Folding, activity and targeting of mutated human cathepsin D that cannot be processed into the double-chain form

2007 ◽  
Vol 39 (3) ◽  
pp. 638-649 ◽  
Author(s):  
Carlo Follo ◽  
Roberta Castino ◽  
Giuseppina Nicotra ◽  
Nicol F. Trincheri ◽  
Ciro Isidoro
Keyword(s):  
Cathepsin D ◽  
Double Chain ◽  
Human Cathepsin ◽  
Chain Form

scholarly journals Human tumour cathepsin B. Comparison with normal liver cathepsin B

1992 ◽  
Vol 285 (2) ◽  
pp. 427-434 ◽  
Author(s):  
K Moin ◽  
N A Day ◽  
M Sameni ◽  
S Hasnain ◽  
T Hirama ◽  
...  
Keyword(s):  
Cathepsin B ◽  
Human Liver ◽  
Normal Liver ◽  
Polyacrylamide Gels ◽  
Single Chain ◽  
Human Tumour ◽  
Double Chain ◽  
Normal Human Liver ◽  
Human Cathepsin ◽  
Chain Form

Cathepsin B was purified from normal human liver and several human tumour tissues and partially characterized. Three forms of cathepsin B, with molecular masses of 25 kDa, 26 kDa (the two appearing as a doublet) and 30 kDa, were detected in SDS/polyacrylamide gels. The 25-26 kDa doublet was associated with the fractions from tumours and normal liver containing the highest cathepsin B activity. Cathepsin B from both sources showed similar pH optima. Both normal liver and tumour cathepsin B exhibited similar kinetics against selected synthetic substrates. At neutral pH and 24 degrees C, cathepsin B from both normal liver and tumour exhibited a lower Km and a higher kcat./Km than at pH 6.0. Their inhibitory profiles against synthetic inhibitors were also similar. Immunological studies with a monospecific antibody against the mature double-chain form of human liver cathepsin B and an antibody against a cathepsin B-derived synthetic peptide established the immunological similarity of liver and tumour enzymes. The N-terminal sequences of the 25 kDa and 26 kDa forms were identical with that of the heavy chain of the mature double-chain form of human cathepsin B, whereas the N-terminal sequence of the 30 kDa species was identical with that of the single-chain form of human cathepsin B. Treatment of the double-chain form of cathepsin B from normal liver and tumours with the endoglycosidase peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase converted the 26 kDa form into 25 kDa in SDS/polyacrylamide gels, suggesting that cathepsin B may exist as both glycosylated and unglycosylated forms. Our results, in contrast with those reported earlier for mouse cathepsin B, indicate that human liver and tumour cathepsin B are similar.

Design of sensitive fluorogenic substrates for human cathepsin D

FEBS Letters ◽  
1997 ◽  
Vol 413 (2) ◽  
pp. 379-384 ◽  
Author(s):  
Sergei V. Gulnik ◽  
Leonid I. Suvorov ◽  
Pavel Majer ◽  
Jack Collins ◽  
Bradley P. Kane ◽  
...  
Keyword(s):  
Cathepsin D ◽  
Fluorogenic Substrates ◽  
Human Cathepsin

scholarly journals Structure-based subsite specificity mapping of human cathepsin D using statine-based inhibitors

1997 ◽  
Vol 6 (7) ◽  
pp. 1458-1466 ◽  
Author(s):  
Pavel Majer ◽  
Jack R. Collins ◽  
Sergei V. Gulnik ◽  
John W. Erickson
Keyword(s):  
Cathepsin D ◽  
Human Cathepsin

Proteolytic processing sites producing the mature form of human cathepsin D

1992 ◽  
Vol 24 (9) ◽  
pp. 1487-1491 ◽  
Author(s):  
Kobayashi Takahiko ◽  
Honke Koichi ◽  
Gasa Shinsei ◽  
Fujii Tetsuya ◽  
Maguchi Shiro ◽  
...  
Keyword(s):  
Cathepsin D ◽  
Proteolytic Processing ◽  
Mature Form ◽  
Human Cathepsin

Purification of bovine cathepsin B: proteomic characterization of the different forms and production of specific antibodies

2003 ◽  
Vol 81 (4) ◽  
pp. 317-326 ◽  
Author(s):  
M A Sentandreu ◽  
L Aubry ◽  
A Ouali
Keyword(s):  
Cathepsin B ◽  
Sodium Dodecyl ◽  
Anion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Peptide Sequence ◽  
Size Exclusion ◽  
Single Chain ◽  
Double Chain ◽  
Bovine Kidney ◽  
Chain Form

Cathepsin B (EC 3.4.22.1) has been highly purified (14 225 fold) from bovine kidney by a rapid procedure that included the preparation of an enriched lysosomal extract, a selective fractionation with ammonium sulphate, size-exclusion chromatography, two cation-exchange chromatographies, and anion-exchange chromatography on diethylaminoethyl–Sephacel. After the last purification step, two hydrolytic peaks against Z-Phe-Arg-AMC were separated from each other, a minor peak corresponding to the cathepsin B single-chain form and a major one representing the double-chain form of cathepsin B. The single-chain form showed a molecular mass of 31 kDa on sodium dodecyl sulphate – polyacrylamide gel electrphoresis (PAGE) under reducing conditions, whereas the heavy chain of the double-chain form appeared as a doublet with molecular masses of 23.4 and 25 kDa, respectively. The identity of the different cathepsin B isoforms and the quality of the final enzyme preparation were confirmed by using two types of antibodies, one against a synthetic peptide sequence and one against purified cathepsin B. The proteomic study confirmed the identity of the different SDS–PAGE protein bands as cathepsin B isoforms and allowed the comparison and study of some structural differences between them at the level of their primary structures.Key words: cathepsin B, bovine kidney, MALDI-TOF, cathepsin B isoforms, antibodies.

Alterations and Role of Human Cathepsin D in Cancer Metastasis

1996 ◽  
Vol 49 (1-3) ◽  
pp. 106-116 ◽  
Author(s):  
Henri Rochefort ◽  
Emmanuelle Liaudet ◽  
Marcel Garcia
Keyword(s):  
Cathepsin D ◽  
Cancer Metastasis ◽  
Human Cathepsin

The human cathepsin D-encoding gene is transcribed from an estrogen-regulated and a constitutive start point

Gene ◽  
1993 ◽  
Vol 134 (2) ◽  
pp. 277-282 ◽  
Author(s):  
Felicity E.B. May ◽  
David J. Smith ◽  
Bruce R. Westley
Keyword(s):  
Cathepsin D ◽  
Human Cathepsin ◽  
Encoding Gene
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