@article{3a40634a87a14b029025c03367934b75,
title = "Calpain in cultured bovine Lens epithelial cells",
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.",
author = "Lipman, {Ruth D.} and Cyr, {Deanna E.} and David, {Larry L.} and Allen Taylor",
note = "Funding Information: We would like to ackncwldge the generosity of time and materials for scanning electron rn.icrcsxpy of cultured cells by Sylvie Laliberte-Verdon, J. Sam Zigler for anti-alpha-crystallin sera, Merrell Dclw Research Institute for CbzValFAeH, the assistance of the Educational Media Center at TUfts-New England Medical Center with figures, and for the critical and helpful discussions with Jessica Jahngen-Hodge and Dr. Joseph J. Beqer. This project has been funded in part with Federal funds f m the U.S. Department of Agriculture, Agricultural Research -ice under contract nmber 53-3KO6-0-1. The contents of this publication do not necessarily reflect the views or policies of the U.S. Department of Agriculture, nor does mention of trade names, cannercia1 prcducts, or oryanizations inply endorsement by the U.S. Govexnment. partial support for this work was in the form of a fellmihip grant frum the National Eye Institute c105966-03 (R.D.L.) and a grant-in-aid fram Fight for Sight, Inc. GA89-046 (R.D.L.).",
year = "1991",
doi = "10.3109/02713689109007606",
language = "English (US)",
volume = "10",
pages = "11--17",
journal = "Current Eye Research",
issn = "0271-3683",
publisher = "Informa Healthcare",
number = "1",
}