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.

Species variations amongst proteinases in liver lysosomes

1986 ◽  
Vol 6 (11) ◽  
pp. 991-997 ◽  
Author(s):  
Daniel Béchet ◽  
Alain Obled ◽  
Christiane Deval
Keyword(s):  
Rat Liver ◽  
Cathepsin B ◽  
Species Differences ◽  
Cathepsin L ◽  
Cathepsin H ◽  
Liver Lysosomes

Cathepsin B, H, L and D activities in liver lysosomes were compared between species. Although cathepsin B and D were detected in bovine, pig, chicken and rat liver, striking species differences were evident for cathepsin H and L. Cathepsin L activity was particularly high in chicken lysosomal extracts, but could not be detected in bovine and pig extracts. Whereas there was no significant cathepsin H activity in bovine extracts, rat liver lysosomal extracts contained large amounts of cathepsin H activity.

scholarly journals Different immunolocalizations of cathepsins B, H, and L in the liver.

1985 ◽  
Vol 33 (11) ◽  
pp. 1173-1175 ◽  
Author(s):  
K Ii ◽  
K Hizawa ◽  
E Kominami ◽  
Y Bando ◽  
N Katunuma
Keyword(s):  
Horseradish Peroxidase ◽  
Kupffer Cells ◽  
Cathepsin B ◽  
Cathepsin L ◽  
Sinusoidal Cells ◽  
Dense Bodies ◽  
Cathepsin H ◽  
Normal Rat ◽  
Endogenous Proteins ◽  
First Time

Different localizations of cathepsin B, H, and L in normal rat liver were revealed immunohistochemically with anticathepsin Fab'-horseradish peroxidase conjugates. Staining of cathepsin B was strong in the periportal sinusoids, possibly in Kupffer cells; and weaker in panlobular hepatocytes. Staining of cathepsin H was strong in panlobular hepatocytes, especially in the periphery of the cytoplasm, possibly representing the peribiliary dense bodies; and weaker in periportal sinusoidal cells, possibly Kupffer cells. Staining of cathepsin L was strongest in centrilobular hepatocytes and weaker in periportal sinusoidal cells, possibly Kupffer cells. These findings, revealed for the first time in the present study, show that the histologic and intracellular localizations of the three cathepsins are different, suggesting that they have different roles in degradation of exogenous and endogenous proteins.

[41] Cathepsin B, cathepsin H, and cathepsin L

1981 ◽  
pp. 535-561 ◽  
Author(s):  
Alan J. Barrett ◽  
Heidrun Kirschke
Keyword(s):  
Cathepsin B ◽  
Cathepsin L ◽  
Cathepsin H

The cysteine proteinases of Schistosoma mansoni cercariae

Parasitology ◽  
1997 ◽  
Vol 114 (2) ◽  
pp. 105-112 ◽  
Author(s):  
J. P. DALTON ◽  
K. A. CLOUGH ◽  
M. K. JONES ◽  
P. J. BRINDLEY
Keyword(s):  
Schistosoma Mansoni ◽  
Cathepsin B ◽  
Cathepsin L ◽  
Serine Proteinase ◽  
Skin Penetration ◽  
Scanning Electron Micrographs ◽  
Cysteine Proteinases ◽  
Similar Function ◽  
Substrate Preferences ◽  
Serine Proteinase Activity

Based on substrate preferences, cercariae of Schistosoma mansoni were seen to express both cathepsin L and cathepsin B cysteine proteinases, although the former activity was many -fold greater. Two cathepsin L activities identified in cercarial extracts by zymography co-migrated with activities in extracts of 3 h and 24 h schisotosomula and in extracts of adult worms. Since these enzymes have been implicated in haemoglob in digestion by adult worms, they may perform a similar function in schistosomula. Immunolocalization using scanning electron micrographs showed that cathepsin L and cathepsin B proteinases were present in the cercarial post-acetabular glands. In addition, cercarial serine proteinase activities considered to facilitate skin penetration efficiently cleaved the substrates Z-Gly-Pro-Arg-NHMec and Z-Gly-Pro-Lys-NHMec. Cercariae release most of this serine proteinase activity when induced to secrete the contents of their acetabular glands. In contrast, newly transformed 3 h and 24 h schistosomula did not express this activity.

Elevations of cathepsin B and cathepsin L activities in forelimb and hind limb muscles of genetically dystrophic mice

1986 ◽  
Vol 93 (3) ◽  
pp. 642-646 ◽  
Author(s):  
Keiji Komatsu ◽  
Kazutomo Tsukuda ◽  
Jun Hosoya ◽  
Susumu Satoh
Keyword(s):  
Cathepsin B ◽  
Hind Limb ◽  
Cathepsin L ◽  
Limb Muscles ◽  
Dystrophic Mice

scholarly journals Divergent Approaches Regulating Beta Agonists and Cloning of Animals for Food: USA and European Union

2020 ◽  
Vol 28 (5-6) ◽  
pp. 613-632
Author(s):  
Terence J. Centner ◽  
Ludivine Petetin
Keyword(s):  
United States ◽  
European Union ◽  
Dairy Products ◽  
Food Products ◽  
The United States ◽  
Beta Agonist ◽  
Spongiform Encephalopathy ◽  
Beta Agonists ◽  
Nonhuman Animals ◽  
Production Technologies

Abstract Technologies being used to produce nonhuman animals who are used for meat and dairy products are viewed by some people as meaningful. Two technologies receiving scrutiny in agriculture are beta agonists that are fed to food animals to improve weight gain and cloning animals to secure offspring with specific traits. The technologies enhance the productive capacities of animals so that fewer resources are needed to produce meat and dairy products. Yet consumers are not sure they want food products with beta agonist residues and that are produced from clones. In overseeing the safety of food products and animals, legislators and regulators in the United States (US) and European Union (EU) have developed contrasting provisions regarding the usage of these technologies. An evaluation of heuristics involving information and experiences with bovine spongiform encephalopathy and animal production technologies offers support in explaining the US’s and EU’s divergent provisions.

scholarly journals Effects of microbial proteinase inhibitors on the degradation of endogenous and internalized proteins by rat yolk sacs

1981 ◽  
Vol 196 (1) ◽  
pp. 41-48 ◽  
Author(s):  
S E Knowles ◽  
F J Ballard ◽  
G Livesey ◽  
K E Williams
Keyword(s):  
Bovine Serum Albumin ◽  
Cathepsin B ◽  
Proteinase Inhibitors ◽  
Cathepsin L ◽  
Minor Role ◽  
Protein Breakdown ◽  
Inhibitory Effects ◽  
Endogenous Protein ◽  
A Minor

1. The effects of leupeptin and other microbial proteinase inhibitors were measured in rat yolk sacs on the uptake and degradation of formaldehyde-denatured 125I-labelled bovine serum albumin as well as on the degradation of 3H-labelled endogenous protein. 2. Leupeptin, at concentrations between 1 and 100 micrograms/ml, inhibits the degradation of added albumin without affecting pinocytic uptake. Accordingly large amounts of undegraded albumin accumulate within the tissue. 3. Removal of leupeptin produces a rapid recovery of the capacity to degrade albumin. 4. Endogenous protein degradation is rapidly inhibited by leupeptin, but to a far lesser extent than the breakdown of albumin. However, the inhibition is only slightly reversed on removal of leupeptin. 5. Degradation of both albumin and endogenous protein in intact yolk sacs is inhibited by the microbial proteinase inhibitors in the order: leupeptin greater than antipain greater than chymostatin; elastatinal, pepstatin and bestatin are ineffective. 6. Similar results are found when albumin is incubated in yolk-sac homogenates at pH 4 with the inhibitors. 7. The marked inhibitory effects of leupeptin, antipain and chymostatin suggest that cathepsin B and possibly cathepsin L participate in the degradation of 125I-labelled albumin in yolk sacs. By comparison, the smaller inhibitory effects of the proteinase inhibitors on endogenous protein breakdown imply a minor role of lysosomal cathepsins in this process.

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
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