Abstract
Rac2 is a small GTPase in the Rho family. The lungs of uninjured Rac2−/− mice show enhanced plasma flux. This study determined if Rac2 is expressed and regulates phosphorylation of cytoskeletal proteins in ECs. Real time PCR showed that ECs isolated from murine lung digests by negative selection of CD45+ cells (leukocytes) and positive selection of CD105+ ECs express Rac2 mRNA. An 11 amino acid region in the C‐terminus of murine Rac2 was used to generate a rabbit polyclonal anti‐Rac2 antibody (Pacific Immunology). This antibody recognized Rac2 (21kDa) on immunoblots of murine Rac2+/+ but not −/− ECs and splenocytes, and not human Rac2 in HL60 cells. Protein arrays assessing 95 proteins associated with the cytoskeleton (cytoskeleton phospho antibody microarray, Full Moon Biosystems) showed that Rac2−/− ECs had increased expression of 2 proteins (caveolin‐1: 2.5 fold, LIMK1: 2.0 fold) and decreased expression or phosphorylation of 4 proteins (cortactin: 0.41, MEK1(Phospho‐Ser217): 0.06, MEK1(Phospho‐Thr291): 0.54, Src: 0.53, Vav(Phospho‐Tyr174): 0.54 fold). Thus, Rac2 mRNA and protein are expressed by ECs. Rac2 appears to regulate the cytoskeletal structure and function of ECs. Funded by HL 077370.
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