Species specificity of the cytokine function of phosphoglucose isomerase

FEBS Letters

Nabi, Ivan R¹  Amraei, Mohammad¹ 

[1] Département de pathologie et biologie cellulaire, Université de Montréal, P.O. Box 6128, succursale A, Montreal, QC, Canada H3C 3J7

关键词: Phosphoglucose isomerase;    Autocrine motility factor receptor;    Cell motility;    Cytokine;    Endocytosis;    Glycolysis;    AMF;    autocrine motility factor;    AMF-R;    autocrine motility factor receptor;    MVB;    multivesicular body;    PGI;    phosphoglucose isomerase;   

DOI  :  10.1016/S0014-5793(02)03072-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Phosphoglucose isomerase (PGI) is a cytosolic glycolytic enzyme that also functions as an extracellular cytokine (neuroleukin/autocrine motility factor (AMF)/maturation factor). Contrary to mammalian PGI, bacterial PGI was not internalized by the PGI/AMF receptor (gp78/AMF-R) and neither bacterial nor yeast PGI competed with mammalian PGI for receptor binding and internalization. Furthermore, while the bacterial, yeast and mammalian preparations all exhibited isomerase activity, only mammalian PGI stimulated the motility of NIH-3T3 fibroblasts. The conserved active site of PGI is therefore not sufficient for receptor binding and cytokine activity of PGI. However, synthetic peptides corresponding to distinct peripheral mammalian PGI sequences did not inhibit internalization of mammalian PGI. Our data therefore argue that the cytokine activity of PGI is specific to mammalian PGI but cannot exclude the possibility that the receptor binding motif of PGI is complex and includes elements within and without the active site.

【 授权许可】

Unknown