Altered storage of proteases in mast cells from mice lacking heparin: a possible role for heparin in carboxypeptidase A processing.
about
Active monomers of human beta-tryptase have expanded substrate specificitiesMast cell proteoglycansSerglycin-deficient cytotoxic T lymphocytes display defective secretory granule maturation and granzyme B storageSerglycin is the major secreted proteoglycan in macrophages and has a role in the regulation of macrophage tumor necrosis factor-alpha secretion in response to lipopolysaccharidePromiscuous processing of human alphabeta-protryptases by cathepsins L, B, and CPolyamines are present in mast cell secretory granules and are important for granule homeostasis.Mast cell protease 5 mediates ischemia-reperfusion injury of mouse skeletal muscleSerglycin-independent release of active mast cell proteases in response to Toxoplasma gondii infection.Intracellular proteoglycans.Molecular mechanism of mast cell mediated innate defense against endothelin and snake venom sarafotoxinLowered expression of heparan sulfate/heparin biosynthesis enzyme N-deacetylase/n-sulfotransferase 1 results in increased sulfation of mast cell heparin.Loss of histochemical identity in mast cells lacking carboxypeptidase A.Serglycin proteoglycan is required for secretory granule integrity in mucosal mast cells.Heparan sulfate 6-O-sulfotransferase isoform-dependent regulatory effects of heparin on the activities of various proteases in mast cells and the biosynthesis of 6-O-sulfated heparin.Mast cell cathepsins C and S control levels of carboxypeptidase A and the chymase, mouse mast cell protease 5.A novel role for antizyme inhibitor 2 as a regulator of serotonin and histamine biosynthesis and content in mouse mast cells.
P2860
Q24647729-CFAF5413-4A6D-4CA5-95DE-B2D1EECF1796Q27022107-E0711C9A-3BE0-49C8-880E-5513466EADD4Q28508375-D5438843-C789-4502-9C74-B2078901B917Q28513593-E6388CA9-7028-40A5-B2B6-31E51FE83F18Q30426444-AE3CFB6B-A029-4E88-93F8-F1B825A71E6BQ33769022-E38A91B5-D3A8-4AF9-BF2B-F4E3C2D1AB79Q34180540-9262A98F-2F15-4138-9A3A-CAA7B56E98A2Q34352022-E1CEF934-4520-4A1B-B703-7EBFC29AC416Q35647324-8B05A3A3-6A15-4235-911F-B718B168BC65Q36229090-27375F87-E313-431C-9607-7F8412E92B2DQ40041775-58C2EDA5-E786-4417-9E8E-646B0381FF8FQ41929285-A54C1E30-001A-4EB7-832C-5FE7C01F948CQ42912814-F24CFF7D-04B2-434F-A69F-796BC6F17251Q43215860-E099A2B2-F505-422B-A99B-983A8DD2CD8EQ44689341-F48AB496-8A0E-4620-9331-1321726FFD8CQ53120920-C6B64A4A-2597-4C4C-9B40-B34DDA981D5E
P2860
Altered storage of proteases in mast cells from mice lacking heparin: a possible role for heparin in carboxypeptidase A processing.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年学术文章
@wuu
2002年学术文章
@zh
2002年学术文章
@zh-cn
2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
@yue
2002年學術文章
@zh-hant
name
Altered storage of proteases i ...... carboxypeptidase A processing.
@en
Altered storage of proteases i ...... carboxypeptidase A processing.
@nl
type
label
Altered storage of proteases i ...... carboxypeptidase A processing.
@en
Altered storage of proteases i ...... carboxypeptidase A processing.
@nl
prefLabel
Altered storage of proteases i ...... carboxypeptidase A processing.
@en
Altered storage of proteases i ...... carboxypeptidase A processing.
@nl
P2093
P2860
P356
P1433
P1476
Altered storage of proteases i ...... carboxypeptidase A processing.
@en
P2093
Carolina Lunderius
Frida Henningsson
Gunnar Pejler
Lars Hellman
Maria Wilén
P2860
P304
P356
10.1515/BC.2002.083
P50
P577
2002-05-01T00:00:00Z