Tryptase is a neutral serine protease with a molecular weight of 134 kDa and a tetrameric structure consisting of non-covalently
نویسندگان
چکیده
Tryptase is a serin protease stored in mast cell granules that has recently been found to be involved in tumor angiogenesis. Data from experimental tumor models have suggested that prior to the onset of angiogenesis mast cells were accumulated near tumor cells and were required for the macroscopic expansion and metastatic spread of primary tumor cells. Hepatocellular cancer (HCC) is a well-established, highly angiogenesis-dependent hypervascular tumor. The aim of this preliminary study was to assess tryptase serum levels in 30 HCC patients prior and subsequent to hepatic transarterial chemoembolization (TACE). In this study, patients with intermediate stage (B) HCC, according to the Barcelona Clinic Liver Cancer (BCLC) staging classification, were enrolled. Additional patient features were adequate liver functional reserve and A or B status, according to the Child-Pugh classification. Tryptase levels were measured using the UniCAP-Tryptase fluoroimmunoassay. TACE was performed by loading doxorubicin on microspheres. The mean ± standard deviation (SD) tryptase level pre-TACE was 7.74±3.62 μg/l, and post-TACE 4.67±2.79 μg/l. A statistically significant difference (P<0.001) was detected, using the Student's t-test, between preand post-TACE tryptase level concentrations. No correlations were found between tryptase levels and other important clinicopathological features of patients. This is the first preliminary study analyzing the potential significance of serum tryptase levels in HCC patients. The results demonstrated higher serum tryptase levels in HCC patients, suggesting tryptase release from HCC tissue. As expected, after TACE, serum tryptase levels were decreased. Therefore, we suggested that tryptase was a potential biomarker of response to TACE treatment in HCC patients.
منابع مشابه
A novel low molecular weight extracellular protease from a moderately halophilic bacterium Salinivibrio sp. strain MS-7: production and biochemical properties
Kinetics of bacterial growth and protease production were monitored on a novel isolated moderately halophilic bacterium, Salinivibrio sp. strain MS-7, and maximum growth and protease activity was achieved after 48 hours at 30°C and 180 rpm. To determine the effect of various carbon sources on protease production, glucose, lactose, sucrose and maltose were investigated and maximum production of...
متن کاملCloning and Enhanced Expression of an Extracellular Alkaline Protease from a Soil Isolate of Bacillus clausii in Bacillus subtilis
in the detergent industry. In this study, the extracellular alkaline serine protease gene, aprE, from Bacillusclausii was amplified by PCR and further cloned and expressed in B. subtilis WB600 using the pWB980 expression vector. Protease activity of the recombinant B. subtilis WB600 harboring the plasmid pWB980/aprEreached up to 1020 U/ml, approximately 3-folds higher than the nativ...
متن کاملThe B12 anti-tryptase monoclonal antibody disrupts the tetrameric structure of heparin-stabilized beta-tryptase to form monomers that are inactive at neutral pH and active at acidic pH.
The novel tetrameric structure of human beta-tryptase faces each active site into the central pore, thereby restricting access of most biologic protease inhibitors. The mechanism by which the anti-tryptase mAb B12 inhibits human beta-tryptase peptidase and proteolytic activities at neutral pH, but augments proteolytic activity at acidic pH, was examined. At neutral pH, B12-beta-tryptase complex...
متن کاملThe kininogenase activity of human mast cell tryptase.
Tryptase is a tetrameric serine protease [l] which is present almost exclusively in the secretory granules of mast cells [2]. There has been some controversy over the extent to which tryptase may contribute to the generation of kinins which has been reported following mast cell activation [3,4]. Earlier studies suggested that tryptase does not generate bradykinin from either low molecular weigh...
متن کاملRECOMBINANT HUMAN TRYPTASE Recombinant Human Tryptase (rhTryptase; Cat.# G7061) is expressed as a fully active mature enzyme in Pichia pastoris by methanol induction and is purified from the supernatant using affinity chromatography
Tryptase, a 135kDa tetrameric serine protease, was originally isolated from lung mast cells (MC). This enzyme is stored in and released from MC granules upon activation. Tryptase is an exquisite marker in heterogeneous populations of MC, allowing for their differentiation from basophils. Because tryptase is the principal protein mediator component of mast cell granules, accounting for 23% of th...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
دوره شماره
صفحات -
تاریخ انتشار 2013