RHO GTPases are key regulators of the actin cytoskeleton and stress fibre formation in smooth muscle. In human myometrium, activated RHOA forms a complex with RHO-kinase (ROCK) which phosphorylates and inhibits myosin phosphatase (MYPT), causing a calcium-independent increase in myosin light chain phosphorylation and tension (Ca²⁺ sensitization) [1,2]. We have recently reported that new family small GTP binding proteins, RND proteins, can inhibit RHOA-ROCK interaction to reduce Ca²⁺ sensitization [3]. There is very little information regarding the mRNA expression of RND proteins in human myometrial or placental tissues. We aim to quantify the relative expression of RND mRNA in non-pregnant, pregnant myometrial and placental tissues using quantitative RT-PCR. mRNA will be extracted from five independent myometrial and placental tissues and differential expression of RND mRNA will be determined using SYBR green detection and normalised to RNA polymerase II (house keeping gene) expression in NP tissue. RND2 and RND3 mRNA were expressed in both non-pregnant and pregnant myometrium, and although there was an increasing trend in mRNA expression in pregnant myometrium relative to non-pregnant myometrium, this was not significant by one-way ANOVA analysis (p> 0.05). This is in marked contrast to previous reports demonstrating significant increases in RND protein expression in pregnancy[3]. RND2 and RND3 mRNA were also expressed in placental tissues. Further work is needed to explore the regulation of the expression on RND GTPases in human myometrium.