The long range objective of this project is to apply the techniques of biochemistry to investigate how genes of the nervous system are expressed and regulated. The nervous system is composed of many neurons which interconnect with one another in a precise manner. The diversity of neurons and the nature of their interactions suggest that specific genes or sets of genes are activated in some neurons and not in others. The autonomic nervous system affords a particularly suitable approach to analyzing specific gene expression. The adrenal medulla is part of the autonomic nervous system which is embryologically derived from neurons tissue and which is analogous to postganglionic neurons. The adrenal medulla is a major site of catecholamine biosynthesis as well as the site for synthesis of neuropeptides. One of the specific aims of this proposal is to develop a better understanding of the molecular events regulating the rate controlling enzyme in catecholamine biosynthesis (tyrosine hydroxylase) and the newly discovered peptide which has been named neuropeptide Y. The brain also synthesizes numerous classical neurotransmitters and neuropeptides. Two of the major neuropeptides found in the brain are neuropeptide Y and cholecystokinin. The tools of molecular biology will be used t develop a better understanding of how the gene(s) encoding cholecystokinin are controlled and modulated during development. The information obtained from these studies should also suggest structures for the precursors to human and rat cholecystokinin(s) and potential sties of post-translational processing.

Agency
National Institute of Health (NIH)
Institute
National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK)
Type
Research Project (R01)
Project #
5R01DK018849-11
Application #
3226159
Study Section
Biochemistry Study Section (BIO)
Project Start
1976-05-01
Project End
1989-06-30
Budget Start
1986-07-01
Budget End
1987-06-30
Support Year
11
Fiscal Year
1986
Total Cost
Indirect Cost
Name
Purdue University
Department
Type
Earth Sciences/Resources
DUNS #
072051394
City
West Lafayette
State
IN
Country
United States
Zip Code
47907
Banerjee, Sourav; Ji, Chenggong; Mayfield, Joshua E et al. (2018) Ancient drug curcumin impedes 26S proteasome activity by direct inhibition of dual-specificity tyrosine-regulated kinase 2. Proc Natl Acad Sci U S A 115:8155-8160
Zhang, Hui; Zhu, Qinyu; Cui, Jixin et al. (2018) Structure and evolution of the Fam20 kinases. Nat Commun 9:1218
Qiu, Yimin; Poppleton, Erik; Mekkat, Arya et al. (2018) Enzymatic Phosphorylation of Ser in a Type I Collagen Peptide. Biophys J 115:2327-2335
Pollak, Adam J; Haghighi, Kobra; Kunduri, Swati et al. (2017) Phosphorylation of serine96 of histidine-rich calcium-binding protein by the Fam20C kinase functions to prevent cardiac arrhythmia. Proc Natl Acad Sci U S A 114:9098-9103
Cui, Jixin; Zhu, Qinyu; Zhang, Hui et al. (2017) Structure of Fam20A reveals a pseudokinase featuring a unique disulfide pattern and inverted ATP-binding. Elife 6:
Wang, Xiaorong; Cimermancic, Peter; Yu, Clinton et al. (2017) Molecular Details Underlying Dynamic Structures and Regulation of the Human 26S Proteasome. Mol Cell Proteomics 16:840-854
Nguyen, Kim B; Sreelatha, Anju; Durrant, Eric S et al. (2016) Phosphorylation of spore coat proteins by a family of atypical protein kinases. Proc Natl Acad Sci U S A 113:E3482-91
Guo, Xing; Wang, Xiaorong; Wang, Zhiping et al. (2016) Site-specific proteasome phosphorylation controls cell proliferation and tumorigenesis. Nat Cell Biol 18:202-12
Tagliabracci, Vincent S; Wiley, Sandra E; Guo, Xiao et al. (2015) A Single Kinase Generates the Majority of the Secreted Phosphoproteome. Cell 161:1619-32
He, Yantao; Guo, Xing; Yu, Zhi-Hong et al. (2015) A potent and selective inhibitor for the UBLCP1 proteasome phosphatase. Bioorg Med Chem 23:2798-809

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