Abstract:
:PGI is a housekeeping gene encoding phosphoglucose isomerase (PGI) a glycolytic enzyme that also functions as a cytokine (autocrine motility factor (AMF)/neuroleukin/maturation factor) upon secretion from the cell and binding to its 78 kDa seven-transmembrane domain receptor (gp78/AMF-R). PGI contains a CXXC motif, characteristic of redox proteins and possibly evolutionarily related to the CC and CXC motif of the chemokine gene family. Using site-directed mutagenesis, single- and double-deletion (CXC, CC) mutants were created by deleting amino acids 331 and 332 of human PGI, respectively. The mutant proteins lost their enzymatic activity; however, neither of the deletions augmented the proteins' binding affinity to the receptor and all maintained cytokine function. The results demonstrate that the enzymatic activity of PGI is not essential for either receptor binding or cytokine function of human PGI.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Tsutsumi S,Gupta SK,Hogan V,Tanaka N,Nakamura KT,Nabi IR,Raz Adoi
10.1016/s0014-6793(02)03773-0keywords:
subject
Has Abstractpub_date
2003-01-16 00:00:00pages
49-53issue
1-3eissn
0014-5793issn
1873-3468pii
S0014579302037730journal_volume
534pub_type
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