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Biomedical subjects

Y Kameyoshi

Publications and source records attributed to Y Kameyoshi.

23 records · Page 2Linked to original sources
PubMed1994

Enhancement of fibroblast-dependent mast cell growth in mice by a conditioned medium of keratinocyte-derived squamous cell carcinoma cells.

We investigated the increase in mast cell numbers at the sites of inoculation of keratinocyte-derived squamous cell carcinoma cell line (KCMH-1) cells in mice. A significant increase in the number of mast cells was observed at the sites of tumours developed at the sites of inoculation of the KCMH-1 cells. Enhancement of mast cell growth was observed by culturing bone marrow-derived mast cells (BMMC) on NIH/3T3 fibroblast monolayers in the presence of conditioned medium (TCM) obtained from KCMH-1. Activities of known factors for mast cell growth, such as interleukin-3 (IL-3), IL-4, IL-9, IL-10 and stem cell factor (SCF), were not detected in the TCM. Nerve growth factor (NGF) did not induce mast cell growth. Mast cell growth induced by the TCM needed 3T3 fibroblasts. These results suggest that KCMH-1 cells may produce a factor which induces mast cell growth with 3T3 fibroblasts, other than the already known mast cell growth factors. This may be the mechanism of mast cell accumulation at sites of tumours.

Animals↗
PubMed1994

Identification of the cytokine RANTES released from platelets as an eosinophil chemotactic factor.

Selective infiltration of eosinophils suggests the presence of the factors that attract eosinophils preferentially. Selective chemotactic polypeptides for human eosinophils were purified from thrombin-stimulated platelet supernatants and this chemotaxin was identified as the chemokine RANTES. The isolation of natural RANTES and its activity for eosinophil migration is summarized here. RANTES induced eosinophil migration at nanomolar range, in both chemotactic and chemokinetic manners. Specific desensitization experiments indicated that RANTES binds to receptors different from those for C5a and PAF, well-known potent eosinophil chemotaxins.

Blood Platelets↗
PubMed1992

Cytokine RANTES released by thrombin-stimulated platelets is a potent attractant for human eosinophils.

Thrombin stimulation of human platelets results in the release of a preformed proteinaceous human eosinophil (Eo)-chemotactic activity. By the use of different high-performance liquid chromatography techniques, two Eo-chemotactic polypeptides (EoCPs), tentatively termed EoCP-1 and EoCP-2, were purified to homogeneity. Upon SDS-PAGE analysis, these chemotaxins showed molecular masses near 8 kD. NH2-terminal amino acid sequence analysis revealed identical sequences for both EoCP-1 and EoCP-2, which are also identical to that of RANTES, a cytokine that structurally belongs to the interleukin 8 superfamily of leukocyte selective attractants, and that is known to be a "memory-type" T lymphocyte-selective attractant. In the major Eo chemotaxin, EoCP-1, the residues 4 and 5, which in EoCP-2 were found to be serine residues, could not be identified. Electrospray mass spectrometry (ESP-MS) of EoCPs revealed for EoCP-2 a molecular mass of 7,862.8 +/- 1.1 daltons, which is 15.8 mass units higher than the calculated value of RANTES, indicating that EoCP-2 is identical to the full-length cytokine, and oxygenation, probably at methionine residue number 64, has taken place. Upon ESP-MS, EoCP-1 showed an average molecular mass of 8,355 +/- 10 daltons, suggesting O-glycosylation at these serine residues. Both natural forms of RANTES showed strong Eo-chemotactic activity (ED50 = 2 nM) with optimal chemotactic migration at concentrations near 10 nM, however, there were no significant migratory responses with human neutrophils. Chemotactic activity of RANTES for human Eos could be confirmed using recombinant material, which has been found to be as active as the natural forms. Since RANTES gene expression has been detected in activated T lymphocytes, and recombinant RANTES was shown to be a "memory" T lymphocyte-selective attractant, it is now tempting to speculate about an important role of RANTES in clinical situations such as allergene-induced late-phase skin reactions in atopic subjects or asthma, where in affected tissues both memory T cells and Eos are characteristic.

Amino Acid Sequence↗
PubMed1989

Murine membrane inhibitor of complement which accelerates decay of human C3 convertase.

A membrane protein of MW 60,000 was purified from mouse erythrocytes. This protein inhibits generation of mouse complement C3/C5 convertases on antibody-sensitized rabbit erythrocytes, in a haemolytic assay system using guinea-pig serum diluted in EDTA as the source of C3 to C9. This protein also has the capacity to accelerate the decay of human C3 convertase of the classical complement pathway. Antibody to this membrane protein also reacted with peripheral blood mononuclear cells and spleen cells, as observed by fluorescent flow cytometry analysis. Since the reactivity of these cells to the antibody was reduced by treatment with phosphatidyl inositol-specific phospholipase C (PIPLC), it is suggested that the protein is attached to the membrane via a glycophospholipid anchor. Based on these results, we conclude that this membrane protein is a murine homologue of human decay-accelerating factor (DAF).

Animals↗