The effects of Mx1-Cre mediated RGS12 conditional knockout on the mouse submandibular gland
Olson, Douglas Peter
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Guanine nucleotide-binding proteins (G-proteins) are a family of heterotrimeric intracellular proteins, which along with their G protein-coupled receptors (GPCRs), form one of the most prominent signaling pathways in mammalian systems. The recently discovered regulators of g-protein signaling (RGS) proteins have been shown to play critical roles in the regulation of GPCR signaling in normal physiology as well as in human diseases such as heart diseases, depression, inflammation, and cancer. Recent evidence has begun to elucidate various roles RGS protein may play in salivary gland function, especially their involvement in maintaining the necessary [Ca2+]i signal needed for normal fluid secretion. RGS12 has the distinction of being the largest member of the RGS family and in vitro studies have demonstrated that Rgs12 plays a critical role in regulating cell differentiation and migration, however its function and mechanism in vivo is largely unknown. Using the RGS12 conditional knockout mouse model generated in our lab we show for the first time that RGS12 is expressed in submandibular glands of mice and we are able to at least partially delete its expression using the Mx1-Cre/loxP recombination system. While at the gross level there appears to be no change in the anatomy of the gland at the microscopic level there is a definite change in the phenotype of the mutant glands as compared to wild-type with an apparent increase in the percentage of mucous acini in relation to serous acini. Regarding function, there was no significant difference found in salivary production. Future studies will look into the distinguishing if there is a difference in the quality of the salivary content as well as discerning the mechanism/pathway involved that results in the noticed phenotype change.