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Journal of Histochemistry and Cytochemistry, Vol. 48, 1195-1202, September 2000, Copyright © 2000, The Histochemical Society, Inc.

ARTICLE

Calcyclin (S100A6) Binding Protein (CacyBP) Is Highly Expressed in Brain Neurons

Beata Jastrzebskaa, Anna Filipeka, Dorota Nowickaa, Leszek Kaczmareka, and Jacek Kúznickia
a Department of Molecular and Cellular Neurobiology, Nencki Institute of Experimental Biology, Warsaw, Poland

Correspondence to: Anna Filipek, Nencki Institute of Experimental Biology, 3 Pasteur, 02-093 Warsaw, Poland. E-mail: anfil@nencki.gov.pl

The expression of a novel calcyclin (S100A6) binding protein (CacyBP) in different rat tissues was determined by Western and Northern blotting. Polyclonal antibodies against recombinant CacyBP purified from E. coli exhibited the highest reaction in the brain and weaker reaction in liver, spleen, and stomach. CacyBP immunoreactivity was also detected in lung and kidney. Densitometric analysis showed that the concentration of CacyBP in the soluble fractions of total brain and cerebellum is approximately 0.17 and 0.34 ng/µg protein, respectively. Northern blotting with a specific cDNA probe confirmed the high level of CacyBP expression in the rat brain and lower levels in other tissues examined. Immunohistochemistry and in situ hybridization of rat brain sections revealed strong expression of CacyBP in neurons of the cerebellum, hippocampus, and cortex. The in situ hybridization detected CacyBP in hippocampus as early as P7 (postnatal day 7) and a peak of expression at P21, and the expression signal was preserved until adulthood. In the entorhinal cortex, the peak of expression was observed at P7, whereas in the cerebellum it was seen at P21. The results presented here show that CacyBP is predominantly a neuronal protein. (J Histochem Cytochem 48:1195–1202)

Key Words: CacyBP, tissue and cell expression, neuronal localization


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