PMID- 2467915
OWN - NLM
STAT- MEDLINE
DCOM- 19890515
LR  - 20061115
IS  - 0730-2312 (Print)
IS  - 0730-2312 (Linking)
VI  - 38
IP  - 4
DP  - 1988 Dec
TI  - Biological functions of serine proteases in mast cells in allergic inflammation.
PG  - 291-301
AB  - Serine proteases in mast cell granules, such as chymase, atypical chymase, and 
      tryptase, which are major proteins in the granules, may play important roles in 
      the process of immunoglobulin E (IgE)-mediated degranulation and in 
      pathobiological alterations in tissues. Indeed, inhibitors of chymase, substrate 
      analogs, and antichymase F(ab')2, but not inhibitors of tryptase, markedly 
      inhibited histamine release induced by IgE-receptor bridging but not that induced 
      by Ca ionophore. In contrast, inhibitors of metalloprotease inhibited histamine 
      release induced not only by IgE-receptor bridging but also by Ca ionophore. These 
      results suggest that chymase and metalloprotease are involved at different steps 
      in the process of degranulation. The extents of inhibition of histamine release 
      were closely correlated with the amounts of the inhibitors of chymase accumulated 
      in the granules. After degranulation, the released proteases may in part 
      contribute to pathobiological alterations in allergic disorders through 
      generations of C3a anaphylatoxin and thrombin by human and rat tryptase, 
      respectively, and those of angiotensin II and a chemotactic factor of neutrophils 
      by human and rat chymase, respectively. Moreover, chymase and atypical chymase 
      from rat were shown to destroy type IV collagen, and human tryptase was found to 
      hydrolyze various plasma proteins, such as fibrinogen and high-molecular-weight 
      kininogen. The biological activities of tryptase and chymase from rat may be 
      regulated by their dissociation from and association with trypstatin, an 
      endogenous inhibitor of these proteases.
FAU - Katunuma, N
AU  - Katunuma N
AD  - Division of Enzyme Chemistry, University of Tokushima, Japan.
FAU - Kido, H
AU  - Kido H
LA  - eng
PT  - Journal Article
PT  - Review
PL  - United States
TA  - J Cell Biochem
JT  - Journal of cellular biochemistry
JID - 8205768
RN  - EC 3.4.21.- (Serine Endopeptidases)
RN  - EC 3.4.21.39 (Chymases)
SB  - IM
MH  - Animals
MH  - Chymases
MH  - Histamine Release
MH  - Humans
MH  - *Hypersensitivity
MH  - Inflammation
MH  - Mast Cells/*enzymology/immunology
MH  - Serine Endopeptidases/*physiology
RF  - 91
EDAT- 1988/12/01 00:00
MHDA- 1988/12/01 00:01
CRDT- 1988/12/01 00:00
PHST- 1988/12/01 00:00 [pubmed]
PHST- 1988/12/01 00:01 [medline]
PHST- 1988/12/01 00:00 [entrez]
AID - 10.1002/jcb.240380408 [doi]
PST - ppublish
SO  - J Cell Biochem. 1988 Dec;38(4):291-301. doi: 10.1002/jcb.240380408.