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Expression profile of heat shock protein 108 during retinal development in the chick
Jinsong Zhao1, Masahiko Yoneda, Yoko Inoue
1Department of Ophthalmology, Aichi Medical University, Nagakute, Aichi 480-1195, Japan, and Department of Ophthalmology, The Second Hospital of Jilin University, Changchun 130041, China.
Insights
Heat shock protein 108 (HSP108) expression in developing chick retinas shows two peaks, correlating with transferrin levels. This suggests HSP108 may play a role in retinal iron metabolism during development.
Area of Science:
- Ophthalmology
- Developmental Biology
- Molecular Biology
Background:
- Heat shock protein 108 (HSP108) has transferrin binding activity.
- Transferrin exhibits two expression peaks during chick retinal development.
- Previous studies demonstrated HSP108 at the mRNA level in developing chick retina.
Purpose of the Study:
- To investigate the protein expression profile of HSP108 in the developing chick retina.
- To determine the localization and expression levels of HSP108 throughout retinal development.
Main Methods:
- Immunohistochemistry using a monoclonal antibody specific for chick HSP108.
- Western blot analysis to measure HSP108 expression levels from embryonic day 12 (E12) to postnatal day 2 (P2) and in adults.
Main Results:
- HSP108 protein was localized in various retinal layers, including the ganglion cell layer, inner nuclear layer, outer plexiform layer, outer nuclear layer, photoreceptor inner segments, and retinal pigment epithelium.
- Two distinct peaks of HSP108 expression were observed around E13 and E18.
- The timing of HSP108 expression peaks correlated with previously observed transferrin expression peaks.
Conclusions:
- HSP108 is expressed throughout the developing chick retina at the protein level.
- The dual peaks of HSP108 expression during retinal development suggest a potential role in iron metabolism.
- HSP108 may be functionally associated with transferrin in regulating iron homeostasis during retinal development.
Abstract:
In the developing chick retina, heat shock protein 108 (HSP108), which exhibits transferrin binding activity, has been demonstrated at the mRNA level, while transferrin shows two expression peaks. Here, we investigated the expression profile of HSP108 in the developing chick retina at the protein level. The localization of HSP108 in embryonic days 15 (E15), E18, and postnatal day 2 (P2) chick retina was examined immunohistochemically using monoclonal antibody 9G10 specific for chick HSP108, while the expression levels of HSP108 in developing chick retina from E12 to P2 and adult were measured by Western blot analysis. HSP108 was expressed in the ganglion cell layer, inner nuclear layer, outer plexiform layer, outer nuclear layer, inner segments of photoreceptors and retinal pigment epithelium. Two peaks of HSP108 expression were found at around E13 and E18, respectively. Since the two HSP108 peaks appeared to be correlated with the transferrin expression peaks during retinal development, HSP108 may be associated with iron metabolism during the development of the retina.
