Linked Life Data

8346912

Source:http://linkedlifedata.com/resource/pubmed/id/8346912

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1993-9-3
pubmed:abstractText
Cathepsin E (CE) is an intracellular, nonlysosomal aspartic proteinase which consists of two identical subunits with a molecular weight of about 42 kDa (K. Yamamoto, M. Takeda, H. Yamamoto, M. Tatsumi, and Y. Kato, 1985, J. Biochem. 97, 821-830). In order to clarify its nature and proteolytic activation, the pro-CE and the mature enzyme were simultaneously purified from human erythrocyte membranes. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the reduced proenzyme showed a single protein band, exhibiting an apparent molecular weight of 46 kDa. The proenzyme was found to be catalytically inactive, but it was rapidly converted into the active enzyme after brief acid treatment at pH 4.0, which was accompanied by a reduction in molecular size to 43 kDa. The activated form of pro-CE was essentially identical with the mature enzyme in enzymatic properties such as specific activities toward synthetic and protein substrates, and susceptibilities to various protease inhibitors. The N-terminal amino acid sequence analysis revealed that pro-CE started with the third amino acid residue, Ser3, of the sequence of human gastric CE predicted from its cDNA sequence and that the autocatalytic cleavage occurred at the Met36-Ile37 and Phe39-Thr40 bonds to produce two mature isozymic forms. The mature enzyme purified from human erythrocyte membranes also showed two different N-terminal sequences identical with those of the in vitro-activated form of pro-CE. The proenzyme, as well as the mature enzyme from human and rat erythrocyte membranes, was shown to be as an endo-beta-N-acetylglucosaminidase H-resistant form, whereas CE from rat spleen was N-glycosylated with a high-mannose-type oligosaccharide chain, suggesting that the carbohydrate modification of this protein varies with the cell type or the cellular localization. These data also suggest that the proenzyme in human erythrocytes is processed from the high-mannose type to the complex/hybrid type during its biosynthesis at early stages of erythroid differentiation, which precedes the proteolytic activation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0003-9861
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
304
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
352-8
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Isolation and biochemical characterization of procathepsin E from human erythrocyte membranes.
pubmed:affiliation
Department of Pharmacology, Kyushu University Faculty of Dentistry, Fukuoka, Japan.
pubmed:publicationType
Journal Article