12310
pmc: PMC6540695
doi:
Substances chimiques
TIMP2 protein, human
0
Tissue Inhibitor of Metalloproteinase-2
127497-59-0
MMP2 protein, human
EC 3.4.24.24
Matrix Metalloproteinase 2
EC 3.4.24.24
MMP14 protein, human
EC 3.4.24.80
Matrix Metalloproteinase 14
EC 3.4.24.80
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Pagination
94-101Informations de copyright
© 2019 The Authors. International Journal of Experimental Pathology © 2019 International Journal of Experimental Pathology.
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