Linked Life Data

9033633

Source:http://linkedlifedata.com/resource/pubmed/id/9033633

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1997-3-6
pubmed:abstractText
The kinetics of transport and the processing of procathepsin D (proCD), the precursor of a lysosomal aspartyl protease involved in tumor-cell proliferation and metastasis, were compared in normal and SV-40- or benzo[a]pyrene-transformed 3T3 mouse fibroblasts. Sorting of newly synthesized proCD in normal cells was almost complete within 3 hr, while in transformed cells a fraction of the precursor survives a long time. In both normal and transformed 3T3 cultures, secretion of proCD started at 3 hr of chase. However, in normal cells secretion of proCD remained constant between 3 and 24 hr of chase, while in transformed cells it increased along with the chase incubation. The efficiency of formation of the mannose-6-phosphate group on proCD varied among the 3 cell types, being minimal in benzo[a]pyrene-transformed 3T3 cells. Ammonium chloride, a drug known to disrupt the segregation and to enhance the secretion of lysosomal proenzymes, was 2-fold more effective in normal than in transformed 3T3 cells. Despite vacuolar alkalinization, about one third of proCD was segregated into the endosomal-lysosomal pathway in normal and in transformed 3T3 fibroblasts, indicating the existence in these cells of alternative, mannose-6-phosphate receptor-independent mechanisms for targeting proCD. Thus, while hypersecretion of proCD and reduced sensitivity to vacuolar alkalinization are common features of both transformed cell types, the mechanisms responsible for inefficient segregation of proCD may differ between virally and chemically transformed 3T3 cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0020-7136
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
70
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
310-4
pubmed:dateRevised
2007-7-24
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Differential targeting and processing of procathepsin D in normal and transformed murine 3T3 fibroblasts.
pubmed:affiliation
Dipartimento di Medicina ed Oncologia Sperimentale, Università di Torino, Italy. isidoro@unito.it
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't