PGI/AMF is correlated with breast cancer and poor prognosis in breast cancer. Inhibition of PGI/AMF expression triggers mesenchymal-to-epithelial transition in aggressive mesenchymal-type breast cancer MD-MB-231 cells
AMF is critical for the migration, invasion, metastasis, and anti-apoptotic effects of malignant tumor cells, and its multiple roles in tumor progression may be mediated by certain downstream pathways and effectors. Phosphoglucose isomerase/autocrine motility factor promotes melanoma cell migration through ERK activation dependent on autocrine production of interleukin-8, overview
multifunctional protein GPI is an endogenous inhibitor to myofibril-bound serine proteinase, and may play a significant role in the regulation of muscular protein metabolism in vivo
PGI/AMF is a housekeeping gene product/cytokine that catalyzes a step in glycolysis and gluconeogenesis, and acts as a multifunctional cytokine associated with aggessive tumors. PGI/AMF induces a mesenchymal-like morphologic conversion being a key enzyme for both epithelial-to-mesenchymal transition in the initiating step of cancer metastasis and mesenchymal-to-epithelial transition in the late stage of metastasis during breast cancer progression, overview
phosphoglucose isomerase plays a key role in both glycolysis and gluconeogenesis inside the cell, whereas outside the cell it exhibits cytokine properties. The enzyme also acts as an autocrine motility factor, a neuroleukin agent and a differentiation and maturation mediator
the Pgi activity is limiting in the control BL310 strain during growth on lactose or galactose. The level of Pgi enzyme activity controls the level of production of those UDP-glucose and UDP-galactose in galactose
autocrine motility factor/phosphoglucose isomerase (AMF/PGI) regulates endoplasmic reticulm (ER) stress and cell death through control of ER calcium release. AMF/PGI also protects against thapsigargin- and tunicamycin-induced ER stress and apoptosis and suppresses cytosolic Ca2+ homeostasis
a leaky mutant expressing PGI1 at a level of 1.9% of the wild type, is able to synthesize the pigment melanin in the presence of 2% glucose. Capsule biosynthesis is remarkably reduced in the mutant, integrity of the cell wall and plasma membrane are impaired. The mutant exhibits hypersensitivity to osmotic stress generated by 2 M NaCl or 1 M KCl and fails to utilize mannose and fructose
starch content in leaves completely lacking PGI1 activity is about 10-15% of that of wild type leaves and can be be reverted by the introduction of a sex1 null mutation impeding beta-amylolytic starch breakdown. In mutant strains, starch granules are present in the chloroplasts of mesophyll cells and plastidic and extra-plastidic beta-amylase encoding genes are higly expressed in leaves. Mutant strains display slow growth and reduced photosynthetic capacity phenotypes even under continuous light conditions
phosphoglucose isomerase plays a key role in both glycolysis and gluconeogenesis inside the cell, whereas outside the cell it exhibits cytokine properties. The enzyme also acts as an autocrine motility factor, a neuroleukin agent and a differentiation and maturation mediator
a leaky mutant expressing PGI1 at a level of 1.9% of the wild type, is able to synthesize the pigment melanin in the presence of 2% glucose. Capsule biosynthesis is remarkably reduced in the mutant, integrity of the cell wall and plasma membrane are impaired. The mutant exhibits hypersensitivity to osmotic stress generated by 2 M NaCl or 1 M KCl and fails to utilize mannose and fructose