Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “ZYMOSAN”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 613 records · Page 34Linked to original sources
PubMed1985

Hydrocortisone and 'macrocortin' inhibit the zymosan-induced release of lyso-PAF from rat peritoneal leucocytes.

Hydrocortisone and the glucocorticoid-induced anti-phospholipase protein macrocortin, were tested as inhibitors of PAF generation. The steroid produced a dose-dependent inhibition of the release of the PAF precursor 2-lyso-PAF, and this effect was mimicked by affinity-purified macrocortin. Neither agent had any effect on the acetylation of lyso-PAF to PAF. Of other drugs tested only phospholipase inhibitors blocked lyso-PAF release and sulphydryl reagents blocked the acetylation step. It is concluded that glucocorticoids inhibit the generation of PAF and this could be an important component of their anti-anaphylactic and anti-inflammatory action.

Acetylation↗
PubMed1990

Abnormal zymosan-induced neutrophil chemiluminescence as a marker of depression.

Preliminary studies have shown that polymorphonuclear neutrophil (PMN) activity is decreased in a state-dependent manner in patients with endogenous depression. The present study investigates this finding in a larger group of psychiatric patients and attempts to determine the identification of the factor responsible for the abnormal neutrophil function. Chemiluminescence responses of PMNs from patients with diagnoses of endogenous depression, panic disorder, anxiety, schizophrenia and alcoholism were assessed concurrently with age- and sex-matched control subjects. The reduction in PMN activity was observed in panic disorder patients as well as during depression but remained normal in schizophrenia, alcoholism and generalised anxiety. The defect in PMN function appears to be related to an abnormal factor in the serum of the patient which is corrected on clinical recovery. Aspirin-inhibited prostaglandin synthesis resulted in an enhancement of PMN activity in healthy subjects, suggesting a possible role for prostaglandins in the abnormal PMN response.

Alcoholism↗
PubMed1994

The requirement of p47 phosphorylation for activation of NADPH oxidase by opsonized zymosan in human neutrophils.

Protein kinase C (PKC) inhibitors, staurosporine or 1,5-isoquinolinesulfonyl)-2-methylpiperazine (H7), inhibited NADPH oxidase activity and phosphorylation of 47 kDa protein (p47) in PMA-stimulated neutrophils in a dose-dependent manner. These PKC inhibitors, at the same doses, did not affect oxidase activity and caused only partial inhibition of p47 phosphorylation in OZ-stimulated neutrophils. There was residual (20%) phosphorylated p47 in the membranes of OZ-stimulated cells in the presence of PKC inhibitors, at concentrations which caused total inhibition of oxidase activity and p47 phosphorylation in PMA-stimulated neutrophils. In the presence of ionomycin, which increased intracellular calcium ion concentrations, staurosporine was less effective in inhibiting both superoxide generation and p47 phosphorylation stimulated by PMA, similar to its effect in OZ-stimulated cells. The results indicate that some phosphorylation of p47 always accompanied oxidase activation induced by PMA or OZ, though the degree of phosphorylation of membrane-bound p47 does not directly correlate with rates of superoxide production.

1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine↗
PubMed1993

Further studies on guinea pig Z-1 antigen that is involved in phagocytosis of zymosan by macrophages: cell type distribution of the antigen and cross-reactivity of anti-Z-1 with human cR3.

We have previously identified a heterodimer molecule, Z-1, on guinea pig peritoneal macrophages (M phi s) by the newly prepared monoclonal antibody, anti-Z-1, and Z-1 has been assumed to be the complement receptor type three (CR3) in this species. To clarify this assumption, the cell type distribution of the antigen in guinea pig and the cross-reactivity of anti-Z-1 with other species were analyzed. It was demonstrated that Z-1 was expressed on peritoneal M phi s, pulmonary M phi s, peritoneal polymorphonuclear leukocytes (PMN), peripheral neutrophils, and some subpopulations of spleen cells and of bone marrow cells, but not on erythrocytes, circulating lymphocytes, and lymphocytes in both spleen and bone marrow in detectable amounts. Thus the expression of Z-1 seems to be restricted to phagocytes as is CR3 of other species. Furthermore, it was found that anti-Z-1 bound with peripheral neutrophils from human, horse and goat and HL-60 cells differentiated into monocytes. Any cross-reactivity of the antibody was not detected with neutrophils from rabbit, cow, sheep and dog and nondifferentiated HL-60 cells. Human Z-1 was indistinguishable from human CR3, since both were the heterodimer consisting of alpha chain of 170 kDa (pI = 6.6-7.2) noncovalently associated with beta chain of 100 kDa (pI = 5.6-6.7). In addition, human CR3 in detergent-lysate of neutrophils was completely adsorbed with anti-Z-1 F(ab')2- Sepharose. These findings indicate that guinea pig Z-1 shares an antigenic determinant with human CR3. It thus seems to be possible that Z-1 may function as CR3 in guinea pigs.

Animals↗