Alterations in the localization of calbindin D28K-, calretinin-, and parvalbumin-immunoreactive neurons of rabbit retinal ganglion cell layer from ischemia and reperfusion.
Calcium-binding proteins are thought to play important roles in calcium buffering. The present study investigated the effects of ischemia and reperfusion on calbindin D28K, calretinin, and parvalbumin immunoreactivity in the ganglion cell layer of the rabbit. Rabbits were administered ischemic damage by increasing the intraocular pressure. After 60 and 90 min of ischemia, reperfusion (7 d) was allowed to occur. The b-wave of the electroretinogram (ERG) was reduced by more than 50% and almost 80% in retina given ischemia for 60 and 90 min, respectively. The oscillatory potential (OPs) wave was reduced approximately 50% at 60 min ischemia and 70% at 90 min ischemia. In both normal and ischemic-treated retina, calcium-binding protein immunoreactivity was seen in many cells in the ganglion cell layer. In eyes subjected to 60 min ischemia, there was a decrease of the density of calbindin D28K- (8.29%), calretinin- (14.44%), and parvalbumin- (26.83%) immunoreactive (IR) cells compared to the control retina. In eyes subjected to 90 min ischemia, there was a higher decrease of the density of calbindin D28K- (18.48%), calretinin- (33.59%), and parvalbumin- (54.26%) IR cells than at 60 min. Some calcium-binding protein-IR neurons, especially calretinin-IR neurons, showed aggregations that were abnormally packed together in retina subjected to ischemia for 90 min. The results show that calbindin D28K-, calretinin-, and parvalbumin-IR cells in the ganglion cell layer are susceptible to ischemic damage and reperfusion. The degree of reduction varied among different calcium-binding proteins and ischemic damage times. These results suggest that calbindin D28K-containing neurons are less susceptible to ischemic damage than calretinin- and parvalbumin-containing neurons in the ganglion cell layer of rabbit retina.
Kwon
Oh-Ju
OJ
Department of Biology, College of Natural Sciences, Kyungpook National University, Daegu 702-701, Korea.
Kim
Jung-Yeol
JY
Kim
Si-Yeol
SY
Jeon
Chang-Jin
CJ
D000818:Animals; D064032:Calbindin 2; D064026:Calbindins; D004596:Electroretinography; D005136:Eye Proteins / Q000032:analysis*; D007511:Ischemia / Q000503:physiopathology; D009474:Neurons / Q000737:chemistry / Q000276:immunology; D009798:Ocular Hypertension / Q000503:physiopathology; D010320:Parvalbumins / Q000032:analysis* / Q000276:immunology; D011817:Rabbits; D015427:Reperfusion Injury / Q000503:physiopathology*; D012165:Retinal Ganglion Cells / Q000737:chemistry*; D064030:S100 Calcium Binding Protein G / Q000032:analysis* / Q000276:immunology
D064032:Calbindin 2; D064026:Calbindins; D005136:Eye Proteins; D010320:Parvalbumins; D064030:S100 Calcium Binding Protein G