PubMed Health⌕ Search

PubMed · 9631581

Mature and immature myeloid cells decrease the granulocyte colony-stimulating factor level by absorption of granulocyte colony-stimulating factor.

Abstract

We studied the effects of polymorphonuclear neutrophils (PMN) and immature myeloid cells on the granulocyte colony-stimulating factor (G-CSF) level in vitro to better understand the regulatory mechanisms of neutropoiesis. Intact normal PMN decreased the G-CSF level after incubation with recombinant human (rh) G-CSF in a time- and dose-dependent manner. The percent reduction decreased as the concentration of rhG-CSF increased. However, the cell-free PMN-conditioned medium (PMN-CM) did not decrease the G-CSF level. The intact PMN also decreased the granulocyte-macrophage (GM)-CSF level after culture with rhGM-CSF, but did not affect the monocyte (M)-CSF level after culture with rhM-CSF. Normal bone marrow (BM) immature neutrophilic cells and G-CSF-dependent acute myeloid leukemic cells (OCI/AML la) also decreased the G-CSF level, whereas K-562 cells, which have no detectable G-CSF receptors, did not affect it. Phenylarsine oxide (PhAsO), an inhibitor of endocytosis of ligand receptor complex, abrogated this decreasing effect of intact PMN and OCI/AML la cells. These findings suggest that mature and immature myeloid cells negatively regulate neutropoiesis by, at least in part, decreasing the G-CSF level probably through receptor-mediated continual absorption and metabolism of G-CSF.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

K Saito, Y Nakamura, K Waga, K Hirota, F Inoue, H Enokihara, N Nara, S Furusawa. 1998. Mature and immature myeloid cells decrease the granulocyte colony-stimulating factor level by absorption of granulocyte colony-stimulating factor.. https://doi.org/10.1016/s0925-5710(97)00107-2

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

Filler-coupling agent-matrix interactions in silica/polymethylmethacrylate composites.

The interactions of the silane coupling agent methacryloxypropyltrimethoxysilane (MPS) with both fumed silica and a polymethylmethacrylate (PMMA) resin matrix were investigated using thermogravimetric analysis and Fourier transform infrared spectroscopy. OX 50 fumed silica was silanated with MPS at concentrations of 1% and 5% in aqueous ethanol (95%), acetone, and anhydrous toluene. Methyl methacrylate was polymerized with the silanated fumed silica (5% wt/wt) to form composites. The amount of MPS adsorption on the fumed silica and the amount of PMMA attached to the silanated fumed silica were determined by thermogravimetric analysis. MPS could be removed from the fumed silica after washing with methanol, but not after it underwent a drying process at 25 degrees C under vacuum. After vacuum drying at 25 degrees C, two types of adsorbed silane were found, i.e., firmly adsorbed and loosely adsorbed silane. The loosely adsorbed silane could desorb from silica and be incorporated into the polymer matrix through copolymerization with monomeric methyl methacrylate, resulting in crosslinking of the matrix. When the silanated silica was dried at 110 degrees C for 2 h, the loosely adsorbed silane was removed and the amount of firmly adsorbed silane increased. There was a positive correlation between the amount of firmly adsorbed MPS and the amount of PMMA attachment. The highest efficiency for PMMA attachment was found when MPS was adsorbed as a monolayer, because the loosely adsorbed silane did not contribute to the bonding of PMMA, and this suggested that not all of the double bonds of the MPS were accessible for reaction with the methacrylate monomer. Drying at 110 degrees C may also decrease the number of unsaturated double bonds of MPS.

Absorption↗

Effect of poly-L-arginine on the nasal absorption of FITC-dextran of different molecular weights and recombinant human granulocyte colony-stimulating factor (rhG-CSF) in rats.

The effect of poly-L-arginine (poly-L-Arg) on the in vivo nasal absorption of FITC-dextrans with a mean molecular weight ranging from 4.3 to 167 kDa and recombinant human granulocyte colony-stimulating factor (rhG-CSF) in rats were studied. When FITC-dextrans were co-administered intranasally with 1.0 w/v% poly-L-Args of different molecular weight (MW, ca. 45.5 and 92 kDa, poly-L-Arg (50) and poly-L-Arg (100)), the bioavailability (F(infinity)) increased markedly compared with that after administration of FITC-dextran alone. However, the F(infinity) decreased exponentially with the increasing molecular weight of FITC-dextrans. There was no significant difference between the enhanced nasal absorption of FITC-dextrans achieved by the co-administration of poly-L-Arg (50) and poly-L-Arg (100). Moreover, the relationship between the F(infinity) and the molecular weight of FITC-dextrans indicated that the molecular weight of protein drugs, which exhibited efficient absorption with poly-L-Arg, was about 20 kDa, when the lower limit of bioavailability for developing a potent transnasal delivery system was assumed to be about 10%. Indeed, the nasal absorption of rhG-CSF, which has a molecular weight of 18.8 kDa, was also increased after co-administration of 1.0 w/v% poly-L-Arg (50) and the F(infinity) was about 11%. It seems likely that poly-L-Arg can be used to provide adequate nasal absorption of various protein drugs which have a molecular weight of about 20 kDa, thereby allowing the successful development of a variety of transnasal drug delivery systems.

Absorption↗

Novel heme ligation in a c-type cytochrome involved in thiosulfate oxidation: EPR and MCD of SoxAX from Rhodovulum sulfidophilum.

The SoxAX complex of the bacterium Rhodovulum sulfidophilum is a heterodimeric c-type cytochrome that plays an essential role in photosynthetic thiosulfate and sulfide oxidation. The three heme sites of SoxAX have been analyzed using electronic absorption, electron paramagnetic resonance, and magnetic circular dichroism spectroscopies. Heme-3 in the ferric state is characterized by a Large g(max) EPR signal and has histidine and methionine axial heme iron ligands which are retained on reduction to the ferrous state. Hemes-1 and -2 both have thiolate plus nitrogenous ligand sets in the ferric state and give rise to rhombic EPR spectra. Heme-1, whose ligands derive from cysteinate and histidine residues, remains ferric in the presence of dithionite ion. Ferric heme-2 exists with a preparation-dependent mixture of two different ligand sets, one being cysteinate/histidine, the other an unidentified pair with a weaker crystal-field strength. Upon reduction of the SoxAX complex with dithionite, a change occurs in the ligands of heme-2 in which the thiolate is either protonated or replaced by an unidentified ligand. Sequence analysis places the histidine/methionine-coordinated heme in SoxX and the thiolate-liganded hemes in SoxA. SoxAX is the first naturally occurring c-type cytochrome in which a thiolate-coordinated heme has been identified.

Absorption↗