@article{silva_sawitzki_scheible_bailey_alho_faith_2018, title={Paternity testing using massively parallel sequencing and the PowerSeq (TM) AUTO/Y system for short tandem repeat sequencing}, volume={39}, ISSN={["1522-2683"]}, DOI={10.1002/elps.201800072}, abstractNote={Abstract}, number={21}, journal={ELECTROPHORESIS}, author={Silva, Deborah S. B. S. and Sawitzki, Fernanda R. and Scheible, Melissa K. R. and Bailey, Sarah F. and Alho, Clarice S. and Faith, Seth A.}, year={2018}, month={Nov}, pages={2669–2673} }
 @article{tipsmark_strom_bailey_borski_2008, title={Leptin stimulates pituitary prolactin release through an extracellular signal-regulated kinase-dependent pathway}, volume={196}, ISSN={["1479-6805"]}, DOI={10.1677/JOE-07-0540}, abstractNote={Leptin was initially identified as a regulator of appetite and weight control centers in the hypothalamus, but appears to be involved in a number of physiological processes. This study was carried out to examine the possible role of leptin in regulating prolactin (PRL) release using the teleost pituitary model system. This advantageous system allows isolation of a nearly pure population of lactotropes in their natural, in situ aggregated state. The rostral pars distalis were dissected from tilapia pituitaries and exposed to varying concentrations of leptin (0, 1, 10, 100 nM) for 1 h. Release of PRL was stimulated by leptin in a potent and concentration-dependent manner. A time-course experiment showed that the strongest response in PRL release with leptin occurs within the first hour (approximately sixfold), and stimulation was sustained after 16 h (approximately twofold). Many of the actions of leptin are mediated by the activation of extracellular signal-regulated kinase (ERK1/2) but nothing is known about the cellular mechanisms by which leptin might regulate PRL secretion in vertebrates. We therefore tested whether ERK1/2 might be involved in the leptin PRL response and found that the ERK inhibitor, PD98059, hindered leptin-induced PRL release. We further analyzed leptin response by quantifying tyrosine and threonine phosphorylation of ERK1/2 using western blots. One hour incubation with leptin induced a concentration-dependent increase in phosphorylated, and thus active, ERK1/2. Our data show that leptin is a powerful stimulator of in vitro PRL release and that its actions occur in part through stimulation of ERK1/2.}, number={2}, journal={JOURNAL OF ENDOCRINOLOGY}, author={Tipsmark, Christian K. and Strom, Christina N. and Bailey, Sean T. and Borski, Russell J.}, year={2008}, month={Feb}, pages={275–281} }