Spinal arteriovenous malformations (sAVM) are rare and heterogeneous group of blood vessel disorders that affect spinal cord function directly or indirectly; however, the pathogenesis of sAVM is still unclear. In this study, we compared four sAVM specimens obtained during surgery and donated control samples in a Tandem Mass Tag (TMT)-labeled proteomic analysis. We identified 3101 proteins, 654 of which were differentially expressed in sAVM samples compared with the controls. Of these, 96 proteins were upregulated and 358 proteins were downregulated. Gene ontology (GO) analysis revealed that extracellular matrix organization in the biological process category and integrin-binding proteins in the molecular function category were the most enriched items. Two significant differentially expressed proteins (MYLK and MMP9) were verified by Western blot analysis. The pathway analysis indicated that the differentially expressed proteins in the pathways of angiogenesis, focal adhesion and cytoplasmic ribosome contributed to sAVM. The changes in protein profiles identified in this proteomic study provide an improved understanding of the pathogenesis of sAVM. The proteomics data are available via ProteomeXchange with identifier PXD007982.
Keywords: Angiogenesis; Focal adhesion; Proteomic; Ribosome; Spinal arteriovenous malformation.
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