Aminopeptidase interference in the assay of muscle cathepsin H

1991 ◽  
Vol 54 (4) ◽  
pp. 651-653 ◽  
Author(s):  
Elías Rico ◽  
Fidel Toldrá ◽  
José Flores
Keyword(s):  
Cathepsin H

scholarly journals Cathepsin H functions as an aminopeptidase in secretory vesicles for production of enkephalin and galanin peptide neurotransmitters

2012 ◽  
Vol 122 (3) ◽  
pp. 512-522 ◽  
Author(s):  
Weiya Douglas Lu ◽  
Lydiane Funkelstein ◽  
Thomas Toneff ◽  
Thomas Reinheckel ◽  
Christoph Peters ◽  
...  
Keyword(s):  
Secretory Vesicles ◽  
Cathepsin H

scholarly journals In vitro effects of L-arginine on lysosomal cysteine proteases activity in isolated experiment and in the state of oxidative stress

2015 ◽  
Vol 96 (5) ◽  
pp. 876-882
Author(s):  
M A Fomina ◽  
A M Kudlaeva
Keyword(s):  
Oxidative Stress ◽  
Sucrose Solution ◽  
Membrane Damage ◽  
Cysteine Proteases ◽  
Lysosomal Membranes ◽  
In Vitro Incubation ◽  
Cathepsin H ◽  
Lysosomal Cysteine Proteases ◽  
Stimulation Of

Aim. Assessment of direct influence of arginine on lysosomal cysteine proteases activity in vitro, in isolation as well as the stimulation of oxidative stress. Methods. The study was conducted on the 72 female conventional mature Wistar rats 280-320 g divided into 6 series of 12 rats each. Lysosome slurries were isolated from the liver of intact animals with a subsequent in vitro incubation in a sucrose solution, in the presence of L-arginine, as well as in the presence of L-arginine accompanied by the stimulation of oxidative stress. Samples of control groups were exposed in vitro with the addition of isolate and oxidant, respectively. Each batch was reproduced three times, incubation was performed at 37 °C in a water bath for 1, 2 and 4 hours. The activity of cathepsins B, L and H was studied using spectrofluorimetric method in two fractions - intra- and extralysosomal. Acid phosphatase activity was used as the main marker of membrane labialization. Results. One hour Incubation with 5 mM arginine in vitro led to inhibition of the cathepsin H activity and lysosomal membrane damage, however, further increase in incubation time led to its stabilization. In vitro exposure to 5 mM H2O2 caused an increase in activity of cathepsines B and L and the drop in the cathepsin H activity without obvious changes in the distribution of enzymes between extra and intralysosomal fractions. In a state of oxidative stress 2-hour in vitro incubation with 5 mM arginine reduced the permeability of lysosomal membranes for cathepsines B, H and L; while 4-hour incubation led to the destabilization of lysosomal membranes. Conclusion. The direct effect of arginine at a concentration of 5 mM within the 1,2 and 4-hour time intervals leads to a distinct change as a lysosomal cysteine protease activity and stability of lysosomal membranes.

Cimaterol reduces cathepsin activities but has no anabolic effect in cultured myotubes

1990 ◽  
Vol 259 (6) ◽  
pp. E822-E827 ◽  
Author(s):  
D. M. Bechet ◽  
A. Listrat ◽  
C. Deval ◽  
M. Ferrara ◽  
J. F. Quirke
Keyword(s):  
Cathepsin B ◽  
Direct Action ◽  
Cathepsin L ◽  
Beta Agonist ◽  
Maximum Effect ◽  
Detectable Effect ◽  
Beta Agonists ◽  
Cathepsin H ◽  
Cultured Myotubes ◽  
Beta Adrenergic Agonist

The effect of the beta-adrenergic agonist cimaterol on bovine and chicken primary myotubes was assessed. Cimaterol at 10-100 nM concentrations reduced cathepsin B benzyloxy-carbonyl-Arg-Arg-4-methyl-7-coumarylamide hydrolyzing activity, as well as benzyloxycarbonyl-Phe-Arg-4-methyl-7-coumarylamide hydrolysis, which is a substrate for both cathepsin B and cathepsin L. Maximum effect was observed after 6-16 h treatment. Cathepsin H Arg-4-methyl-7-coumarylamide hydrolyzing activity was low and not significantly affected by cimaterol treatment. Despite decreasing cathepsin activities, cimaterol also increased proteolysis rates but induced no detectable effect on protein synthesis rates. These observations suggest that beta-agonists, as a result of a direct action on muscle, can decrease cathepsin activities but that beta-agonist-induced muscle hypertrophy may not be due to a direct effect on muscle cells.

scholarly journals Sodium salicylate activates cathepsin B but not cathepsin H from rat spleen

1984 ◽  
Vol 36 ◽  
pp. 49
Author(s):  
Kenji Yamamoto ◽  
Masahiro Tatsumi ◽  
Mitsue Takeda ◽  
Hisako Yamamoto ◽  
Osamu Kamata ◽  
...  
Keyword(s):  
Cathepsin B ◽  
Sodium Salicylate ◽  
Cathepsin H

Cathepsin B, Cathepsin H, Cathepsin X and Cystatin C in Sera of Patients with Early-Stage and Inflammatory Breast Cancer

2008 ◽  
Vol 23 (3) ◽  
pp. 161-168 ◽  
Author(s):  
J. Decock ◽  
N. Obermajer ◽  
S. Vozelj ◽  
W. Hendrickx ◽  
R. Paridaens ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Cystatin C ◽  
Inflammatory Breast Cancer ◽  
Tumor Size ◽  
Cathepsin B ◽  
Early Stage ◽  
Menopausal Status ◽  
Preoperative Serum ◽  
Cathepsin H ◽  
Cathepsin X

Numerous studies have linked cathepsins and their inhibitor cystatin C to tumor invasion and metastasis. We examined whether cathepsin B, cathepsin H, cathepsin X and cystatin C could be detected in sera from women with early-stage or inflammatory breast cancer and whether they correlated with clinicopathological characteristics. Preoperative serum was obtained from 176 patients with early-stage breast cancer (tumor size <5 cm, negative lymph nodes) and 31 patients with inflammatory breast cancer. Cathepsin and cystatin C levels were measured by ELISA. The patient and tumor characteristics under study were age at diagnosis, menopausal status, tumor size, tumor grade, and steroid hormone receptor status. Serum cathepsin B levels were significantly lower in patients with poorly differentiated tumors. High cystatin C levels were associated with tumor size, postmenopausal status and patient age. Interestingly, significantly lower levels of cathepsin X and H were found in patients with inflammatory breast cancer, a trend also observed for cathepsin B and cystatin C. In conclusion, our results show a limited association of cathepsins B, H, X and cystatin C with established prognostic parameters. These data are promising and encourage future analysis of the clinical outcome of our patients in order to examine the potential prognostic value of these biomarkers. Further, this study indicates a role for cathepsin X and H in inflammatory breast cancer.

Expression and the role of cathepsin H in human glioma progression and invasion

1996 ◽  
Vol 104 (1) ◽  
pp. 121-126 ◽  
Author(s):  
Marupudi Sivaparvathi ◽  
Raymond Sawaya ◽  
Ziya L. Gokaslan ◽  
Kumar S. Chintala ◽  
Jasti S. Rao
Keyword(s):  
Human Glioma ◽  
Cathepsin H ◽  
Glioma Progression

scholarly journals Histochemical examination on principal collagen fibers in periodontal ligaments of ascorbic acid-deficient ODS-od/od rats

Microscopy ◽  
2019 ◽  
Vol 68 (5) ◽  
pp. 349-358 ◽  
Author(s):  
Tomoka Hasegawa ◽  
Yukina Miyamoto-Takasaki ◽  
Miki Abe ◽  
Zixuan Qiu ◽  
Tomomaya Yamamoto ◽  
...  
Keyword(s):  
Ascorbic Acid ◽  
Acid Solution ◽  
Collagen Fibers ◽  
Collagen Fibrils ◽  
Male Rats ◽  
Control Group ◽  
Ascorbic Acid Solution ◽  
Cathepsin H ◽  
Periodontal Ligaments

Abstract In this study, we aimed to clarify the role of ascorbic acid in collagen synthesis in periodontal ligaments using osteogenic disorder Shionogi (ODS)/ShiJcl-od/od rats lacking L-gulonolactone oxidase. These rats cannot synthesize ascorbic acid in vivo. Eight-week-old ODS/ShiJcl-od/od male rats were administered ascorbic acid solution at a concentration of 200 mg/dL (control group, n = 6) or ascorbic acid solution at concentration of 0.3 mg/dL (insufficient group, n = 12). Six rats of the insufficient group were then given with ascorbic acid solution at concentration of 200 mg/dL for additional 3 weeks (rescued group, n = 6), and then, their mandibles were histochemically examined. Consequently, the insufficient group specimens were seen to possess fewer collagen fibers, and silver impregnation revealed numerous fine, reticular fiber-like fibrils branching off from collagen in the periodontal ligaments. In control group, faint immunoreactivities for matrix metalloproteinase (MMP)2 and cathepsin H were seen in the periphery of blood vessels and throughout the ligament, respectively. In contrast, in the insufficient group, intense MMP2-immunoreactivity was observed to be associated with collagen fibrils in the periodontal ligaments, and cathepsin H-immunopositivity was seen in ligamentous cells. The rescued group showed abundant collagen fibers filling the periodontal ligament space. Under transmission electron microscopy, ligamentous fibroblasts incorporated collagen fibrils into tubular endosomes/lysosomes while simultaneously synthesizing collagen fibril bundles. Thus, ascorbic acid insufficiency affected the immunolocalization of cathepsin H and MMP2; however, ligamentous fibroblasts appear to possess the potential to synthesize collagen fibers when supplied with ascorbic acid.

scholarly journals Cathepsin H Mediates the Processing of Talin and Regulates Migration of Prostate Cancer Cells

2012 ◽  
Vol 288 (4) ◽  
pp. 2201-2209 ◽  
Author(s):  
Zala Jevnikar ◽  
Matija Rojnik ◽  
Polona Jamnik ◽  
Bojan Doljak ◽  
Urša Pečar Fonović ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Cancer Cells ◽  
Prostate Cancer Cells ◽  
Cathepsin H
Sign in / Sign up

Export Citation Format

Share Document