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Originally published In Press as doi:10.1074/jbc.M009723200 on March 8, 2001

J. Biol. Chem., Vol. 276, Issue 23, 20735-20742, June 8, 2001
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Caspase Remodeling of the Spectrin Membrane Skeleton during Lens Development and Aging*

Andria LeeDagger , Jon S. Morrow§, and Velia M. FowlerDagger

From the Dagger  Department of Cell Biology, The Scripps Research Institute, La Jolla, California 92037 and the § Department of Pathology, Yale University School of Medicine, New Haven, Connecticut 06520

Terminal differentiation of lens fiber cells resembles the apoptotic process in that organelles are lost, DNA is fragmented, and changes in membrane morphology occur. However, unlike classically apoptotic cells, which are disintegrated by membrane blebbing and vesiculation, aging lens fiber cells are compressed into the center of the lens, where they undergo cell-cell fusion and the formation of specialized membrane interdigitations. In classically apoptotic cells, caspase cleavage of the cytoskeletal protein alpha -spectrin to ~150-kDa fragments is believed to be important for membrane blebbing. We report that caspase(s) cleave alpha -spectrin to ~150-kDa fragments and beta -spectrin to ~120- and ~80-kDa fragments during late embryonic chick lens development. These fragments continue to accumulate with age so that in the oldest fiber cells of the adult lens, most, if not all, of the spectrin is cleaved to discrete fragments. Thus, unlike classical apoptosis, where caspase-cleaved spectrin is short lived, lens fiber cells contain spectrin fragments that appear to be stable for the lifetime of the organism. Moreover, fragmentation of spectrin results in reduced membrane association and thus may lead to permanent remodeling of the membrane skeleton. Partial and specific proteolysis of membrane skeleton components by caspases may be important for age-related membrane changes in the lens.

* This work was supported in part by National Institutes of Health Grants EY10814 (to V. M. F.) and NS32578 and DK43812 (to J. S. M.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF354639.

To whom correspondence should be addressed: Dept. of Cell Biology, MB24, The Scripps Research Institute, 10550 N. Torrey Pines Rd., La Jolla, CA 92037. Tel.: 858-784-8277; Fax: 858-784-8753; E-mail: velia@scripps.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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