Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
10
|
pubmed:dateCreated |
1994-3-23
|
pubmed:abstractText |
Among the intracellular proteinases, the thiol proteinases such as cathepsin B (EC 3.4.22.1), cathepsin H (EC 3.4.22.16) and cathepsin L (EC 3.4.22.15) which act at slightly acidic pHs are more likely to play an important role in lysosomal protein catabolism. Out of these, cathepsin L plays a major role primarily because it has high degradative activity on cellular and matrix proteins. However, the studies on cathepsin L in crude homogenates and subcellular fractions have always been hampered by the lack of a specific substrate to exclusively measure the activity of this proteinase. The only synthetic substrate alpha-N-benzyloxycarbonyl-L-Phe-L-Arg-4-methoxy-beta-naphthylamide (Z-Phe-Arg-NNapOMe) which is hydrolysed by cathepsin L is hydrolysed equally well by cathepsin B. This substrate was manipulated to act as a selective substrate for cathepsin L. In presence of 4 M urea at pH 5.0, cathepsin B (the only other cathepsin which also hydrolyses Z-Phe-Arg-NNapOMe) was inactivated and, therefore, under these conditions, the enzyme activity quantitated by using this substrate is only due to cathepsin L. Using this newly-developed colorimetric assay method specific for cathepsin L, the subcellular and regional distribution of this proteinase were established in goat brain tissue. About 80% cathepsin L activity was recovered in the lysosomal fraction thus establishing its lysosomal nature. Among the various brain parts, highest activity was found in cerebrum followed by cerebellum, pituitary body, pons-varolli, thalamus, medulla-oblongata and hypothalamus.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Benzoylarginine-2-Naphthylamide,
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsin B,
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsin L,
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsins,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Dipeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Urea
|
pubmed:status |
MEDLINE
|
pubmed:issn |
0300-9084
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
75
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
873-8
|
pubmed:dateRevised |
2009-11-19
|
pubmed:meshHeading |
pubmed-meshheading:8312391-Amino Acid Sequence,
pubmed-meshheading:8312391-Animals,
pubmed-meshheading:8312391-Benzoylarginine-2-Naphthylamide,
pubmed-meshheading:8312391-Brain,
pubmed-meshheading:8312391-Cathepsin B,
pubmed-meshheading:8312391-Cathepsin L,
pubmed-meshheading:8312391-Cathepsins,
pubmed-meshheading:8312391-Colorimetry,
pubmed-meshheading:8312391-Cysteine Endopeptidases,
pubmed-meshheading:8312391-Dipeptides,
pubmed-meshheading:8312391-Endopeptidases,
pubmed-meshheading:8312391-Goats,
pubmed-meshheading:8312391-Hydrogen-Ion Concentration,
pubmed-meshheading:8312391-Lysosomes,
pubmed-meshheading:8312391-Molecular Sequence Data,
pubmed-meshheading:8312391-Substrate Specificity,
pubmed-meshheading:8312391-Tissue Distribution,
pubmed-meshheading:8312391-Urea
|
pubmed:year |
1993
|
pubmed:articleTitle |
A selective colorimetric assay for cathepsin L using Z-Phe-Arg-4-methoxy-beta-naphthylamide.
|
pubmed:affiliation |
Department of Chemistry, Kurukshetra University, Haryana, India.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|