Human granulocyte colony-stimulating factor specifically binds to murine myeloblastic NFS-60 cells and activates their guanosine triphosphate binding proteins/adenylate cyclase system
Author(s) -
Sachiko Matsuda,
Naoki Shirafuji,
Shingo Asano
Publication year - 1989
Publication title -
blood
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.515
H-Index - 465
eISSN - 1528-0020
pISSN - 0006-4971
DOI - 10.1182/blood.v74.7.2343.2343
Subject(s) - adenylate kinase , guanosine , gtp' , cyclase , guanosine triphosphate , biology , receptor , biochemistry , microbiology and biotechnology , intracellular , chemistry , enzyme
The specific binding of human granulocyte colony-stimulating factor (G-CSF) to its receptors on NFS-60 cells acts as a primer for cellular proliferation. There are approximately 400 binding sites per cell, with a binding constant of about 100 pmol/L. Before the proliferative response, the affinity constant of the membrane particulate fraction to 35S-labeled guanosine triphosphate-gamma-S (35S-GTP gamma S) and the intracellular cyclic adenylate monophosphate (cAMP) level increased in the presence of G-CSF to about 2.5-fold and about fivefold higher, respectively, than the levels seen in the absence of G-CSF. The increases were time-dependent, with a peak occurring 15 minutes after the addition of G-CSF at 37 degrees C. These findings suggest that, following the binding of the G-CSF to its surface receptors, the activation of the guanosine triphosphate (GTP)-binding protein/adenylate cyclase system may be involved in the proliferation of immature myeloid cells.
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