Abstract |
Heat shock protein 70 (HSP70) expression in the rabbit retina was evaluated in the ischemia-reperfusion model. Ischemia was induced by increasing the pressure in the anterior chamber, and the retinas were collected 1 or 12 h after reperfusion. HSP70 expression was examined by Western blot, confocal laser scanning microscopy and immunoelectron microscopy. Western blot showed that HSP70 was significantly increased in the retina 12 h after reperfusion, compared with normal control or 1 h after reperfusion. Confocal microscopy demonstrated that HSP70 was constitutive in Müller cells and that its expression was increased 12 h after reperfusion. Electron microscopy showed that glycogen-like granules were significantly decreased with prominent endoplasmic reticulum 1 h after reperfusion. Twelve hours after reperfusion, however, the density of glycogen-like granules was restored, and immunoelectron microscopy indicated that HSP70 was associated with the organelles of the Müller cells. Taken together, these data suggest that HSP70 in Müller cells plays a role in accommodation to stress.
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Authors | T Gohdo, H Ueda, S Ohno, H Iijima, S Tsukahara |
Journal | Ophthalmic research
(Ophthalmic Res)
2001 Sep-Oct
Vol. 33
Issue 5
Pg. 298-302
ISSN: 0030-3747 [Print] Switzerland |
PMID | 11586064
(Publication Type: Journal Article)
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Copyright | Copyright 2001 S. Karger AG, Basel |
Chemical References |
- HSP70 Heat-Shock Proteins
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Topics |
- Animals
- Blotting, Western
- HSP70 Heat-Shock Proteins
(metabolism)
- Microscopy, Confocal
- Microscopy, Immunoelectron
- Neuroglia
(metabolism, ultrastructure)
- Rabbits
- Reperfusion Injury
(metabolism, pathology)
- Retina
(metabolism, ultrastructure)
- Retinal Diseases
(metabolism, pathology)
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