L. Bezin et al., QUANTITATIVE STUDY OF TYROSINE-HYDROXYLASE PROTEIN-LEVELS WITHIN THE SOMATIC AREA OF THE RAT LOCUS-COERULEUS DURING POSTNATAL-DEVELOPMENT, The Journal of neuroscience, 14(12), 1994, pp. 7502-7510
To date only global dosages of tyrosine hydroxylase (TH) protein have
been realized in the locus coeruleus (LC) without discriminating the e
nzyme contained in the cell body area from the one in the surrounding
neuropil. The preceding immunohistochemical study (Bezin et al., 1994)
revealed a dramatic plasticity of the cellular expression of TH in th
e LC during the postnatal development of the rat. It was therefore nec
essary to develop a quantitative biochemical approach, strengthened by
a great anatomical resolution, to follow the developmental evolution
of TH levels exactly in the space containing the coerulean TH-immunore
active perikarya. In the present work two biochemical parameters neces
sary for precisely defining the phenotypic characterization of TH expr
ession within the rat LC have been established during the postnatal de
velopment at six different stages: postnatal day 4 (PND4), PND10, PND1
4, PND21, PND30, and PND42. TH tissue concentration and content were p
recisely determined along the caudorostral extent of the LC within the
previously (Bezin et al., 1994) defined spaces delimited by the TH-co
ntaining perikarya. TH tissue concentration remained quite stable duri
ng the postnatal development. TH quantity exhibited few age-related va
riations with a transient peak at PND10 and followed the same evolutio
n as the volume containing the TH-expressing perikarya. The mean cell
contribution to the total quantity of TH measured in the whole LC show
ed important age-related fluctuations with a dramatic peak at PND10 fo
llowed by a drastic decrease until PND21. Such modifications of the st
eady-state levels of TH in the perikarya of coerulean neurons could be
related to temporal requirements of this enzyme in their other cellul
ar compartments such as dendrites or terminals, and/or alterations of
the synthesis of the protein.