We are using different muscle types of the chicken as model systems to investigate the mechanisms which regulate the biogenesis and degradation of specific well-defined eucaryotic proteins. Elucidation of these mechanisms is required for an in-depth understanding of both normal cell-function and the breakdown of normal cell function which is associated with certain disease states. We have recently made the significant observation that skeletal, cardiac and smooth (gizzard) muscles of the chicken synthesize secretory proteins. These observations are surprising since, unlike tissues such as liver and pancreas, muscle has not previously been considered to be a """"""""secretory"""""""" tissue. We have identified the secretory protein synthesized by skeletal and cardiac muscles as apolipoprotein A1, the main protein component of the """"""""high density"""""""" class of serum lipoprotein particles. We are in the process of identifying the 73,000 dalton secretory protein produced by gizzard muscle. The main goal of our research project is to investigate the regulation of synthesis of several intracellular enzymes (aldolase, glyceraldehyde-3-P dehydrogenase, and creatine kinase) and the regulation of synthesis and secretion of the muscle secretory proteins. These studies will involve measurements of specific mRNAs in these muscle types as determined in cDNA/mRNA hybridization experiments and measurements of relative rates of synthesis of the proteins in amino acid incorporation experiments conducted with intact muscle cells. Of major interest will be the work on the effect of development in vivo and of long term culture in vitro on the synthesis of these proteins by the muscle types. These latter experiments may help to identify the endogenous and exogeneous """"""""signals"""""""" which ultimately regulate the synthesis of these intracellular and secretory muscle proteins.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM023045-10
Application #
3271485
Study Section
Biochemistry Study Section (BIO)
Project Start
1976-05-01
Project End
1989-07-31
Budget Start
1985-08-01
Budget End
1986-07-31
Support Year
10
Fiscal Year
1985
Total Cost
Indirect Cost
Name
San Diego State University
Department
Type
Schools of Arts and Sciences
DUNS #
073371346
City
San Diego
State
CA
Country
United States
Zip Code
92182
Gehring, Andrew G; Ezzell, John L; Lebherz, Herbert G (2008) A selective reaction of fructose bisphosphate aldolase with fluorescein isothiocyanate in chicken muscle extracts. J Mol Recognit 21:137-47
Marsh, J J; Lebherz, H G (1992) Fructose-bisphosphate aldolases: an evolutionary history. Trends Biochem Sci 17:110-3
Nodes, B R; Shackelford, J E; Lebherz, H G (1987) Synthesis and secretion of serum gelsolin by smooth muscle tissue. J Biol Chem 262:5422-7
Lebherz, H G; Burke, T; Shackelford, J E et al. (1986) Specific proteolytic modification of creatine kinase isoenzymes. Implication of C-terminal involvement in enzymic activity but not in subunit-subunit recognition. Biochem J 233:51-6
Swain, M S; Lebherz, H G (1986) Hybridization between fructose diphosphate aldolase subunits derived from diverse biological systems: anomolous hybridization behavior of some aldolase subunit types. Arch Biochem Biophys 244:35-41
Swain, M S; Lebherz, H G (1986) Specific, limited tryptic modification of wheat-germ fructose-bisphosphate aldolase subunits: destruction of catalytic activity but not of ability to establish precise subunit-subunit recognition. Biochim Biophys Acta 869:185-91
Shackelford, J E; Lebherz, H G (1985) Synthesis of apolipoprotein A1 in skeletal muscles of normal and dystrophic chickens. J Biol Chem 260:288-91
Petell, J K; Lebherz, H G (1985) Content and synthesis of glycolytic enzymes and creatine kinase in skeletal muscles and normal and dystrophic chickens. Arch Biochem Biophys 237:271-80
Okamoto, V R; Moulton, M P; Runte, E M et al. (1985) Characterization of transverse tubule membrane proteins: tentative identification of the Mg-ATPase. Arch Biochem Biophys 237:43-54