scholarly journals Diacylglycerol metabolism in mast cells: a potential role in membrane fusion and arachidonic acid release.

1979 ◽  
Vol 150 (4) ◽  
pp. 1039-1044 ◽  
Author(s):  
D A Kennerly ◽  
T J Sullivan ◽  
P Sylwester ◽  
C W Parker

Purified rat peritoneal mast cells stimulated with the polycationic histamine-releasing agent compound 48/80 demonstrated a two- to four-fold increase in cellular levels of 1,2-diacylglycerol (DAG) within 1 min as detected by radioactive labeling and direct quantitation experiments. When 2-[1-14C]arachidonoyl-DAG was incubated in the presence of mast-cell homogenates, a rapid conversion to free arachidonate, and to a lesser extent, to monoacylglycerol, triglyceride, and phospholipid was observed. The release of arachidonate was proportional to the amount of broken-cell preparation added and the time of incubation, was prevented by preheating mast-cell preparations, and did not occur when 1-[1-14C]arachidonoyl-phosphatidylcholine was used as substrate, suggesting that the degradation was mediated by an enzyme with Dag-lipase activity. Although much work remains to be done to clarify the precise role of DAG in mast cells, DAG metabolism may be involved in secretion by generating substances which may faciliate membrane fusion and also in arachidonic acid-derived mediator formation by liberating esterified arachidonic acid from mast-cell lipids. Taken together, these studies indicate that the formation of DAG may play a central role in mast-cell function.

2008 ◽  
Vol 295 (5) ◽  
pp. C1427-C1433 ◽  
Author(s):  
Mariko Sakanaka ◽  
Satoshi Tanaka ◽  
Yukihiko Sugimoto ◽  
Atsushi Ichikawa

Accumulating evidence has indicated that mast cells can modulate a wide variety of immune responses. Migration and adhesion play a critical role in regulation of tissue mast cell function, in particular, under inflammatory conditions. We previously demonstrated that prostaglandin (PG) E2 stimulates adhesion of a mouse mastocytoma cell line, P-815, to the Arg-Gly-Asp (RGD)-enriched matrix through cooperation between two PGE2 receptor subtypes: EP3 and EP4 (Hatae N, Kita A, Tanaka S, Sugimoto Y, Ichikawa A. J Biol Chem 278: 17977–17981, 2003). We here investigated PGE2-induced adhesion of IL-3-dependent bone marrow-derived cultured mast cells (BMMCs). In contrast to the elevated cAMP-dependent adhesion of P-815 cells, EP3-mediated Ca2+ mobilization plays a pivotal role in PGE2-induced adhesion of BMMCs. Adhesion and Ca2+ mobilization induced by PGE2 were abolished in the Ptger3−/− BMMCs and were significantly suppressed by treatment with pertussis toxin, a phospholipase C inhibitor, U-73122, and a store-operated Ca2+ channel inhibitor, SKF 36965, indicating the involvement of Gi-mediated Ca2+ influx. We then investigated PGE2-induced adhesion of peritoneal mast cells to the RGD-enriched matrix. EP3 subtype was found to be the dominant PGE receptor that expresses in mouse peritoneal mast cells. PGE2 induced adhesion of the peritoneal mast cells of the Ptger3+/+ mice, but not that of the Ptger3−/− mice. In rat peritoneal mast cells, PGE2 or an EP3 agonist stimulated both Ca2+ mobilization and adhesion to the RGD-enriched matrix. These results suggested that the EP3 subtype plays a pivotal role in PGE2-induced adhesion of murine mast cells to the RGD-enriched matrix through Ca2+ mobilization.


1985 ◽  
Vol 127 (3) ◽  
pp. 726-732 ◽  
Author(s):  
Yukio Okano ◽  
Yasuhiro Ishizuka ◽  
Shigeru Nakashima ◽  
Toyohiko Tohmatsu ◽  
Hajime Takagi ◽  
...  

2014 ◽  
Vol 458 (2) ◽  
pp. 291-299 ◽  
Author(s):  
Nobuaki Higashi ◽  
Michihiko Waki ◽  
Mayumi Sue ◽  
Yusuke Kogane ◽  
Hiroaki Shida ◽  
...  

Connective tissue-type mast cells express heparin and heparanase in the secretory granules. Cleavage of granular heparin by heparanase accelerates release of granular components from collagen-based extracellular matrices. A size-dependent novel regulatory role of heparin for mast cell function is proposed.


1986 ◽  
Vol 236 (1) ◽  
pp. 215-219 ◽  
Author(s):  
G Struckhoff ◽  
E Heymann

Purified rat peritoneal mast cells have a 10-20-fold higher dipeptidyl peptidase II (DPP II) activity as compared with that of macrophages from the same source. Upon stimulation with the secretagogue Compound 48/80, DPP II is released from peritoneal-lavage cells and from purified mast cells, but not from purified macrophages, in a dose-dependent manner. Maximally, about one-third of the DPP II present in peritoneal-lavage cells is released. Substance P and the antigen/IgE system probably produce a similar effect. Both histamine and Zn2+, two ingredients of mast-cell granules, strongly inhibit DPP II at concentrations reported to occur in the granules. A possible role of mast-cell DPP II in the remodelling of connective tissue is discussed.


Allergy ◽  
2021 ◽  
Author(s):  
Lea Pohlmeier ◽  
Sanchaita Sriwal Sonar ◽  
Hans‐Reimer Rodewald ◽  
Manfred Kopf ◽  
Luigi Tortola

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