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.

Inhibitions of Cathepsin B and Cathepsin L by E-64 In Vivo. II. Incorporation of [3H]E-64 into Rat Liver Lysosomes In Vivo1

1982 ◽  
Vol 91 (4) ◽  
pp. 1373-1380 ◽  
Author(s):  
Seiichi HASHIDA ◽  
Eiki KOMINAMI ◽  
Nobuhiko KATUNUMA
Keyword(s):  
Rat Liver ◽  
Cathepsin B ◽  
Cathepsin L ◽  
Liver Lysosomes ◽  
Rat Liver Lysosomes

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 Cathepsin L. A New Proteinase from Rat-Liver Lysosomes

1977 ◽  
Vol 74 (2) ◽  
pp. 293-301 ◽  
Author(s):  
Heidrun KIRSCHKE ◽  
Jurgen LANGER ◽  
Bernd WIEDERANDERS ◽  
Siegfried ANSORGE ◽  
Peter BOHLEY
Keyword(s):  
Rat Liver ◽  
Cathepsin L ◽  
Liver Lysosomes ◽  
Rat Liver Lysosomes

scholarly journals Identification of targeting proteinase for rat α1-macroglobulin in vivo. Mast-cell tryptase is a major component of the α1-macroglobulin-proteinase complex endocytosed into rat liver lysosomes

1994 ◽  
Vol 298 (1) ◽  
pp. 79-85 ◽  
Author(s):  
A Tsuji ◽  
T Akamatsu ◽  
H Nagamune ◽  
Y Matsuda
Keyword(s):  
Mast Cell ◽  
Rat Liver ◽  
Cathepsin L ◽  
Deae Cellulose ◽  
Serine Proteinase ◽  
Mast Cell Tryptase ◽  
Diisopropyl Fluorophosphate ◽  
Liver Lysosomes ◽  
Rat Liver Lysosomes

The alpha 1-macroglobulin-proteinase complex endocytosed into rat liver lysosomes was purified by a series of column chromatographic steps on concanavalin A-Sepharose, Sephacryl S-300, DEAE-cellulose and TSK gel DEAE-5PW columns. The complex contained no detectable alpha 2-macroglobulin. Studies on the substrate specificity indicated that the complex had tryptase-like activities towards various synthetic substrates, but no elastase, chymotrypsin, cathepsin-B and cathepsin-L activities. The proteinase activity was completely inhibited by di-isopropyl fluorophosphate, leupeptin and antipain, indicating that the proteinase bound to alpha 1-macroglobulin is a serine proteinase. Two protein bands (62 and 59 kDa) of the complex were labelled with [3H]diisopropyl fluorophosphate and both bands cross-reacted with anti-(mast-cell tryptase)antibody. These results suggest that mast-cell tryptase is a major targeting proteinase for alpha 1-macroglobulin in vivo. The main alpha-macroglobulin-proteinase complex in the adjuvant-treated rats was also the alpha 1-macroglobulin-tryptase complex, even though the plasma level of alpha 2-macroglobulin was elevated.

Cathepsin L and Cathepsin B3 from Rat Liver Lysosomes

1977 ◽  
pp. 299-303 ◽  
Author(s):  
H. Kirschke ◽  
J. Langner ◽  
B. Wiederanders ◽  
S. Ansorge ◽  
P. Bohley ◽  
...  
Keyword(s):  
Rat Liver ◽  
Cathepsin L ◽  
Liver Lysosomes ◽  
Rat Liver Lysosomes

Inhibition of cathepsin L and B by haptoglobin, the haptoglobin–hemoglobin complex, and asialohaptoglobin. "In vitro" studies in the rat

1982 ◽  
Vol 60 (6) ◽  
pp. 631-637 ◽  
Author(s):  
M. Pagano ◽  
M. A. Nicola ◽  
R. Engler
Keyword(s):  
Rat Liver ◽  
Inflammatory Reaction ◽  
Cathepsin B ◽  
Cathepsin L ◽  
In Vitro Studies ◽  
The Other ◽  
Michaelis Constant ◽  
Thiol Proteinases ◽  
Thiol Proteinase

In broadening our research on the inhibition of cathepsin B (EC 3.4.22.1) by rat haptoglobin, we have used the haptoglobin–hemoglobin complex and asialohaptoglobin. The inhibition of cathepsin L (EC 3.4.22.15), another lysosomal thiol proteinase, by haptoglobin and its related molecules has also been investigated.With azocasein as substrate, both enzymes were inhibited by both haptoglobin and its related molecules. When azocasein was used as a substrate, the apparent Michaelis constant (Km, app.) for cathepsin L was 1 × 10−5 ± 0.4 × 10−5 M. When haptoglobin was added, the apparent inhibition constant (Ki, app.) was 3 × 10−8 ± 2.5 × 10−8 M.The results suggest that rat haptoglobin specifically inhibits lysosomal thiol proteinases and that it has a regulatory role in tissue proteolysis associated with the inflammatory reaction. On the other hand, these properties would seem to be peculiar to the systems rat haptoglobin – rat liver cathepsin B or L.

scholarly journals Action of rat liver cathepsin L on collagen and other substrates.

1982 ◽  
Vol 201 (2) ◽  
pp. 367-372 ◽  
Author(s):  
H Kirschke ◽  
A A Kembhavi ◽  
P Bohley ◽  
A J Barrett
Keyword(s):  
Rat Liver ◽  
Active Site ◽  
Cathepsin B ◽  
Specific Activity ◽  
Cathepsin L ◽  
Purification Method ◽  
Mercury Derivative ◽  
Insoluble Collagen ◽  
And Storage

1. It has been found that cathepsin L is very susceptible to loss of activity through autolysis. When this is prevented by purification and storage of the enzyme as its mercury derivative, preparations are obtained with higher specific activity than previously. 2. Active-site titration shows, however, that even the new purification method does not give preparations in which the enzyme is 100% active. 3. Benzyloxycarbonylphenylalanylarginine 7-(4-methyl)coumarylamide has been discovered to be a very sensitive substrate for cathepsin L. Like all other known substrates for cathepsin L, however, it is also cleaved by cathepsin B. 4. Cathepsin L degrades insoluble collagen at pH 3.5 over 5-fold faster than at pH 6.0. The specific activity at pH 3.5 is 5-10-fold higher than that of cathepsin B (rat or human) or bovine spleen cathepsin N (‘collagenolytic cathepsin’). 5. Qualitatively, the action of cathepsin L on collagen is similar to that of cathepsins B and N, i.e. selective cleavage of terminal peptides leads to conversion of beta- and higher components mainly to alpha-chains.

scholarly journals Enzyme-substrate interactions in the hydrolysis of peptides by cathepsins B and H from rat liver

1987 ◽  
Vol 245 (2) ◽  
pp. 381-385 ◽  
Author(s):  
D Brömme ◽  
K Bescherer ◽  
H Kirschke ◽  
S Fittkau
Keyword(s):  
Rat Liver ◽  
Cathepsin B ◽  
Hydrolysis Rate ◽  
Amino Acid Residues ◽  
Enzyme Substrate ◽  
Cathepsin H ◽  
Substrate Peptide ◽  
Scissile Bond ◽  
Peptide Amide ◽  
Hydrolysis Of

The number of possible subsites of the rat liver cysteine proteinases cathepsin B and cathepsin H was determined in the N-terminal direction from the scissile bond. An elongation of the substrate peptide chain of up to four amino acid residues enhances the hydrolysis rate of both cathepsins. The greatest increase in activity was observed by elongation to the dipeptide substrate for cathepsin B and to the tetrapeptide substrate for cathepsin H. Both proteinases discriminate proline from their subsites S1 and S2, but accept it well in S3. A quantitative distinction between the endopeptidase and the peptidyl dipeptidase activity of cathepsin B was feasible by using two model peptides: (Formula: see text) (Z = benzyloxycarbonyl; X = NH2 or OH; the arrow shows the cleavage site). Whereas the peptide acid, representing the peptidyl dipeptidase substrate, was hydrolysed by cathepsin B twice as fast as the peptide amide as an endopeptidase substrate, cathepsin H clearly had a preference for the amide substrate.

Inhibitions by E-64 Derivatives of Rat Liver Cathepsin B and Cathepsin L In Vitro and In Vivo 1

1980 ◽  
Vol 88 (6) ◽  
pp. 1805-1811 ◽  
Author(s):  
Seiichi HASHIDA ◽  
Takae TOWATARI ◽  
Eiki KOMINAMI ◽  
Nobuhiko KATUNUMA
Keyword(s):  
Rat Liver ◽  
Cathepsin B ◽  
Cathepsin L ◽  
Derivatives Of
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