Linked Life Data

9056407

Source:http://linkedlifedata.com/resource/pubmed/id/9056407

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1997-3-20
pubmed:abstractText
The MPM-2 monoclonal antibody recognizes a distinctive group of proteins that are associated with structural components of the mitotic apparatus. These proteins become phosphorylated and MPM-2 reactive during M-phase and appear to be required for both the onset and completion of M-phase. Based upon the analysis of reported MPM-2 reactive sequences, we have developed a model for the essential elements that comprise the MPM-2 epitope. This model was tested by employing a series of synthetic phosphopeptides. We show here that a 14 amino acid synthetic phosphopeptide, derived from a potential MPM-2 site on human DNA topoisomerase II, is recognized by the MPM-2 antibody. This phosphopeptide was sufficient to compete for MPM-2 antibody recognition of (1) an isolated native mitotic MPM-2 antigen on dot blots, (2) proteins on immunoblots of mitotic cell lysates, and (3) specific immunostaining of mitotic cells. These results indicated that the topoisomerase peptide contained all of the essential elements of the MPM-2 epitope. By substituting selected amino acids with alanine, we were able to examine the contribution of different amino acids to the binding between the MPM-2 antibody and the epitope. Changing the amino acid that was adjacent to the phosphorylated threonine residue on the C-terminal side (the +1 position) had no effect on MPM-2 antibody binding. However, substitution of aromatic amino acids at either the -2 or +2 positions reduced antibody recognition. The aromatic amino acid at the -2 position appeared to be the most critical residue of those tested that influenced antibody binding. These results provide information required for the molecular definition of the MPM-2 epitope and should aid in the identification of potential MPM-2 reactive sites on other mitotic phosphoproteins.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0014-4827
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
231
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3-13
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Partial characterization of the MPM-2 phosphoepitope.
pubmed:affiliation
Department of Cell Biology, Neurobiology, and Anatomy, The Ohio State University, Columbus, Ohio, 43210, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.