Isolation and Characterization of Stem Cells from Human Central Nervous System Malignancies

Author(s):  
Imad Saeed Khan ◽  
Moneeb Ehtesham
Genetics ◽  
1990 ◽  
Vol 126 (4) ◽  
pp. 1033-1044 ◽  
Author(s):  
T Watanabe ◽  
D R Kankel

Abstract Previous genetic studies have shown that wild-type function of the l(1)ogre (lethal (1) optic ganglion reduced) locus is essential for the generation and/or maintenance of the postembryonic neuroblasts including those from which the optic lobe is descended. In the present study molecular isolation and characterization of the l(1)ogre locus was carried out to study the structure and expression of this gene in order to gain information about the nature of l(1)ogre function and its relevance to the development of the central nervous system. About 70 kilobases (kb) of genomic DNA were isolated that spanned the region where l(1)ogre was known to reside. Southern analysis of a l(1)ogre mutation and subsequent P element-mediated DNA transformation mapped the l(1)ogre+ function within a genomic fragment of 12.5 kb. Northern analyses showed that a 2.9-kb message transcribed from this 12.5-kb region represented l(1)ogre. A 2.15-kb portion of a corresponding cDNA clone was sequenced. An open reading frame (ORF) of 1,086 base paris was found, and a protein sequence of 362 amino acids with one highly hydrophobic segment was deduced from conceptual translation of this ORF.


2012 ◽  
Vol 35 (3) ◽  
pp. 468-477 ◽  
Author(s):  
Trevor J. McGill ◽  
Benjamin Cottam ◽  
Bin Lu ◽  
Shaomei Wang ◽  
Sergej Girman ◽  
...  

1992 ◽  
Vol 32 (4) ◽  
pp. 593-604 ◽  
Author(s):  
V. S. Sapirstein ◽  
R. Durrie ◽  
B. Cherksey ◽  
M. E. Beard ◽  
C. J. Flynn ◽  
...  

2019 ◽  
Vol 23 (11) ◽  
pp. 7382-7394 ◽  
Author(s):  
Maria Teresa De Angelis ◽  
Gianluca Santamaria ◽  
Elvira Immacolata Parrotta ◽  
Stefania Scalise ◽  
Michela Lo Conte ◽  
...  

1996 ◽  
Vol 55 (8) ◽  
pp. 889-895 ◽  
Author(s):  
Michael C. Irizarry ◽  
Tae-Wan Kim ◽  
Megan MCNamara ◽  
Rudolph E. Tanzi ◽  
Julia M. George ◽  
...  

1988 ◽  
Vol 106 (4) ◽  
pp. 1273-1279 ◽  
Author(s):  
D D Mikol ◽  
K Stefansson

Here we report the isolation and initial biochemical characterization of a 120-kD peanut agglutinin-binding glycoprotein from the adult human central nervous system (CNS), which is anchored to membranes through a phosphatidylinositol linkage. Myelin incubated with phosphatidylinositol-specific phospholipase C released the protein as a soluble polypeptide of 105 kD, which was isolated with peanut agglutinin-agarose affinity chromatography. The protein was found to be highly glycosylated. The protein appears to be confined to the CNS, where its developmental expression is region specific and parallels myelination. It is in greater quantity in white matter than in gray matter and it is in isolated human CNS myelin. Furthermore, ovine oligodendrocytes in culture contain the protein on their surfaces and release it into the supernatant as a soluble 105-kD form. We call this protein the oligodendrocyte-myelin protein.


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