Linked Life Data

9428640

Source:http://linkedlifedata.com/resource/pubmed/id/9428640

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2-3
pubmed:dateCreated
1998-1-27
pubmed:abstractText
Lysosomal beta-galactosidase precursor is processed to a mature form and associated with protective protein in lysosomes. In this study we used two cysteine protease proinhibitors, E64-d for cathepsins B, S, H, and L, and CA074Me for cathepsin B. They are converted intracellularly to active forms, E-64c and CA074, respectively. Both active compounds inhibited maturation of the exogenous beta-galactosidase precursor, but E-64c did not inhibit further degradation to an inactive 50-kDa product. We concluded that cathepsin B participated exclusively in maturation of beta-galactosidase, and a non-cysteine protease was involved in further degradation and inactivation of the enzyme molecule.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
419
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
231-4
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Maturation and degradation of beta-galactosidase in the post-Golgi compartment are regulated by cathepsin B and a non-cysteine protease.
pubmed:affiliation
Department of Clinical Genetics, The Tokyo Metropolitan Institute of Medical Science, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't