Linked Life Data

7983070

Source:http://linkedlifedata.com/resource/pubmed/id/7983070

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
49
pubmed:dateCreated
1995-1-4
pubmed:abstractText
The subcellular distribution and targeting of the non-lysosomal aspartic proteinase cathepsin E have been studied using mouse L cells and monkey Cos 1 cells that were transfected with cDNA encoding cathepsin E. The cathepsin E was retained in L cells for at least 20 h without significant degradation and its single N-linked oligosaccharide remained sensitive to endo-beta-N-acetyl-glucosaminidase H. When cathepsin E was overexpressed by transient transfection in Cos 1 cells, it was very slowly secreted into the media. The intracellular form of the enzyme contained a high mannose oligosaccharide which was processed to a complex type species upon secretion. In double label immunofluorescence studies, cathepsin E co-localized with cathepsin D-myc-KDEL, an endoplasmic reticulum (ER) marker. Subcellular fractionation on a Percoll density gradient showed that the cathepsin E co-migrated with membranous vesicles that were distinct from dense lysosomes. Only a trace amount of the enzyme was recovered in the soluble fraction. These findings indicate that in L cells and Cos 1 cells, the intracellular location of cathepsin E is the endoplasmic reticulum. To identify the protein sequences required for ER retention, we made chimeric proteins between cathepsin E and pepsinogen, an aspartic proteinase that is rapidly secreted by Cos 1 cells. We found that amino acids 1-48 of cathepsin E are important for its retention in the ER. Within this region, Cys7, which is involved in covalent dimer formation, plays a significant role in the retention.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
9
pubmed:volume
269
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
31259-66
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:7983070-Alternative Splicing, pubmed-meshheading:7983070-Amino Acid Sequence, pubmed-meshheading:7983070-Animals, pubmed-meshheading:7983070-Antibodies, pubmed-meshheading:7983070-Base Sequence, pubmed-meshheading:7983070-Cathepsin E, pubmed-meshheading:7983070-Cathepsins, pubmed-meshheading:7983070-Cell Line, pubmed-meshheading:7983070-Cross-Linking Reagents, pubmed-meshheading:7983070-Endoplasmic Reticulum, pubmed-meshheading:7983070-Fluorescent Antibody Technique, pubmed-meshheading:7983070-Haplorhini, pubmed-meshheading:7983070-L Cells (Cell Line), pubmed-meshheading:7983070-Mice, pubmed-meshheading:7983070-Molecular Sequence Data, pubmed-meshheading:7983070-Oligodeoxyribonucleotides, pubmed-meshheading:7983070-Pepstatins, pubmed-meshheading:7983070-Protein Binding, pubmed-meshheading:7983070-Rats, pubmed-meshheading:7983070-Recombinant Fusion Proteins, pubmed-meshheading:7983070-Sepharose, pubmed-meshheading:7983070-Subcellular Fractions
pubmed:year
1994
pubmed:articleTitle
Subcellular localization and targeting of cathepsin E.
pubmed:affiliation
Department of Medicine, Washington University School of Medicine, St. Louis, Missouri 63110.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't