Key Specifications Table
|Species Reactivity||Key Applications||Host||Format||Antibody Type|
|H||DB, IHC||M||Biotin||Monoclonal Antibody|
|Safety Information according to GHS|
|Storage and Shipping Information|
|Storage Conditions||Maintain at 2-8°C in undiluted aliquots for up to 12 months from date of receipt.|
|Material Size||100 µg|
|Reference overview||Pub Med ID|
|Phenotypic change and accumulation of smooth muscle cells in strictures in Crohn's disease: relevance to local angiotensin II system.|
Takehisa Suekane,Yoshihiro Ikura,Kenji Watanabe,Junko Arimoto,Yoko Iwasa,Yoshimi Sugama,Soichiro Kayo,Kenichi Sugioka,Takahiko Naruko,Kiyoshi Maeda,Kosei Hirakawa,Tetsuo Arakawa,Makiko Ueda
Journal of gastroenterology 45 2010
Intestinal stricture lesions in Crohn's disease are characterized as submucosal fibromuscular accumulation. There has been a controversy about whether the fibrogenic cells in stricture lesions in Crohn's disease originate from a smooth muscle cell or a fibroblast lineage. In the present study, we aimed to elucidate: (1) the origin of the fibrogenic cells in stricture lesions; and (2) the roles of the local angiotensin II system, including mast cell chymase, in stricture formation.
|Critical role of mast cell chymase in mouse abdominal aortic aneurysm formation.|
Sun, J; Zhang, J; Lindholt, JS; Sukhova, GK; Liu, J; He, A; Abrink, M; Pejler, G; Stevens, RL; Thompson, RW; Ennis, TL; Gurish, MF; Libby, P; Shi, GP
Circulation 120 973-82 2009
Mast cell chymase may participate in the pathogenesis of human abdominal aortic aneurysm (AAA), yet a direct contribution of this serine protease to AAA formation remains unknown.Human AAA lesions had high numbers of chymase-immunoreactive mast cells. Serum chymase level correlated with AAA growth rate (P=0.009) in a prospective clinical study. In experimental AAA produced by aortic elastase perfusion in wild-type (WT) mice or those deficient in the chymase ortholog mouse mast cell protease-4 (mMCP-4) or deficient in mMCP-5 (Mcpt4(-/-), Mcpt5(-/-)), Mcpt4(-/-) but not Mcpt5(-/-) had reduced AAA formation 14 days after elastase perfusion. Even 8 weeks after perfusion, aortic expansion in Mcpt4(-/-) mice fell by 50% compared with that of the WT mice (P=0.0003). AAA lesions in Mcpt4(-/-) mice had fewer inflammatory cells and less apoptosis, angiogenesis, and elastin fragmentation than those of WT mice. Although Kit(W-sh/W-sh) mice had protection from AAA formation, reconstitution with mast cells from WT mice, but not those from Mcpt4(-/-) mice, partially restored the AAA phenotype. Mechanistic studies suggested that mMCP-4 regulates expression and activation of cysteine protease cathepsins, elastin degradation, angiogenesis, and vascular cell apoptosis.High chymase-positive mast cell content in human AAA lesions, greatly reduced AAA formation in Mcpt4(-/-) mice, and significant correlation of serum chymase levels with human AAA expansion rate suggests participation of mast cell chymase in the progression of human and mouse AAA.
|Mast cells in diffuse large B-cell lymphoma; their role in fibrosis.|
H Fukushima, M Ohsawa, Y Ikura, T Naruko, Y Sugama, T Suekane, C Kitabayashi, T Inoue, M Hino, M Ueda
Histopathology 49 498-505 2006
AIMS: Mast cells (MCs) are associated with fibrosis in various diseases. MCs comprise two phenotypes: the MC(TC) phenotype contains tryptase and chymase, whereas the MC(T) phenotype contains tryptase. Interleukin (IL)-4 promotes the development of MC(TC) from the MC(T) phenotype. The aim of this study was to determine the relationship between MC phenotypes and fibrosis in diffuse large B-cell lymphoma (DLBCL). METHODS AND RESULTS: We examined the distribution and density of MCs in 50 DLBCL and 20 reactive lymph nodes, and evaluated MC phenotypes and IL-4-expressing cells. To detect MCs, immunohistochemistry for tryptase and chymase was performed. The 50 DLBCLs were histologically divided into three groups: no fibrosis (32 cases), reticular type (eight cases) showing reticular fibrosis, and bundle type (10 cases) showing collagenous bundles. The density of tryptase-positive MCs was higher than that of chymase-positive MCs. The densities of tryptase-positive and chymase-positive MCs in fibrotic areas were significantly higher than those in the cellular areas in the reticular and bundle groups. Double immunostaining revealed that MCs in DLBCL comprised MC(T) and MC(TC) phenotypes. Chymase-positive MCs and T lymphocytes expressed IL-4. Although there were few chymase-positive MCs in reactive lymph nodes, the density of tryptase-positive MCs was not different from that in the 'no fibrosis' group. CONCLUSIONS: Tryptase-positive and chymase-positive MCs are associated with fibrosis in DLBCL.
|Highly increased numbers of leukocytes in inflamed gingiva from patients with HIV infection.|
Maung Myint, Svein Steinsvoll, Zuanning N Yuan, Berit Johne, Kristen Helgeland, Karl Schenck
AIDS (London, England) 16 235-43 2002
BACKGROUND: HIV infection increases susceptibility for marginal periodontitis, with horizontal and rapid loss of periodontal soft tissues and alveolar bone. OBJECTIVES: To examine whether numbers, distribution and some properties of mast cells, neutrophils and macrophages are normal in chronically inflamed gingiva of HIV-positive patients. METHODS: Gingival biopsies were stained for mast cell tryptase and chymase, neutrophil elastase, CD68, human transforming growth factor beta(1), HLA-DR, Fc gamma RI, Fc gamma RII and Fc gamma RIII and calprotectin. RESULTS: Patients at all stages of HIV infection showed radically increased numbers of mast cells and neutrophils throughout the connective tissue, and of macrophages below the oral gingival epithelium (P 0.05). CONCLUSION: HIV infection is associated with increased numbers of mast cells, macrophages and neutrophils in the chronic periodontal lesion. This may predispose for tissue destruction through the release of inflammatory mediators and effector molecules. The unusually heavy cell infiltrate throughout the gingival connective tissue may contribute to the diverging pattern of periodontal tissue loss in HIV-positive patients.
|Increased mast cells in hepatocellular carcinoma and intrahepatic cholangiocarcinoma|
Terada, T. and Matsunaga, Y.
J. Hepatology, 33:961-966 (2000) 2000
|A functional proteomics screen of proteases in colorectal carcinoma.|
McKerrow, JH; Bhargava, V; Hansell, E; Huling, S; Kuwahara, T; Matley, M; Coussens, L; Warren, R
Molecular medicine (Cambridge, Mass.) 6 450-60 2000
Proteases facilitate several steps in cancer progression. To identify proteases most suitable for drug targeting, actual enzyme activity and not messenger RNA levels or immunoassay of protein is the ideal assay readout.An automated microtiter plate assay format was modified to allow detection of all four major classes of proteases in tissue samples. Fifteen sets of colorectal carcinoma biopsies representing primary tumor, adjacent normal colon, and liver metastases were screened for protease activity.The major proteases detected were matrix metalloproteases (MMP9, MMP2, and MMP1), cathepsin B, cathepsin D, and the mast cell serine proteases, tryptase and chymase. Matrix metalloproteases were expressed at higher levels in the primary tumor than in adjacent normal tissue. The mast cell proteases, in contrast, were at very high levels in adjacent normal tissue, and not detectable in the metastases. Cathepsin B activity was significantly higher in the primary tumor, and highest in the metastases. The major proteases detected by activity assays were then localized in biopsy sections by immunohistochemistry. Mast cell proteases were abundant in adjacent normal tissue, because of infiltration of the lamina propria by mast cells. Matrix metalloproteases were localized to the tumor cells themselves; whereas, cathepsin B was predominantly expressed by macrophages at the leading edge of invading tumors. Although only low levels of urinary plasminogen activator were detected by direct enzyme assay, immunohistochemistry showed abundant protein within the tumor.This analysis, surveying all major classes of proteases by assays of activity rather than immunolocalization or in situ hybridization alone, serves to identify proteases whose activity is not completely balanced by endogenous inhibitors and which may be essential for tumor progression. These proteases are logical targets for initial efforts to produce low molecular weight protease inhibitors as potential chemotherapy.
|Mast cell subpopulations in the synovial tissue of patients with osteoarthritis: selective increase in numbers of tryptase-positive, chymase-negative mast cells.|
Buckley, M G, et al.
J. Pathol., 186: 67-74 (1998) 1998
Although there is relatively little evidence of inflammation in osteoarthritis (OA), increases in mast cell numbers and mast cell activation are prominent features of the synovial tissue. As little is known of the types of mast cells which may be involved, the numbers and distribution of mast cell subpopulations have been investigated as defined according to their content of proteases. Tissue was obtained from patients with OA undergoing total knee replacement surgery (n = 14) and from control subjects either post-mortem (n = 11) or following leg amputation for peripheral vascular disease (n = 3); a double-labelling immunocytochemical procedure with monoclonal antibodies specific for tryptase and chymase was applied to identify those mast cells which contain both tryptase and chymase (MCTC) and those with tryptase but not chymase (MCT). There was considerable variation between individual tissues and between sites of tissue sampling, but cells of the MCTC subset were predominant in the synovial layer of both groups of subjects without joint disease, accounting for some 60 per cent of all mast cells present. In tissue from OA patients, however, there appeared to have been a striking shift in the relative proportions of mast cells from the MCTC to the MCT phenotype, with many more MCT cells present in the synovial tissues of OA patients (median 53 MCT/mm2) than in tissue from post-mortem (7.5 MCT/mm2, P < 0.0001) or amputation controls (12 MCT/mm2). In contrast, numbers of synovial MCTC cells in the synovium of OA patients (20 MCTC/mm2) differed little from those in either of the control groups (both 12 MCTC/mm2). In several other conditions, the MCT cells have been linked with inflammatory events, but it seems that in OA, other factors may be operating to induce a selective expansion of this subpopulation.
|Fixation with Carnoy's fluid reduces the number of chymase-positive mast cells: not all chymase-positive mast cells are also positive for tryptase|
KleinJan, A. et al.
Allergy, 51:614-620 (1996) 1996
|Mast cells in cutaneous mastocytosis: accumulation of the MCTC type.|
Irani, A A, et al.
Clin. Exp. Allergy, 20: 53-8 (1990) 1990
Lesional (n = 15) and non-lesional (n = 10) skin of subjects with mastocytosis was analysed for the distribution and concentration of trypase positive, chymase negative mast cells (MCT) and tryptase positive, chymase positive mast cells (MCTC) cells and compared to normal skin (n = 23) and non-lesional skin of subjects with unexplained anaphylaxis or flushing episodes (n = 6). Skin biopsies were fixed in Carnoy's fluid and subjected to double immunohistochemical staining with biotinylated mouse monoclonal anti-chymase antibody followed by alkaline phosphatase-conjugated mouse monoclonal anti-tryptase antibody. MCTC cells were the only type of mast cells seen in all specimens analysed and in each case were more numerous in superficial compared to deep regions of dermis. The concentration (mean +/- s.d.) of mast cells in the superficial dermis of mastocytosis lesions (40 985 +/- 21 772 mast cells/mm3) was significantly increased over that in corresponding areas of non-lesional skin from subjects with mastocytosis (7178 +/- 3607 mast cells/mm3), skin from subjects with idiopathic anaphylaxis or flushing episodes (6974 +/- 3873 mast cells/mm3) and normal skin (7347 +/- 2973 mast cells/mm3). The exclusive presence of MCTC cells in skin lesions of mastocytosis which are characterized by non-malignant hyperplasia of mast cells suggests involvement of local tissue factors in mast cell recruitment and differentiation.
|Human conjunctival mast cells: distribution of MCT and MCTC in vernal conjunctivitis and giant papillary conjunctivitis|
Irani, A. et al.
J. Allergy Clin. Immunol., 86:34-39 (1990) 1990
|Anti-Chymase, Clone B7, Biotin Conjugated - Data Sheet|