| Autor: |
Owh P; Division of Biochemistry, Hospital for Sick Children, Toronto, Ontario/Canada., da Cruz LA, Ackerley CA, Moscarello MA |
| Jazyk: |
angličtina |
| Zdroj: |
European journal of cell biology [Eur J Cell Biol] 1997 Oct; Vol. 74 (2), pp. 172-80. |
| Abstrakt: |
An astrocytoma cell line (HTB-14), expressing high amounts of a CD44 variant compared to other astrocytoma lines was shown to bind myelin basic protein to a greater extent than low expressing lines in a concentration-dependent manner. The CD44 variant expressed by HTB-14 cells was determined to migrate in sodium dodecyl sulfate polyacrylamide gel electrophoresis with a molecular mass of 100 kDa compared to that from white matter which had a molecular mass of 80 kDa. The most cationic component of myelin basic protein (MBP), (component 1) bound more avidly than the least cationic isomer (component 8). Internalization of MBP was demonstrated by immunogold electron microscopy and was localized to the perinuclear area with some gold particles in the cytoplasm but not near the plasma membrane. Colocalization with glial fibrillary acid protein suggested an interaction between these two molecules. Binding and internalization of MBP was accompanied by an increase in CD44 as determined by quantitation of gold particles and the measurement of CD44 by sandwich enzyme-linked immunosorbent assay. The implication of these studies for the mechanism of demyelination is discussed. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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