CNS myelinogenesis in vitro: Myelin basic protein deficientshiverer oligodendrocytes

2002 ◽  
Vol 69 (3) ◽  
pp. 305-317 ◽  
Author(s):  
Chika Seiwa ◽  
Kyoko Kojima-Aikawa ◽  
Isamu Matsumoto ◽  
Hiroaki Asou
Keyword(s):  
Myelin Basic Protein ◽  
Basic Protein

In vitro carboxymethylation of myelin basic protein

1986 ◽  
Vol 4 (2) ◽  
pp. 143-151 ◽  
Author(s):  
Toshihiko Innami ◽  
Masaharu Miyake ◽  
Yasuo Kakimoto
Keyword(s):  
Myelin Basic Protein ◽  
Basic Protein

In vitro and in vivo phosphorylation of myelin basic protein by cerebral protein kinase

Nature ◽  
1974 ◽  
Vol 249 (5453) ◽  
pp. 150-151 ◽  
Author(s):  
EISHICHI MIYAMOTO ◽  
SHIRO KAKIUCHI ◽  
YASUO KAKIMOTO
Keyword(s):  
Protein Kinase ◽  
Myelin Basic Protein ◽  
Basic Protein

scholarly journals Studies on an insulin-stimulated insulin receptor serine kinase activity: separation of the kinase activity from the insulin receptor and its reconstitution back to the insulin receptor

1995 ◽  
Vol 308 (3) ◽  
pp. 915-922 ◽  
Author(s):  
K A Asamoah ◽  
P G P Atkinson ◽  
W G Carter ◽  
G J Sale
Keyword(s):  
Myelin Basic Protein ◽  
Insulin Receptor ◽  
Receptor Tyrosine Kinase ◽  
Kinase Activity ◽  
Basic Protein ◽  
Serine Phosphorylation ◽  
Serine Kinase ◽  
Insulin Receptor Tyrosine Kinase ◽  
Mitogen Activated Protein

In cells insulin stimulates autophosphorylation of the insulin receptor on tyrosine and its phosphorylation on serine and threonine by poorly characterized kinases. Recently we have achieved co-purification of the insulin receptor with insulin-stimulated insulin receptor serine kinase activity. We now show that the co-purified serine kinase activity can be removed by NaCl washing and reconstituted by adding back the NaCl eluate. Reconstitution enabled higher serine phosphorylation than achieved with the co-purified preparation. Myelin basic protein was discovered to be a potent substrate for insulin-stimulated serine phosphorylation by the co-purified preparation, with the activity responsible having similar properties to the serine kinase activity towards the receptor. Myelin basic protein was also phosphorylated on serine by the NaCl eluate. Myelin basic protein phosphorylated by the co-purified preparation or the NaCl eluate gave the same set of phosphoserine peptides. The major myelin basic protein serine kinase activity in the NaCl eluate co-purified exactly on Mono Q with the activity that restored insulin-stimulated insulin receptor serine phosphorylation. These results provide strong evidence for the true separation of the serine kinase from the insulin receptor and the distinctiveness of the serine kinase activity from the insulin receptor tyrosine kinase and mitogen-activated protein kinases. The procedures developed for the isolation of the serine kinase and the establishment of an effective in vitro substrate should allow purification of the kinase. The protocols also provide flexible systems for identifying the functions of the insulin-stimulated serine phosphorylations and the respective kinase(s).

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