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Immunohistochemical and immunochemical localization of heat shock protein 27KD in the developing rat retina: The differential localization from alpha-B crystallin

, : Immunohistochemical and immunochemical localization of heat shock protein 27KD in the developing rat retina: The differential localization from alpha-B crystallin. Acta Histochemica et Cytochemica 28(4): 299-304

The localization of two stress proteins, small heat shock protein (HSP27) and alpha-B crystallin, in the developing rat retina were studied immunohistochemically and immunochemically, using the antibodies for HSP27 and alpha-B crystallin. At embryonic day 15, the immunoreactivity to alpha-B crystallin was observed in some cells in the neural retina and in the pigment epithelium (PE). At postnatal day (P) 5, immunoreactivity to HSP27 was first observed in the inner limiting membrane (ILM), nerve fiber layer (NFL) and PE. Immunoreactivity to alpha-B crystallin was present in almost the same portions of the retina. At P10, the differentiating outer segments of the photoreceptor cells (ROS) and PE were intensely immunoreactive to alpha-B crystallin, as compared with other layers, while the ILM, NFL and some portions of PE were immunoreactive to HSP27. At time progressed, immunoreactivity to HSP27 in the IPL and alpha-B crystallin in the ROS increased. Our enzyme immunoassay of the retina revealed that the concentration of HSP27 gradually increased over time. In contrast, the concentration of alpha-B crystallin increased after birth and reached almost to adult level at P30. The concentration of HSP27 was much lower as compared to that of alpha-B crystallin. The differences in locations and changes in the levels of concentration between HSP27 and alpha-B crystallin suggested that these two stress proteins may have different functions in the developing retina.


DOI: 10.1267/ahc.28.299

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