Abstract

Nonapeptide thymic hormone thymulin is produced by thymic endocrine epithelial cells. Its biological activities have been well described and its role in various immunopathological status including AIDS has been implicated. Although its complete amino acid sequence has been established more than 10 years ago, the presence of prothymulin was not discovered till recently. Moreover, its gene has not been cloned yet. The advancement in the field of molecular biology of thymulin has been severely hindered by the lack of in vitro model system. Here we report the recent establishment of thymic endocrine epithelial cell line which produces thymulin and proposes to: 1) purify and sequence prothymulin; 2) clone thymulin gene and 3) study the control mechanism of thymulin gene activation and expression. We are now developing cDNA library from thymic endocrine epithetial cell line. We have also developed rabbit antibody to thymulin which recognizes prothymulin molecule as well. With this cell line and antiserum in our hand, we are confident that we can achieve the proposed study.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Cancer Institute (NCI)
Type
Research Program Projects (P01)
Project #
5P01CA037589-07
Application #
3812544
Study Section
Project Start
Project End
Budget Start
Budget End
Support Year
7
Fiscal Year
1990
Total Cost
Indirect Cost

  Institution

Name
Adirondack Biomedical Research Institute
Department
Type
DUNS #
City
Lake Placid
State
NY
Country
United States
Zip Code
12946

  Publications

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McKeehan, W L; Kan, M (1994) Heparan sulfate fibroblast growth factor receptor complex: structure-function relationships. Mol Reprod Dev 39:69-81;discusison 81-2
Hyatt, S L; Liao, L; Chapline, C et al. (1994) Identification and characterization of alpha-protein kinase C binding proteins in normal and transformed REF52 cells. Biochemistry 33:1223-8
Liao, L; Jaken, S (1993) Effect of alpha-protein kinase C neutralizing antibodies and the pseudosubstrate peptide on phosphorylation, migration, and growth of REF52 cells. Cell Growth Differ 4:309-16
Chapline, C; Ramsay, K; Klauck, T et al. (1993) Interaction cloning of protein kinase C substrates. J Biol Chem 268:6858-61
Palczewski, K; Buczylko, J; Lebioda, L et al. (1993) Identification of the N-terminal region in rhodopsin kinase involved in its interaction with rhodopsin. J Biol Chem 268:6004-13
Yan, G; McBride, G; McKeehan, W L (1993) Exon skipping causes alteration of the COOH-terminus and deletion of the phospholipase C gamma 1 interaction site in the FGF receptor 2 kinase in normal prostate epithelial cells. Biochem Biophys Res Commun 194:512-8

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