Surface morphology of rat peritoneal mast cells during in vitro regeneration after histamine secretion

1981 ◽  
Vol 216 (3) ◽  
Author(s):  
Peter Bytzer ◽  
EllenHolm Nielsen ◽  
J�rgen Clausen
2002 ◽  
Vol 15 (3) ◽  
pp. 233-238 ◽  
Author(s):  
E. Brzezińska-Blaszczyk ◽  
M. Wasiela

Sixteen strains of physiological and pathological vaginal bacteria were tested for their ability to secrete histamine from rat peritoneal mast cells in vitro. We noticed that Mycoplasma hominis -induced histamine release was very high (up to 53.6%). The stimulation of rat mast cells with Staphylococccus cohnii, Staphylococcus coagulase(-) (two strains), Ureaplasma urealyticum, Peptostreptococcus spp., Bacteroides capillosus, Staphylococcus aureus and Streptococcus agalactiae resulted in lower, but significant histamine secretion (11.2%–17.5%). Other bacterial strains ( Staphylococcus epidermidids, Enterococcus faecalis, Escherichia coli, Actinomyces naeslundii (two strains) and Lactobacillus fermentum (two strains) caused very low (4.2 % – 8.8%) histamine release.


1979 ◽  
Vol 178 (3) ◽  
pp. 681-687 ◽  
Author(s):  
Shamshad Cockcroft ◽  
Bastien D. Gomperts

Histamine secretion and phosphatidylinositol turnover were compared in antigen-sensitized rat peritoneal mast cells stimulated with a number of different ligands. A small and variable increase in the incorporation of [32P]Pi and of [3H]inositol into phosphatidylinositol was observed when the cells were treated with immunoglobulin E-directed ligands (antigens and concanavalin A), and this was accompanied by a low amount of secretion (<10% of total cell histamine). In the presence of added phosphatidylserine, the addition of immunoglobulin E-directed ligands invariably led to an enhanced rate (approx. 4-fold) of labelling of phosphatidylinositol and, in the presence of Ca2+, this was accompanied by the secretion of histamine. The labelling of phosphatidylinositol and histamine secretion were also stimulated by chymotrypsin and compound 48/80. Whereas the phosphatidylinositol response did not require the presence of extracellular Ca2+, the secretion of histamine was either enhanced or dependent on extracellular Ca2+ (depending on the ligand used). The dependence on ligand concentration for the phosphatidylinositol response and histamine secretion were similar. The increased isotopic incorporation into phosphatidylinositol continued for about 1h although histamine secretion (elicited with concanavalin A) stopped within 2min. These results support the proposition that metabolic events involving phosphatidylinositol play a necessary intermediate role in the regulation of Ca2+ channels by ligand-activated receptors.


1972 ◽  
Vol 20 (11) ◽  
pp. 917-922 ◽  
Author(s):  
DAVID I. WILKINSON ◽  
DAVID GLICK

In an attempt to clarify the question of whether histidine is stored in the mast cell for coversion to histamine or whether the rate of conversion is rapid enough to prevent accumulation of histidine so that the rate-limiting step is the histidine uptake, it was found that no histidine was demonstrable in rat peritoneal mast cells by either quantitative analysis or paper chromatographic detection. Microadaptation of Hassall's method, based on conversion of l-histidine by histidase to urocanic acid and measurement of the latter by its absorbance at 277 nm, was made to permit determination of histidine in nanogram amounts in the presence of histamine. This adaptation was found reliable when compared with the o-phthalaldehyde method in estimation of l-histidine in serum and in insulin hydrolysate, and then it was applied to analysis of mast cells before and after l-histidine uptake in vitro. The adaptation should be generally useful in microanalysis of l-histidine in histologically and cytologically defined samples.


1986 ◽  
Vol 35 (12) ◽  
pp. 1939-1942 ◽  
Author(s):  
Giuliana Decorti ◽  
Fiora Bartoli Klugmann ◽  
Luigi Candussio ◽  
Luciano Baldini

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