1999
DOI: 10.1002/(sici)1096-9861(19990208)404:2<235::aid-cne8>3.0.co;2-7
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Distribution of a specific calcium-binding protein of the S100 protein family, S100A6 (calcyclin), in subpopulations of neurons and glial cells of the adult rat nervous system

Abstract: S100A6 (calcyclin) is a member of the large S100 Ca2+‐binding protein family, considered to activate several processes along the calcium signal transduction pathway including the regulation of cell growth, proliferation, secretion, and exocytosis. In the present study, the distribution of S100A6 in the rat nervous system was examined by immunohistochemistry with a goat antiserum against recombinant human S100A6, which recognizes the rat S100A6 homologue. The main S100A6‐immunoreactive elements were 1) neuronal… Show more

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Cited by 65 publications
(38 citation statements)
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References 76 publications
(65 reference statements)
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“…Significant up-regulation of members of the S100 family was observed in E15 injured spinal cords. The greater up-regulation at E15 of calcyclin (S100A6), that has been associated with astrogliosis (Lesniak et al, 2009; Yachnis et al, 1993; Yamashita et al, 1999), may be due to the increase in astrocyte number with development and consequently greater astrogliotic response following injury. Altogether, the changes in the expression of Ca ++ -dependent molecules revealed by our screen reflect the changes in apoptosis and the degree of spinal cord damage occurring at the two developmental stages studied, strengthening the view that early response to injury is developmentally regulated and plays a crucial role in neural repair.…”
Section: Discussionmentioning
confidence: 99%
“…Significant up-regulation of members of the S100 family was observed in E15 injured spinal cords. The greater up-regulation at E15 of calcyclin (S100A6), that has been associated with astrogliosis (Lesniak et al, 2009; Yachnis et al, 1993; Yamashita et al, 1999), may be due to the increase in astrocyte number with development and consequently greater astrogliotic response following injury. Altogether, the changes in the expression of Ca ++ -dependent molecules revealed by our screen reflect the changes in apoptosis and the degree of spinal cord damage occurring at the two developmental stages studied, strengthening the view that early response to injury is developmentally regulated and plays a crucial role in neural repair.…”
Section: Discussionmentioning
confidence: 99%
“…In the brain, S100A6 protein was first described in neurons of the hippocampus, the cerebellum and the brain stem [2]. However, expression of S100A6 is not restricted to neurons of these brain regions; S100A6 is observed in a wide variety of brain structures, with high expression in neurons and in astrocytes and ependymal cells of the brain [3]. …”
Section: Introductionmentioning
confidence: 99%
“…Although the apparent typical location of S100 proteins is either plasma membrane-bound or cytoplasmic, the S100A6 protein has been localized with annexin II to the nuclear envelope of smooth muscle cells [17]. S100A6 has also been reported to be associated with subpopulation of neurons and glial cells [18]. S100 proteins have been implicated as modulators of Ca 2+ -dependent processes, such as secretion/neurotransmission [19][20][21] and intracellular Ca 2+ release [22].…”
Section: Introductionmentioning
confidence: 99%
“…In non-neuronal tissues, S100B and S100A1 are involved in the proper function and development of a variety of tissues [16][17][18][19][20][21][22][23][24][25][26][27][28][29][30][31][32][33][34][35]. The distribution of S100B and S100A1 has been categorized in a number of non-neuron tissues [36].…”
Section: Introductionmentioning
confidence: 99%