Possible Involvement of Cathepsin L in Processing of Rat Liver Hexokinase to Eliminate Mitochondria-Binding Ability

1992 ◽  
Vol 112 (3) ◽  
pp. 409-413 ◽  
Author(s):  
Hiroshi Okazaki ◽  
Chiemi Tanl ◽  
Miyuki Ando ◽  
Kyoko Ishii ◽  
Sadahiko Ishibashi ◽  
...  
Keyword(s):  
Rat Liver ◽  
Cathepsin L ◽  
Binding Ability

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.

scholarly journals Identification of a protein from rat liver cytosol that enhances activation of the glucocorticoid receptor

1988 ◽  
Vol 256 (1) ◽  
pp. 47-52 ◽  
Author(s):  
J L Tymoczko ◽  
S Ahern ◽  
A L Unger ◽  
J L Colby ◽  
G Ede
Keyword(s):  
Dna Binding ◽  
Glucocorticoid Receptor ◽  
Rat Liver ◽  
Deae Cellulose ◽  
Maximal Effect ◽  
Binding Ability ◽  
Liver Cytosol ◽  
Low Salt ◽  
Cellulose Binding ◽  
Rat Liver Cytosol

We have identified a factor from rat liver cytosol that enhances the DNA-cellulose-binding ability of the glucocorticoid receptor and lowers the sedimentation value from 9-10 S to 4-5 S. Cytosol is prepared in the presence of molybdate, and unactivated receptor is isolated by chromatography on DEAE-cellulose in the presence of molybdate. This receptor sediments at 9-10 S and has little affinity for DNA. If the molybdate is removed and the receptor is incubated at 25 degrees C with the low-salt wash of the DEAE-cellulose column, DNA binding is enhanced by 50-600% relative to controls incubated with buffer only. In addition, the factor present in the low-salt wash converts the 9-10 S receptor into a mixture of 5 S and 4 S forms. The factor must be present during the incubation in order to exert its maximal effect. Factor added after the incubation has only marginal effects on the DNA-binding ability of the receptor, indicating that the factor does not increase the DNA-binding ability of activated receptor. Moreover, the factor is significantly less effective on receptor that has been activated before incubation with the factor. These results suggest that the factor acts as an activation enhancer. Preliminary characterization indicates that the activation enhancer is a trypsin-sensitive protein of approx. 70,000 Da, whose activation-enhancing properties are inhibited by ATP. RNAase A, which has effects similar to those described above on the 7-8 S receptor, does not mimic the effects of the activation enhancer on the 9-10 S receptor.

The structures of asparagine-linked oligosaccharides of rat liver cathepsin L reflect the substrate specificity of lysosomal alpha-mannosidase

1998 ◽  
Vol 256 (1) ◽  
pp. 163-169 ◽  
Author(s):  
Takae Towatari ◽  
Tsuyoshi Miyamura ◽  
Akihiro Kondo ◽  
Ikunoshin Kato ◽  
Masahiro Inoue ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Rat Liver ◽  
Cathepsin L

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.

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.

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