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Full-Text Articles in Nervous System
A Cytochemical Evaluation Of Blood-Brain Barrier Sodium, Potassium- And Calcium-Adenosine Triphosphatase Polarity, Panya Steve Manoonkitiwongsa
A Cytochemical Evaluation Of Blood-Brain Barrier Sodium, Potassium- And Calcium-Adenosine Triphosphatase Polarity, Panya Steve Manoonkitiwongsa
Loma Linda University Electronic Theses, Dissertations & Projects
The blood-brain barrier (BBB) is formed by cerebral vascular endothelial cells. Brain ion and fluid homeotasis essential for proper neural functioning is due to the BBB. Sodium-potassium and calcium-activated adenosine triphosphatase (Na+, K+-ATPase and Ca2+-ATPase) serve as one of the main mechanisms controlling brain Na+, K+, and Ca2+ concentrations. The present accepted concept is that both of these enzymes are localized to the abluminal plasma membrane of endothelial cells although there have been contrary results from some studies. Because of these discrepancies, further work was needed. Various cytochemical procedures …
Myelin-Associated Glycoprotein Interacts With Neurons Via A Sialic Acid Binding Site At Arg118 And A Distinct Neurite Inhibition Site, Song Tang, Ying Jing Shen, Maria Elena Debellard, Gitali Mukhopadhyay, James L. Salzer, Paul R. Crocker, Marie T. Filbin
Myelin-Associated Glycoprotein Interacts With Neurons Via A Sialic Acid Binding Site At Arg118 And A Distinct Neurite Inhibition Site, Song Tang, Ying Jing Shen, Maria Elena Debellard, Gitali Mukhopadhyay, James L. Salzer, Paul R. Crocker, Marie T. Filbin
Publications and Research
Inhibitory components in myelin are largely responsible for the lack of regeneration in the mammalian CNS. Myelin-associated glycoprotein (MAG), a sialic acid binding protein and a component of myelin, is a potent inhibitor of neurite outgrowth from a variety of neurons both in vitro and in vivo. Here, we show that MAG’s sialic acid binding site is distinct from its neurite inhibitory activity. Alone, sialic acid–dependent binding of MAG to neurons is insufficient to effect inhibition of axonal growth. Thus, while soluble MAG-Fc (MAG extracellular domain fused to Fc), a truncated form of MAG-Fc missing Ig-domains 4 and 5, MAG(d1-3)-Fc, …