Proteomic profiling of medial degeneration in human ascending aorta.

OBJECTIVE

The objective of this study was the construction of a reference map for aortic medial degeneration by a proteomic approach.

METHODS

A proteomic profiling of the media of human ascending aorta was performed by two-dimensional electrophoresis and MALDI-TOF mass spectrometry.

RESULTS

A reliable protocol for two-dimensional electrophoresis analysis of human aortic media proteins was developed allowing the selection and identification of 52 spots. Protein identifications revealed that the predominant vascular smooth muscle cell proteins isolated from grade 1 aortic medial degeneration (MD) included proteins involved in muscle contraction, protein folding, cytoskeletal structure and metabolic processes, and those with antioxidant or transport functions. The most populated functional classes were those related to muscle contraction and cytoskeletal proteins, including actin, calmodulin, calponin, myosin light chain, tropomyosin, vimentin, profilin and transgelin.

CONCLUSIONS

The obtained aortic MD proteomic profile provides a relevant background for future studies aimed to find further specific molecular changes potentially related to the aortic MD process.