Guanylate-binding protein 1 (GBP-1) is a member of the GBP family whose members are GTPases induced in response to interferon-λ (IFN-λ), with seven highly homologous members in humans, termed HuGBP-1 to HuGBP-7. GBP-1 expression is induced by type1 and type2 interferons, including IFN-λ and also by interleukin-1β (IL-1β), IL-1α, and tumor necrosis factor-α (TNF-α). GBP-1 is key to the protective immunity against microbial and viral pathogens. GBP-1 was only secreted from endothelial cells. Secretion occurred without the presence of a leader peptide. Secretion procession is a nonclassical, likely ABC transporter-dependent, pathway and independent of GBP-1 GTPase activity and isoprenylation, and did not require additional interferon-λ-induced factors. Clinically most important was the detection of significantly increased GBP-1 concentrations in the cerebrospinal fluid of patients with bacterial meningitis as compared to control patients.
Glutaryl-CoA Dehydrogenase Mitochondrial (GCDH) is an enzyme that acts upon glutaryl-coenzyme A, creating crotonyl-coenzyme A. It plays a role in the metabolism of lysine, hydroxylysine and tryptophan. It uses electron transfer flavoprotein as its electron acceptor. Isoform Short is inactive Glutaryl-CoA and electron-transfer flavoprotein to (E)-but-2-enoyl-CoA, CO2 and reduced electron-transfer flavoprotein. A defect in this enzyme is associated with neurological condition glutaric acidemia type 1 and cause a progressive form of early-onset generalized dystonia.
Glutamate-cysteine ligase, also known as gamma-glutamylcysteine synthetase is the first rate-limiting enzyme of glutathione synthesis. The enzyme consists of two subunits, a heavy catalytic subunit and a light regulatory subunit. This locus encodes the catalytic subunit, while the regulatory subunit is derived from a different gene located on chromosome 1p22-p21. Mutations at this locus have been associated with hemolytic anemia due to deficiency of gamma-glutamylcysteine synthetase and susceptibility to myocardial infarction.
Human Granulocyte-Colony-Stimulating Factor (G-CSF) is 20 kD glycoprotein containing internal disulfide bonds. It induces the survival, proliferation, and differentiation of neutrophilic granulocyte precursor cells and it functionally activates mature blood neutrophils. Among the family of colony-stimulating factors, G-CSF is the most potent inducer of terminal differentiation to granulocytes and macrophages of leukemic myeloid cell lines. The synthesis of G-CSF can be induced by bacterial endotoxins, TNF, Interleukin-1, and GM-CSF. Prostaglandin E2 inhibits the synthesis of G-CSF. In epithelial, endothelial, and fibroblastic cells secretion of G-CSF is induced by Interleukin-17.
Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This CSF induces granulocytes.
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