Characteristics of anaphylaxis-inducing IgG immune complexes triggering murine passive systemic anaphylaxis

Allergy ◽  
2012 ◽  
Vol 68 (2) ◽  
pp. 236-245 ◽  
Author(s):  
D. Jiao ◽  
Y. Liu ◽  
X. Lu ◽  
Q. Pan ◽  
J. Zheng ◽  
...  
Keyword(s):  
Immune Complexes ◽  
Systemic Anaphylaxis ◽  
Passive Systemic Anaphylaxis

scholarly journals Fate of two mast cell tryptases in V3 mastocytosis and normal BALB/c mice undergoing passive systemic anaphylaxis: prolonged retention of exocytosed mMCP-6 in connective tissues, and rapid accumulation of enzymatically active mMCP-7 in the blood.

1996 ◽  
Vol 184 (3) ◽  
pp. 1061-1073 ◽  
Author(s):  
N Ghildyal ◽  
D S Friend ◽  
R L Stevens ◽  
K F Austen ◽  
C Huang ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Mast Cell ◽  
Mast Cells ◽  
Chromosome 17 ◽  
Macromolecular Complex ◽  
Connective Tissues ◽  
Systemic Anaphylaxis ◽  
Rich Domain ◽  
Passive Systemic Anaphylaxis ◽  
Mouse Mast Cell

The mouse mast cell protease granule tryptases designated mMCP-6 and mMCP-7 are encoded by highly homologous genes that reside on chromosome 17. Because these proteases are released when mast cells are activated, we sought a basis for distinctive functions by examining their fates in mice undergoing passive systemic anaphylaxis. 10 min-1 h after antigen (Ag) was administered to immunoglobulin (Ig)E-sensitized mice, numerous protease/proteoglycan macromolecular complexes appeared in the extracellular matrix adjacent to most tongue and heart mast cells of normal BALB/c mice and most spleen and liver mast cells of V3 mastocytosis mice. These complexes could be intensively stained by anti-mMCP-6 Ig but not by anti-mMCP-7 Ig. Shortly after Ag challenge of V3 mastocytosis mice, large amounts of properly folded, enzymatically active mMCP-7 were detected in the plasma. This plasma-localized tryptase was approximately 150 kD in its multimeric state and approximately 32 kD in its monomeric state, possessed an NH2 terminus identical to that of mature mMCP-7, and was not covalently bound to any protease inhibitor. Comparative protein modeling and electrostatic calculations disclosed that mMCP-6 contains a prominent Lys/Arg-rich domain on its surface, distant from the active site. The absence of this domain in mMCP-7 provides an explanation for its selective dissociation from the exocytosed macromolecular complex. The retention of exocytosed mMCP-6 in the extracellular matrix around activated tissue mast cells suggests a local action. In contrast, the rapid dissipation of mMCP-7 from granule cores and its inability to be inactivated by circulating protease inhibitors suggests that this tryptase cleaves proteins located at more distal sites.

scholarly journals Humanized mouse model of mast cell–mediated passive cutaneous anaphylaxis and passive systemic anaphylaxis

2016 ◽  
Vol 138 (3) ◽  
pp. 769-779 ◽  
Author(s):  
Paul J. Bryce ◽  
Rustom Falahati ◽  
Laurie L. Kenney ◽  
John Leung ◽  
Christopher Bebbington ◽  
...  
Keyword(s):  
Mast Cell ◽  
Mouse Model ◽  
Passive Cutaneous Anaphylaxis ◽  
Humanized Mouse ◽  
Humanized Mouse Model ◽  
Systemic Anaphylaxis ◽  
Passive Systemic Anaphylaxis

scholarly journals S1P4 Regulates Passive Systemic Anaphylaxis in Mice but Is Dispensable for Canonical IgE-Mediated Responses in Mast Cells

2018 ◽  
Vol 19 (5) ◽  
pp. 1279 ◽  
Author(s):  
Joseph Kulinski ◽  
Richard Proia ◽  
Elisabeth Larson ◽  
Dean Metcalfe ◽  
Ana Olivera
Keyword(s):  
Mast Cells ◽  
Systemic Anaphylaxis ◽  
Ige Mediated ◽  
Passive Systemic Anaphylaxis
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