Immunocytochemical and biochemical localization of parvalbumin in the retina
- 1 January 1986
- journal article
- research article
- Published by Springer Nature in Cell and tissue research
- Vol. 243 (1) , 213-217
- https://doi.org/10.1007/bf00221870
Abstract
The cellular distribution of parvalbumin-like immunoreactivity (PA-LI) in normal retina of rat, monkey, and human was investigated by immunohistochemical peroxidase antiperoxidase methods, and the levels of PA-LI in normal rat retina and brain were measured by radioimmunoassay. The antibody, raised in rabbits using rat skeletal muscle parvalbumin, did not cross-react with other Ca2+-binding proteins such as calmodulin or S-100 proteins. In rat retina, PA-LI-containing cells are located in the proximal inner nuclear layer and send processes to the external half of the internal plexiform layer, suggesting that they are amacrine cells. In monkey and human retina, PA-LI positive cells exist in the outermost sublayer of inner nuclear layer, and PA-LI-containing fibers that extend horizontally are found in the internal zone of outer plexiform layer. The radioimmunoassay revealed that the rat retina contained 1710±91 ng PA-LI/mg protein, the levels of which were higher than that of brain (881±165 ng PA-LI/mg protein). These results show an additional location for PA-LI outside skeletal muscle and brain, and also provide information on the function of interneurons of retina, which are still poorly understood.Keywords
This publication has 12 references indexed in Scilit:
- Parvalbumin Exists in Rat Endocrine GlandsEndocrinology, 1985
- Parvalbumin in non-muscle tissues of the rat. Quantitation and immunohistochemical localization.Journal of Biological Chemistry, 1984
- An immunocytochemical study on the localization of S-100 protein in the retina of ratsCell and tissue research, 1983
- Purification and characterization of adipose tissue S-100b protein.Journal of Biological Chemistry, 1983
- Correlation of parvalbumin concentration with relaxation speed in mammalian muscles.Proceedings of the National Academy of Sciences, 1982
- Calcium-binding protein parvalbumin as a neuronal markerNature, 1981
- The evolution of muscular parvalbumins investigated by the maximum parsimony methodJournal of Molecular Evolution, 1977
- The labelling of proteins to high specific radioactivities by conjugation to a 125I-containing acylating agent. Application to the radioimmunoassayBiochemical Journal, 1973
- Receptive fields of cones in the retina of the turtleThe Journal of Physiology, 1971
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970