Quantitive protein profiling and pathway analysis for spinal arteriovenous malformations

Spinal arteriovenous malformations (sAVM) were rare and heterogeneous group of blood vessel disorders that affected the function of spinal cord directly or indirectly. In the past decades, the pathogenesis for SAVM was still not elucidated. Here we compared the specimens of four sAVM obtained from surgery and control samples from donations using TMT labeled proteomic study. In our proteomic study, we identified a total of 3101 proteins and 654-proteins were changed in SAVM compares with control, among which 96 proteins were upregulated and 358 proteins were downregulated. Gene Ontology (GO) analysis revealed that extracellular matrix organization in biological process and integrin binding proteins in molecular function were the most enriched items. Four significant changed proteins (PLG, MPZ, MMP9 and RPL23a) were verified by Western blot. The pathway analysis revealed that the changed proteins in pathways of angiogenesis, focal adhesion and cytoplasmic ribosome likely contributed to SAVM. The protein profile changes identified by our proteomic studies provide a comprehensive understanding of sAVM for us.