Linked Life Data

7827138

Source:http://linkedlifedata.com/resource/pubmed/id/7827138

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1995-2-21
pubmed:abstractText
The effect of exogenous and endogenous products storage in lysosomes on the activity and multiple forms of alpha-L-fucosidase from human skin fibroblasts was investigated. It was shown that sucrose load, modelling intralysosomal accumulation of nonhydrolyzable products, causes certain changes in secretion level of alpha-L-fucosidase and multiple forms' spectra of the intracellular and secreted enzymes. These changes were different for the enzyme from embryonal and postnatal normal fibroblasts. Some changes of secreted alpha-L-fucosidase isoforms' spectra were found in fibroblasts from a patient with Fabry's disease, characterized by the intralysosomal storage of di- and trihexosylceramides. The alterations of isoforms' profiles in Fabry fibroblasts at the early and late accumulation stages were similar to those in sucrose-loaded embryonal and postnatal fibroblasts, respectively. It is proposed that intralysosomal accumulation of nonhydrolyzable compounds influences the alpha-L-fucosidase posttranslational processing.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
1270
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7-11
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Change of isoforms' spectra of alpha-L-fucosidase from human skin fibroblasts in intracellular storage of nonhydrolyzable substances.
pubmed:affiliation
Institute of Biomedical Chemistry, Russian Academy of Medical Sciences, Moscow.
pubmed:publicationType
Journal Article