Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
21
pubmed:dateCreated
1986-9-17
pubmed:abstractText
Apolipoprotein C-II plays a major role in lipid metabolism as a cofactor for lipoprotein lipase, the enzyme involved in the hydrolysis of triglyceride-rich lipoproteins. Apo-C-II is initially synthesized as a 101 amino acid protein that undergoes subsequent cotranslational cleavage of a signal peptide. Post-translational processing of apo-C-II has not been previously described. In this manuscript we identify four major plasma isoforms of apo-C-II by two-dimensional gel electrophoresis and immunoblot analysis that result from post-translational modification of apo-C-II. Neuraminidase studies have shown that two of these isoforms are early secreted sialic acid containing glycoproteins. Amino acid compositional and amino-terminal analysis have established that the major plasma isoform of apo-C-II is proapo-C-II. Proapo-C-II undergoes proteolytic cleavage of its amino-terminal hexapeptide to generate the mature form of apo-C-II. Thus, apo-C-II appears to be secreted as a carbohydrate containing proprotein that then undergoes deglycosylation and proteolytic cleavage to generate mature apo-C-II, a minor isoform in plasma. An improved understanding of the structural relationship of the various plasma isoforms of apo-C-II will help to elucidate the mechanisms involved in normal, as well as defective, processing of apo-C-II.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
261
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9591-4
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
Human preproapolipoprotein C-II. Analysis of major plasma isoforms.
pubmed:publicationType
Journal Article