Reversible expression of tryptases and chymases in the jejunal mast cells of mice infected with Trichinella spiralis.
It is has been established that mouse mast cells (MCs) can reversibly alter their expression of serglycin proteoglycans and the homologous granule chymases that have been designated mouse MC protease (mMCP)-1, mMCP-2, and mMCP-5 in vivo. Nevertheless, it remained to be determined whether these immune cells could modify their expression of other chymases and the granule tryptases mMCP-6 and mMCP-7. As assessed immunohistochemically, we now show that MCs reversibly change their expression of the recently described chymase mMCP-9 and both tryptases as these cells traverse the jejunum during the amplification and regression stages of the reactive MC hyperplasia. In noninfected mice, most jejunal MCs reside in the submucosa and express mMCP-6 and mMCP-7, but not mMCP-9 or the chymase mMCP-2. During the inductive phase of the helminth-induced inflammation, when the jejunal MCs move from the submucosa to the tips of the villus, the MCs briefly express mMCP-9, cease expressing mMCP-6 and mMCP-7, and then express mMCP-2. During the recovery phase of the inflammation, jejunal MCs cease expressing mMCP-2 and then express varied combinations of mMCP-6, mMCP-7, and mMCP-9 as they move from the tips of the villus back toward the submucosa. In other model systems, mMCP-6 elicits neutrophil extravasation, and mMCP-7 regulates fibrin deposition and fibrinogen-mediated signaling events. Thus, the ability of a jejunal MC to reversibly alter its tryptase expression during an inflammatory event has important functional implications.
Friend
D S
DS
Department of Pathology, Harvard Medical School, Boston, MA 02115, USA.
Ghildyal
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N
Gurish
M F
MF
Hunt
J
J
Hu
X
X
Austen
K F
KF
Stevens
R L
RL
D000818:Animals; D002452:Cell Count; D053818:Chymases; D006965:Hyperplasia; D007579:Jejunal Diseases / Q000201:enzymology* / Q000209:etiology / Q000473:pathology; D007583:Jejunum / Q000201:enzymology* / Q000473:pathology; D008407:Mast Cells / Q000201:enzymology* / Q000473:pathology; D051379:Mice; D008807:Mice, Inbred BALB C; D012697:Serine Endopeptidases / Q000096:biosynthesis*; D017160:Trichinella spiralis / Q000276:immunology*; D014235:Trichinellosis / Q000201:enzymology / Q000209:etiology / Q000473:pathology; D053802:Tryptases
C509190:Tpsb2 protein, mouse; D012697:Serine Endopeptidases; C083294:chymase 2; D053818:Chymases; C509229:Cma2 protein, mouse; C509222:Tpsab1 protein, mouse; D053802:Tryptases