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Vascular Surgery 2019
Journal of Vascular and Endovascular Therapy
ISSN: 2573-4482
Page 64
March 28-29, 2019
Rome, Italy
Vascular Surgery
4
th
Edition of World Congress & Exhibition on
R Srinanthalogen et al., J Vasc Endovasc Therapy 2019, Volume 4
DOI: 10.21767/2573-4482-C1-006
A novel view to varicose veins pathogenesis: Proteomic
analysis
R Srinanthalogen
1
, M Urbonavicius
2
, A Høgh
1
, G Urbonaviciene
3
, J Cicenas
4
, M
Valius
5
and
S Urbonavicius
1
1
Hospitalsenhed Midt, Viborg, Denmark
2
University of Copenhagen, Denmark
3
Hospitalsenhed Midt, Silkeborg, Denmark
4
Swiss Institute of Bioinformatics, University of Basel, Switzerland
5
Vilnius University, Lithuania
Introduction:
The advent of proteomics techniques
allows large-scale studies of gene expression at protein
level. Although morphological and anatomical studies
indicate that venous wall weakening and sub-endothelial
fibrosis characterize varicose veins, the pathogenesis of
varicose veins remains poorly understood. The aim this
study is to obtain protein expression profiles in patients
with varicose veins. Finally, the identification of possible
biomarkers may open possibilities for pharmacological
inhibition of disease progression.
Methods:
Varicose saphenous veins removed during
phlebectomy and normal saphenous veins obtained
during vascular surgery were collected for proteomics
analysis. The same layers of venous wall from varicose
and non-varicose veins were incubated, and the proteins
released were analyzed by ion mobility spectrometry
(IMS-MS) with Synapt G2. All differentially expressed
proteins and their pathways, coexpression and physical
interactions were analyzed in GeneMANIA and AmiGO
databases.
Results:
Proteomic analysis of the human vein revealed
totally 1389 proteins. 220 proteins demonstrated
significant differences in their quantity (more than 1.5
fold) between the two types of venous tissue (p<0.05).
Among the most differentially expressed proteins 10
were found significantly decreased in the varicose vein
tissue, and only two-increased. CXXC-type zinc finger
protein was more permanent (38-fold down regulated).
This protein is known as receptor for vascular endothelial
growth factor. Most prominent proteins were proved with
Western Blotting analysis.
Conclusion:
This study provides novel insights into the
biochemical mechanisms of this disease and a basis
for further studies. Our proteomics discovery approach
suggests that altered connective tissue proteins and
increased proteolytic enzyme activity appear to be central
to the pathophysiology of varicose veins. Abnormalities in
vein wall architecture probably precede the development
of valvular incompetence and overt varicosities. Larger
studies are required to confirm the potential and clinical
role of the identified proteins.