Developmental changes in human cerebellum: Expression of intracellular calcium receptors, calcium-binding proteins, and phosphorylated and nonphosphorylated neurofilament protein

Author(s):  
Ana Milosevic ◽  
Nada Zecevic
2019 ◽  
Vol 20 (9) ◽  
pp. 2146 ◽  
Author(s):  
Richard Fairless ◽  
Sarah K. Williams ◽  
Ricarda Diem

Neuronal subpopulations display differential vulnerabilities to disease, but the factors that determine their susceptibility are poorly understood. Toxic increases in intracellular calcium are a key factor in several neurodegenerative processes, with calcium-binding proteins providing an important first line of defense through their ability to buffer incoming calcium, allowing the neuron to quickly achieve homeostasis. Since neurons expressing different calcium-binding proteins have been reported to be differentially susceptible to degeneration, it can be hypothesized that rather than just serving as markers of different neuronal subpopulations, they might actually be a key determinant of survival. In this review, we will summarize some of the evidence that expression of the EF-hand calcium-binding proteins, calbindin, calretinin and parvalbumin, may influence the susceptibility of distinct neuronal subpopulations to disease processes.


1982 ◽  
Vol 243 (6) ◽  
pp. E483-E488 ◽  
Author(s):  
M. Thomasset ◽  
C. O. Parkes ◽  
P. Cuisinier-Gleizes

The tissue distribution, developmental changes, and the vitamin D dependence in the rat of two calcium-binding proteins [CaBPs, 28,000 and 10,000 Mr (28 and 10 K)] were examined. The radioimmunoassays used employed specific antibodies to either the human cerebellar CaBP (28 K protein) or to the smaller rat intestinal CaBP (10 K protein). The assay for the 28 K CaBP may be used to detect this protein in a number of mammalian species and tissues, whereas the 10 K CaBP assay appears to be specific only for the rat intestinal CaBP. This report demonstrates that the tissue distribution of the two CaBPs is different in the rat. High levels of the 28 H protein were found in the cerebellum and kidney, whereas the smaller CaBP was concentrated in the duodenum, jejunum, and cecum. Many other organs and tissues contained small quantities of both CaBPs. Developmental studies indicated some variability in the concentration of the CaBPs. Duodenum, kidney, and cerebellum all contained small amounts of one of the CaBPs prior to birth. Adult levels in all three tissues were already reached at 30 postpartum days. Levels of both CaBPs began to decline in rats older than 2 mo. The vitamin D dependence appeared to reflect cell turnover in that the duodenal and kidney CaBPs showed a vitamin D dependence not observed for the cerebellar protein.


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