Calpain in cultured bovine lens epithelial cells
- 1 January 1991
- journal article
- research article
- Published by Taylor & Francis in Current Eye Research
- Vol. 10 (1) , 11-17
- https://doi.org/10.3109/02713689109007606
Abstract
Calcium dependent proteolysis was examined in supernatant prepared from cultured bovine lens epithelial (BLE) cells. The presence of the calcium activated protease, calpain, was indicated by immunorecognition of 80 kDa and 30 kDa subunits of calpain in BLE cell supernatant. Degradation of 125I-alpha-crystallin and FTTC labeled casein by BLE cell supernatant were shown to be calcium dependent. Inhibition of activity was achieved with EGTA, calpastatin or CbzValPheH. The data presented are the first measurement of calpain activity in cultured lens cells.Keywords
This publication has 18 references indexed in Scilit:
- Aging and cellular maturation cause changes in ubiquitin-eye lens protein conjugatesPublished by Elsevier ,2004
- Lens proteasome shows enhanced rates of degradation of hydroxyl radical modified alpha-crystallinFree Radical Biology & Medicine, 1990
- Age-related changes in calpain II and calpastatin in rat lensExperimental Eye Research, 1989
- Intracellular protein degradation in cultured bovine lens epithelial cellsIn Vitro Cellular & Developmental Biology, 1988
- Protease activities in cultured beef lens epithelial cells peak and then decline upon progressive passageExperimental Eye Research, 1988
- Properties of the ubiquitin conjugation system from bovine eye lensCurrent Eye Research, 1988
- Calcium activated neutral protease: domain structure and activity regulationTrends in Biochemical Sciences, 1987
- Metal-dependent proteinase of the lens. Assay, purification and properties of the bovine enzymeBiochemical Journal, 1975
- [73] Spectrophotometric and turbidimetric methods for measuring proteinsPublished by Elsevier ,1957
- PLAQUE FORMATION AND ISOLATION OF PURE LINES WITH POLIOMYELITIS VIRUSESThe Journal of Experimental Medicine, 1954