Abstract

The specific objectives of this project are the following: (1) Isolate and structurally characterize phosphorylated variants of bovine PRL and GH and identify the cellular location and protein kinase that performs the phosphorylation; (2) Determine the physiological agents that regulate the phosphorylation and secretion of bovine PRL and GH; and (3) Determine the biological actions of phosphorylated variants of bovine PRL and GH in a series of bioassays and compare these activities with those induced by nonphosphorylated forms of these hormones and by reference preparations.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK)
Type
Research Project (R01)
Project #
1R01DK042604-01A2
Application #
3243748
Study Section
Biochemical Endocrinology Study Section (BCE)
Project Start
1991-08-01
Project End
1994-07-31
Budget Start
1991-08-01
Budget End
1992-07-31
Support Year
1
Fiscal Year
1991
Total Cost
Indirect Cost

  Institution

Name
Ohio State University
Department
Type
Schools of Veterinary Medicine
DUNS #
098987217
City
Columbus
State
OH
Country
United States
Zip Code
43210

  Publications

Schenck, E J H; Brooks, C L (2006) Effects of an S84E mutation of bovine growth hormone in transgenic mice. Exp Biol Med (Maywood) 231:296-302
Peterson, F C; Anderson, P J; Berliner, L J et al. (1999) Expression, folding, and characterization of small proteins with increasing disulfide complexity by a pT7-7-derived phagemid. Protein Expr Purif 15:16-23
Wicks, J R; Brooks, C L (1999) GH kinase activity in bovine anterior pituitary subcellular fractions. Endocrine 10:77-82
Brooks, C L; Saiduddin, S (1998) Phosphorylation of bovine prolactin eliminates luteotropic activity in the rat. Life Sci 63:1281-7
Peterson, F C; Brooks, C L (1997) Identification of a motif associated with the lactogenic actions of human growth hormone. J Biol Chem 272:21444-8
Maciejewski, P M; Peterson, F C; Anderson, P J et al. (1995) Mutation of serine 90 to glutamic acid mimics phosphorylation of bovine prolactin. J Biol Chem 270:27661-5
Wicks, J R; Brooks, C L (1995) Biological activity of phosphorylated and dephosphorylated bovine prolactin. Mol Cell Endocrinol 112:223-9
Brooks, C L; Isaacs, L A; Wicks, J R (1994) Preparative purification of phosphorylated and nonphosphorylated bovine prolactins. Mol Cell Endocrinol 99:301-5
Kim, B G; Brooks, C L (1993) Isolation and characterization of phosphorylated bovine prolactin. Biochem J 296 ( Pt 1):41-7