TY - JOUR
T1 - Stathmin Is a Major Phosphoprotein and Cyclic AMP‐Dependent Protein Kinase Substrate in Mouse Brain Neurons but Not in Astrocytes in Culture
T2 - Regulation During Ontogenesis
AU - Chneiweiss, Hervé
AU - Beretta, Laura
AU - Cordier, Jocelyne
AU - Boutterin, Marie‐Claude ‐C
AU - Glowinski, Jacques
AU - Sobel, André
N1 - Copyright:
Copyright 2016 Elsevier B.V., All rights reserved.
PY - 1989/9
Y1 - 1989/9
N2 - Stathmin is a ubiquitous soluble protein (Mr˜ 19,000; pI ˜ 6.2–5.5) whose phosphorylation is associated with the intracellular mechanisms involved in the regulations of cell differentiation and functions by extracellular effectors. It is present in various tissues and cell types and has several nonphosphorylated and increasingly phosphorylated forms, and it is particularly abundant in brain. Very high concentrations of stathmin were also detected in mouse embryo striatal neurons grown in primary culture, whereas stathmin was barely detectable in astrocytes from the same source. Stathmin appeared in neurons as a major substjrate for protein phosphorylation and, in particular, for the cyclic AMP (cAMP)‐dependent protein kinase, because its phosphorylation was stimulated by cAMP in cell‐free preparations and in intact cells by forskolin, a potent activator of adenylate cyclase. During brain ontogenesis, stathmin was first detected at embryonic day 12; its concentration increased until birth and then decreased from postnatal day 10 to adulthood. In parallel, its molecular forms shifted from the least phosphorylated to the more phosphorylated ones. This result may reflect the evolution of the activity of stathmin during development and the subsequent maturation of the brain. In conclusion, our results substantiate the likely role of stathmin as an intracellular relay of extracellular regulations, as they point out its specific importance related to neuronal functions and brain differentiation.
AB - Stathmin is a ubiquitous soluble protein (Mr˜ 19,000; pI ˜ 6.2–5.5) whose phosphorylation is associated with the intracellular mechanisms involved in the regulations of cell differentiation and functions by extracellular effectors. It is present in various tissues and cell types and has several nonphosphorylated and increasingly phosphorylated forms, and it is particularly abundant in brain. Very high concentrations of stathmin were also detected in mouse embryo striatal neurons grown in primary culture, whereas stathmin was barely detectable in astrocytes from the same source. Stathmin appeared in neurons as a major substjrate for protein phosphorylation and, in particular, for the cyclic AMP (cAMP)‐dependent protein kinase, because its phosphorylation was stimulated by cAMP in cell‐free preparations and in intact cells by forskolin, a potent activator of adenylate cyclase. During brain ontogenesis, stathmin was first detected at embryonic day 12; its concentration increased until birth and then decreased from postnatal day 10 to adulthood. In parallel, its molecular forms shifted from the least phosphorylated to the more phosphorylated ones. This result may reflect the evolution of the activity of stathmin during development and the subsequent maturation of the brain. In conclusion, our results substantiate the likely role of stathmin as an intracellular relay of extracellular regulations, as they point out its specific importance related to neuronal functions and brain differentiation.
KW - Glia
KW - Neuron
KW - Ontogenesis
KW - Phosphorylation
KW - Stathmin
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U2 - 10.1111/j.1471-4159.1989.tb11783.x
DO - 10.1111/j.1471-4159.1989.tb11783.x
M3 - Article
C2 - 2474633
AN - SCOPUS:0024391802
SN - 0022-3042
VL - 53
SP - 856
EP - 863
JO - Journal of neurochemistry
JF - Journal of neurochemistry
IS - 3
ER -