Data on hepatic lipolysis, adipose triglyceride lipase, and hormone-sensitive lipase in fasted and non-fasted C57BL/6J female mice
Phillip M. Marvyn,
Emily B. Mardian,
Ryan M. Bradley,
Kristin A. Marks,
Robin E. Duncan
Affiliations
Phillip M. Marvyn
University of Waterloo, Department of Kinesiology, Faculty of Applied Health Sciences, 200 University Avenue W., BMH1110, Waterloo, Ontario, Canada N2L 3G1
Emily B. Mardian
University of Waterloo, Department of Kinesiology, Faculty of Applied Health Sciences, 200 University Avenue W., BMH1110, Waterloo, Ontario, Canada N2L 3G1
Ryan M. Bradley
University of Waterloo, Department of Kinesiology, Faculty of Applied Health Sciences, 200 University Avenue W., BMH1110, Waterloo, Ontario, Canada N2L 3G1
Kristin A. Marks
University of Waterloo, Department of Kinesiology, Faculty of Applied Health Sciences, 200 University Avenue W., BMH1110, Waterloo, Ontario, Canada N2L 3G1
Robin E. Duncan
Corresponding author.; University of Waterloo, Department of Kinesiology, Faculty of Applied Health Sciences, 200 University Avenue W., BMH1110, Waterloo, Ontario, Canada N2L 3G1
Liver homogenates produced from fasted and non-fasted C57BL/6J female mice were assayed for total lipolytic activity measured as hydrolysis of [9,10-3H(N)]-triolein into [3H] free fatty acids (FFA). Liver homogenates were also used for immunoblotting to determine levels of the lipolytic enzymes adipose-triglyceride lipase (ATGL) and hormone-sensitive lipase (HSL), as well as site specific phosphorylation at the 14-3-3 binding site of ATGL and the serine 565 and serine 660 sites of HSL. Significantly higher triolein hydrolysis activity was observed in fasted liver samples, as well as a significant increase in total ATGL and a significant decrease in HSL phosphorylation at the S565 site.
