Dopamine-β-hydroxylase is located inside amine storage vesicles of norepinephrine neurons. Dopamine is actively transported from the cytoplasm into the vesicles. As the enzyme is a copper containing protein, its activity can be inhibited by copper chelating agents, such as diethyldithiocarbamate
Glutamine is a common precursor for the biosynthesis of both glutamate and GABA. Glutamine can be transported in and out of neurons and astrocytes utilizing different glutamine carriers. The neurotransmitter glutamate can be synthesized from glutamine by the action of
Cholesterol undergoes esterification to improve transport. Cholesterol esters are more easily packaged into the interior of lipoproteins - increasing the quantity that can be readily transported in the blood stream.
Oxidative stress is mediated, in part, by reactive oxygen species produced by multiple cellular processes and controlled by cellular antioxidant mechanisms such as enzymatic scavengers or antioxidant modulators. Free radicals, such as reactive oxygen species, cause cellular damage via cellular.
Troponin together with tropomyosin, regulate the binding of myosin to actin. Troponin is a trimeric protein composed of Troponin subunits I, C and T. Troponin C binds calcium ions, Troponin T binds to tropomyosin and troponin I binds
Adenylyl cyclases occur throughout the animal kingdom and play diverse roles in cell regulation. In bacteria, the enzyme may be regulated in response to nutrients or it may constitute a toxic factor in mammals, as with adenylyl cyclases of B.
The amino acid glycine is a major inhibitory neurotransmitter in the vertebrate CNS. Glycinergic synapses are particularly abundant in spinal cord and brain stem, but are also found in higher brain regions including the hippocampus. The inhibitory actions of glycine
The amount of cholesterol that is synthesized in the liver is tightly regulated by dietary cholesterol levels. LDL receptors regulate the cellular transport of lipid rich low density lipoprotein (LDL) particles.
Myelin Associated Glycoprotein (MAG) is a type I transmembrane glycoprotein containing five Ig-like domains in its extracellular domain. It is an adhesion molecule belonging to the immunoglobin superfamily.
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