The integral endoplasmic reticulum membrane-based enzyme G6PC hydrolyzes its substrate glucose-6-phosphate into glucose. Specifically, G6PC breaks down D-glucose 6-phosphate to D-glucose and orthophosphate. Because G6PC forms with the glucose-6-phosphate transporter (SLC37A4/G6PT), the resulting complex is responsible for glucose production. Thus, G6PC is the key enzyme in glucose homeostasis, functioning in both the processes of gluconeogenesis and glycogenolysis. Defects in the enzyme cause glycogen storage disease type I (von Gierke disease). Not surprisingly, G6PC is localized mainly in the liver and kidneys. It is unique in that it is membrane-bound, unlike most other enzymes that act upon water soluble substrates.
Immunohistochemistry-Paraffin: G6PC Antibody
An overview of the G6PC system including discussions of its regulation by glucose, insulin, cAMP, and glucocorticoids can be found in van Schaftingen’s review article1. Banka and Newman have more recently presented a clinical and molecular review on G6PC mutations and their physiological manifestations and links to various diseases2. Cicherchi et al employed the G6PC antibody to help them document the downstream effects of uric acid-dependent inhibition of AMP kinase (AMPK) in diabetes and starvation through an evolutionary standpoint3. Their data shows that an uricase mutation dating back 1.5 x 107 yrs ago to the hominid Miocene period (and triggered by a widespread famine period in Europe) when expressed in modern cell lines, likely conferred a survival advantage. This adaptation helped human ancestors to maintain critical glucose levels under situations of near-starvation, but in modern times, only serves to feed diabetes and insulin resistance.
Novus Biologicals offers G6PC reagents for your research needs including:
PMIDs
