Linked Life Data

12237860

Source:http://linkedlifedata.com/resource/pubmed/id/12237860

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2002-9-18
pubmed:abstractText
To further our understanding of the functions of the major myelin proteins, myelin basic protein (MBP) and proteolipid protein (PLP), and other myelin proteins, such as 2'3'-cyclic nucleotide 3'-phosphodiesterase (CNP) and myelin-associated glycoprotein (MAG), bovine brain myelin was extracted with Triton X-100, and protein complexes in the detergent-soluble fraction were isolated by coimmunoprecipitation and sucrose density gradient sedimentation. MBP, PLP, and the small isoform of MAG (S-MAG) were coimmunoprecipitated from the detergent-soluble fraction by anti-PLP, anti-MBP or anti-MAG monoclonal antibodies. Additionally, a 30 kDa phosphoserine-containing protein and two phosphotyrosine-containing proteins (M(r) 30 and 42 kDa) were found in the coimmunoprecipitates. The 42 kDa protein is probably p42MAPK, in that MAPK was shown also to be present in the immunoprecipitated complex. CNP, the small PLP isoform DM20, the large MAG isoform L-MAG, MOG, CD44, MEK, p44MAPK, and actin were not present in the immunoprecipitates, although they were present in the detergent-soluble fraction. Lipid analysis revealed that the PLP-MBP-S-MAG coimmunoprecipitated with some phospholipids and sulfatide but not cholesterol or galactosylceramide. However, the complex had a high density, indicating that the lipid/protein ratio is low, and it was retained on a Sepharose CL6B column, indicating that it is not a large membrane fragment. Given that MAG is localized mainly in the periaxonal region of myelin, where it interacts with axonal ligands, the PLP-MBP-S-MAG complex may come from these regions, where it could participate in dynamic functions in the myelin sheath and myelin-axonal interactions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0360-4012
pubmed:author
pubmed:copyrightInfo
Copyright 2002 Wiley-Liss, Inc.
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
70
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
8-23
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:12237860-Animals, pubmed-meshheading:12237860-Blotting, Western, pubmed-meshheading:12237860-Cattle, pubmed-meshheading:12237860-Cell Extracts, pubmed-meshheading:12237860-Central Nervous System, pubmed-meshheading:12237860-Centrifugation, Density Gradient, pubmed-meshheading:12237860-Chromatography, Gel, pubmed-meshheading:12237860-Immunoblotting, pubmed-meshheading:12237860-Mitogen-Activated Protein Kinase 1, pubmed-meshheading:12237860-Myelin Basic Proteins, pubmed-meshheading:12237860-Myelin Proteolipid Protein, pubmed-meshheading:12237860-Myelin-Associated Glycoprotein, pubmed-meshheading:12237860-Octoxynol, pubmed-meshheading:12237860-Phosphoserine, pubmed-meshheading:12237860-Phosphotyrosine, pubmed-meshheading:12237860-Precipitin Tests, pubmed-meshheading:12237860-Solubility
pubmed:year
2002
pubmed:articleTitle
Myelin proteolipid protein, basic protein, the small isoform of myelin-associated glycoprotein, and p42MAPK are associated in the Triton X-100 extract of central nervous system myelin.
pubmed:affiliation
Research Institute, The Hospital for Sick Children, Department of Laboratory Medicine and Pathobiology, University of Toronto, Toronto, Ontario, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't