Progress To Date
«Growth - Recombinant Human Growth Hormone (hGH) and hGH Antagonists (A)»
«Proteomics»
«Genomics»
Growth - Recombinant Human GH (hGH)
- Generated and purified glyco (g) hGH
- g-hGH binds to GH receptor (R) with same affinity as hGH
- g-hGH activates Stat-5 in cultured cells identically to hGH
- g-hGH is equi-potent to hGH in vivo
- g-hGH has extended serum half-life when compared to hGH
- g-hGH induces elevated levels of IGF-1 in vivo to the same extent as hGH but the elevated IGF-1 levels are prolonged
- Generated and purified a g-hGHA
- These experiments were done in collaboration with Drs. Marcia Kieliszewski and Jianfeng Xu of Ohio University
- Human serum analysis; same patient: serum analysis before and after surgery, drug treatment, etc.
- Several candidate proteins identified in the GH area
- Diabetes area
- Over 600 proteins identified (click on image for larger version)
- Several target proteins are either up- or down-regulated or are post-translational
modified as a function of insulin resistance or diabetes
(click on image for larger version)
- Proteins are being validated as therapeutics or therapeutic targets
- Many unknown proteins
- Using a genomics approach to diabetes and aging, we have discovered a gene expressed in the liver that
increases as a function of age (see ‘A’ below). It is also increased “early” in the liver of diabetic mice
(see ‘B’ below). This gene has been validated as a therapeutic target. Additionally, using a
genomics approach, we have discovered three other target genes that are currently being validated.
