Immortalization of Mouse Bone Marrow-Derived Mast Cells with Ad12-SV40 Virus

1993 ◽  
Vol 100 (4) ◽  
pp. 319-327 ◽  
Author(s):  
Naveen Arora ◽  
Kyung-Up Min ◽  
John J. Costa ◽  
Johng S. Rhim ◽  
Dean D. Metcalfe
Keyword(s):  
Bone Marrow ◽  
Mast Cells ◽  
Mouse Bone Marrow ◽  
Sv40 Virus

Regulation of proliferation of mouse bone marrow-derived mast cells by activated fibroblasts

1996 ◽  
Vol 19 (5) ◽  
pp. 368-373
Author(s):  
Sung-Joo Park ◽  
Hyung-Ryong Kim ◽  
Hye-Won Cho ◽  
Hyung-Min Kim
Keyword(s):  
Bone Marrow ◽  
Mast Cells ◽  
Mouse Bone Marrow ◽  
Regulation Of Proliferation ◽  
Activated Fibroblasts

scholarly journals The immediate phase of c-kit ligand stimulation of mouse bone marrow-derived mast cells elicits rapid leukotriene C4 generation through posttranslational activation of cytosolic phospholipase A2 and 5-lipoxygenase.

1995 ◽  
Vol 182 (1) ◽  
pp. 197-206 ◽  
Author(s):  
M Murakami ◽  
K F Austen ◽  
J P Arm
Keyword(s):  
Bone Marrow ◽  
Arachidonic Acid ◽  
Mast Cells ◽  
Cell Membrane ◽  
Phospholipase A2 ◽  
Mouse Bone Marrow ◽  
Kit Ligand ◽  
Cytosolic Phospholipase ◽  
Delayed Phase ◽  
Stimulation Of

c-kit ligand (KL) activated mouse bone marrow-derived mast cells (BMMC) for the dose- and time-dependent release of arachidonic acid from cell membrane phospholipids, with generation of leukotriene (LT) C4 in preference to prostaglandin (PG)D2. KL at concentrations of 10 ng/ml elicited half-maximal eicosanoid generation and at concentrations of > 50 ng/ml elicited a maximal generation of approximately 15 ng LTC4 and 1 ng PGD2 per 10(6) cells, with 20% net beta-hexosaminidase release 10 min after stimulation. Of the other cytokines tested, none, either alone or in combination with KL, elicited or modulated the immediate phase of mediator release by BMMC, indicating strict specificity for KL. Activation of BMMC in response to KL was accompanied by transient phosphorylation of cytosolic phospholipase A2 and reversible translocation of 5-lipoxygenase to a cell membrane fraction 2-5 min after stimulation, when the rate of arachidonic acid release and LTC4 production were maximal. BMMC continuously exposed to KL in the presence of IL-10 and IL-1 beta generated LTC4 in marked preference to PGD2 over the first 10 min followed by delayed generation of PGD2 with no LTC4 over several hours. Pharmacologic studies revealed that PGD2 generation in the immediate phase depended on prostaglandin endoperoxide synthase (PGHS)-1 and in the delayed phase on PGHS-2. Thus, KL provided a nonallergic stimulus for biphasic eicosanoid generation by mast cells. The immediate phase is dominated by LTC4 generation with kinetics and postreceptor biosynthetic events similar to those observed after cell activation through the high affinity IgE receptor, whereas the delayed phase of slow and selective PGD2 production is mediated by induction of PGHS-2.

scholarly journals In vitro activation of the contact (Hageman factor) system of plasma by heparin and chondroitin sulfate E

Blood ◽  
1984 ◽  
Vol 63 (6) ◽  
pp. 1453-1459 ◽  
Author(s):  
Y Hojima ◽  
CG Cochrane ◽  
RC Wiggins ◽  
KF Austen ◽  
RL Stevens
Keyword(s):  
Bone Marrow ◽  
Mast Cells ◽  
Connective Tissue ◽  
Chondroitin Sulfate ◽  
Mouse Bone Marrow ◽  
Hageman Factor ◽  
In Vitro Activation ◽  
Chondroitin Sulfate E ◽  
Charged Macromolecules

Abstract A large number of negatively charged macromolecules, including DNA, glycosaminoglycans, and proteoglycans, were tested as possible activators of the contact (Hageman factor) system in vitro. Activation was assessed by conversion of prekallikrein to kallikrein, as determined by amidolytic assay and by cleavage of 125I-Hageman factor into 52,000- and 28,000-dalton fragments. Of particular interest to these studies, heparin proteoglycan and glycosaminoglycan from rat peritoneal mast cells, and squid chondroitin sulfate E, which is representative of the glycosaminoglycan from cultured mouse bone marrow derived mast cells, induced the reciprocal activation between Hageman factor and prekallikrein. In addition, naturally occurring heparin glycosaminoglycans from pig mucosa, bovine lung, and rat mast cells also induced activation. In contrast, native connective tissue matrix glycosaminoglycans and proteoglycans from several sources were inactive, although when one such chondroitin sulfate was further sulfated in vitro, it gained activity. When the negative charge of the activating agents was blocked by the addition of hexadimethrine bromide, the cleavage of 125I-Hageman factor in the presence of prekallikrein was prevented. The active negatively charged macromolecules induced cleavage of 125I-high molecular weight kininogen in normal plasma but not in Hageman factor-deficient or prekallikrein- deficient plasmas. Reconstitution of prekallikrein-deficient plasma with purified prekallikrein restored the kininogen cleavage upon addition of the active proteoglycans. These results suggest that both heparin from connective tissue mast cells and highly sulfated chondroitin sulfate E from cultured mouse bone marrow derived mast cells (which are considered synonomous with mucosal mast cells) could activate the contact system of plasma subsequent to an activation secretion response.

scholarly journals Regulation of Microtubule Nucleation in Mouse Bone Marrow-Derived Mast Cells by Protein Tyrosine Phosphatase SHP-1

Cells ◽  
2019 ◽  
Vol 8 (4) ◽  
pp. 345 ◽  
Author(s):  
Klebanovych ◽  
Sládková ◽  
Sulimenko ◽  
Vosecká ◽  
Čapek ◽  
...  
Keyword(s):  
Bone Marrow ◽  
Mast Cells ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Sh2 Domain ◽  
Negative Regulator ◽  
Mast Cell Activation ◽  
Mouse Bone Marrow ◽  
Microtubule Nucleation ◽  
Protein Tyrosine

The antigen-mediated activation of mast cells initiates signaling events leading to their degranulation, to the release of inflammatory mediators, and to the synthesis of cytokines and chemokines. Although rapid and transient microtubule reorganization during activation has been described, the molecular mechanisms that control their rearrangement are largely unknown. Microtubule nucleation is mediated by γ-tubulin complexes. In this study, we report on the regulation of microtubule nucleation in bone marrow-derived mast cells (BMMCs) by Src homology 2 (SH2) domain-containing protein tyrosine phosphatase 1 (SHP-1; Ptpn6). Reciprocal immunoprecipitation experiments and pull-down assays revealed that SHP-1 is present in complexes containing γ-tubulin complex proteins and protein tyrosine kinase Syk. Microtubule regrowth experiments in cells with deleted SHP-1 showed a stimulation of microtubule nucleation, and phenotypic rescue experiments confirmed that SHP-1 represents a negative regulator of microtubule nucleation in BMMCs. Moreover, the inhibition of the SHP-1 activity by inhibitors TPI-1 and NSC87877 also augmented microtubule nucleation. The regulation was due to changes in γ-tubulin accumulation. Further experiments with antigen-activated cells showed that the deletion of SHP-1 stimulated the generation of microtubule protrusions, the activity of Syk kinase, and degranulation. Our data suggest a novel mechanism for the suppression of microtubule formation in the later stages of mast cell activation.

Insulin potentiates FcɛRI-mediated signaling in mouse bone marrow-derived mast cells

2010 ◽  
Vol 47 (5) ◽  
pp. 1039-1046 ◽  
Author(s):  
Alexander Kettner ◽  
Mario Di Matteo ◽  
Angela Santoni
Keyword(s):  
Bone Marrow ◽  
Mast Cells ◽  
Mouse Bone Marrow

Characterization of a functional relationship between hepatocyte growth factor and mouse bone marrow-derived mast cells

1999 ◽  
Vol 65 (1) ◽  
pp. 27-42 ◽  
Author(s):  
Christine C. Fehlner-Gardiner ◽  
Henian Cao ◽  
Linda Jackson-Boeters ◽  
Toshikazu Nakamura ◽  
Bruce E. Elliott ◽  
...  
Keyword(s):  
Bone Marrow ◽  
Growth Factor ◽  
Mast Cells ◽  
Hepatocyte Growth Factor ◽  
Functional Relationship ◽  
Mouse Bone Marrow ◽  
Hepatocyte Growth

Responses during cell preparation for functional analyses in mouse bone marrow-derived cultured mast cells

2005 ◽  
Vol 238 (1) ◽  
pp. 49-55 ◽  
Author(s):  
Masaru Murakami ◽  
Teruo Ikeda ◽  
Yoshii Nishino ◽  
Masayuki Funaba
Keyword(s):  
Bone Marrow ◽  
Mast Cells ◽  
Mouse Bone Marrow ◽  
Cell Preparation ◽  
Functional Analyses
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