ALDEHYDE DEHYDROGENASE 1A1 IN GUINEA PIG CORNEA: MOLECULAR FEATURES AND TISSUE LOCALIZATION

SUAREZ MARÍA F; CORREA L; ESPOSITO E; A. URRETS-ZAVALÍA, JULIO; SERRA HM

Congreso; ARVO 2015; 2015

Since aldehyde dehydrogenase 1A1 (ALDH1A1) also contribute to cornealpreservation against oxidative stress, we decided to study the molecular aspectsand localization of this enzyme in guinea pig cornea.Total corneal extract as well as epithelium, stromaand endothelium extracts from male guinea pigs were used. The expression ofALDH1A1 was studied by means of immunoblotting, and immunofluorescence assays.The existence of isoforms for the enzyme was investigated by isoelectricfocusing.  ALDH1A1 from guinea pig corneas presents some uniquecharacteristics compared with other mammals. This enzyme has a molecular weightof about 54 kDa, as another crystalline present in the cornea (ALDH3A1),previously characterized by our group in corneal epithelial cells of normalguinea pigs. Isoelectric focusing studies revealed the existence of a singleisoenzyme for ALDH1A1 with a pI of approximately 9 as opposed to the twoisoforms of the enzyme ALDH3A1. Immunofluorescencestudies showed that ALDH1A1 enzyme as well as ALDH3A1 enzyme is expressed inepithelial cells, keratocytes and endothelial cells from the cornea.In this work we identified and molecularlycharacterized for the first time, the enzyme ALDH1A1 in the different cellular compartmentsof normal guinea pig cornea. We also describe their tissue location and compareit to the location of the other crystalline (ALDH3A1).