Calpain-induced light scattering by crystallins from three rodent species

Chiho Fukiage, Mitsuyoshi Azuma, Yoshikuni Nakamura, Yoshiyuki Tamada, Thomas (Tom) Shearer

Research output: Contribution to journalArticle

20 Citations (Scopus)

Abstract

The purpose of the present investigation was to compare in vitro light scattering in the soluble proteins from rodent lenses after hydrolysis by the calcium-activated protease, m-calpain (EC 3.4.22.17). Light scattering was measured in solutions of lens proteins from mice, rats, and guinea pigs after activation of endogenous m-calpain or after addition of purified m-calpain. We found for the first time that, in addition to rat, crystallins from another rodent lens, young mouse, were susceptible to calpain-induced light scattering. As in rats, aging of mouse lens prevented calpain-induced light scattering. Although crystallins from guinea pig lens were also partially hydrolysed by calpain, appreciable light scattering did not occur. Limited proteolysis may cause common changes in the biophysical properties of mouse and rat crystallins to decrease their solubility. Discovery of the nature of these biophysical changes may help our understanding as to why crystallins precipitate under cataractous conditions.

Original languageEnglish (US)
Pages (from-to)757-770
Number of pages14
JournalExperimental Eye Research
Volume65
Issue number6
DOIs
StatePublished - Dec 1997

Fingerprint

Crystallins
Calpain
Rodentia
Light
Lenses
Guinea Pigs
Solubility
Proteolysis
Hydrolysis
m-calpain

Keywords

  • Crystallins
  • Guinea pig
  • Lens
  • Light scattering
  • M-calpain protease
  • Mouse
  • Rat

ASJC Scopus subject areas

  • Ophthalmology
  • Sensory Systems

Cite this

Calpain-induced light scattering by crystallins from three rodent species. / Fukiage, Chiho; Azuma, Mitsuyoshi; Nakamura, Yoshikuni; Tamada, Yoshiyuki; Shearer, Thomas (Tom).

In: Experimental Eye Research, Vol. 65, No. 6, 12.1997, p. 757-770.

Research output: Contribution to journalArticle

Fukiage, Chiho ; Azuma, Mitsuyoshi ; Nakamura, Yoshikuni ; Tamada, Yoshiyuki ; Shearer, Thomas (Tom). / Calpain-induced light scattering by crystallins from three rodent species. In: Experimental Eye Research. 1997 ; Vol. 65, No. 6. pp. 757-770.
@article{df947d7c49fb4d53a2ed93aa4bb802d5,
title = "Calpain-induced light scattering by crystallins from three rodent species",
abstract = "The purpose of the present investigation was to compare in vitro light scattering in the soluble proteins from rodent lenses after hydrolysis by the calcium-activated protease, m-calpain (EC 3.4.22.17). Light scattering was measured in solutions of lens proteins from mice, rats, and guinea pigs after activation of endogenous m-calpain or after addition of purified m-calpain. We found for the first time that, in addition to rat, crystallins from another rodent lens, young mouse, were susceptible to calpain-induced light scattering. As in rats, aging of mouse lens prevented calpain-induced light scattering. Although crystallins from guinea pig lens were also partially hydrolysed by calpain, appreciable light scattering did not occur. Limited proteolysis may cause common changes in the biophysical properties of mouse and rat crystallins to decrease their solubility. Discovery of the nature of these biophysical changes may help our understanding as to why crystallins precipitate under cataractous conditions.",
keywords = "Crystallins, Guinea pig, Lens, Light scattering, M-calpain protease, Mouse, Rat",
author = "Chiho Fukiage and Mitsuyoshi Azuma and Yoshikuni Nakamura and Yoshiyuki Tamada and Shearer, {Thomas (Tom)}",
year = "1997",
month = "12",
doi = "10.1006/exer.1997.0381",
language = "English (US)",
volume = "65",
pages = "757--770",
journal = "Experimental Eye Research",
issn = "0014-4835",
publisher = "Academic Press Inc.",
number = "6",

}

TY - JOUR

T1 - Calpain-induced light scattering by crystallins from three rodent species

AU - Fukiage, Chiho

AU - Azuma, Mitsuyoshi

AU - Nakamura, Yoshikuni

AU - Tamada, Yoshiyuki

AU - Shearer, Thomas (Tom)

PY - 1997/12

Y1 - 1997/12

N2 - The purpose of the present investigation was to compare in vitro light scattering in the soluble proteins from rodent lenses after hydrolysis by the calcium-activated protease, m-calpain (EC 3.4.22.17). Light scattering was measured in solutions of lens proteins from mice, rats, and guinea pigs after activation of endogenous m-calpain or after addition of purified m-calpain. We found for the first time that, in addition to rat, crystallins from another rodent lens, young mouse, were susceptible to calpain-induced light scattering. As in rats, aging of mouse lens prevented calpain-induced light scattering. Although crystallins from guinea pig lens were also partially hydrolysed by calpain, appreciable light scattering did not occur. Limited proteolysis may cause common changes in the biophysical properties of mouse and rat crystallins to decrease their solubility. Discovery of the nature of these biophysical changes may help our understanding as to why crystallins precipitate under cataractous conditions.

AB - The purpose of the present investigation was to compare in vitro light scattering in the soluble proteins from rodent lenses after hydrolysis by the calcium-activated protease, m-calpain (EC 3.4.22.17). Light scattering was measured in solutions of lens proteins from mice, rats, and guinea pigs after activation of endogenous m-calpain or after addition of purified m-calpain. We found for the first time that, in addition to rat, crystallins from another rodent lens, young mouse, were susceptible to calpain-induced light scattering. As in rats, aging of mouse lens prevented calpain-induced light scattering. Although crystallins from guinea pig lens were also partially hydrolysed by calpain, appreciable light scattering did not occur. Limited proteolysis may cause common changes in the biophysical properties of mouse and rat crystallins to decrease their solubility. Discovery of the nature of these biophysical changes may help our understanding as to why crystallins precipitate under cataractous conditions.

KW - Crystallins

KW - Guinea pig

KW - Lens

KW - Light scattering

KW - M-calpain protease

KW - Mouse

KW - Rat

UR - http://www.scopus.com/inward/record.url?scp=0031437175&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0031437175&partnerID=8YFLogxK

U2 - 10.1006/exer.1997.0381

DO - 10.1006/exer.1997.0381

M3 - Article

VL - 65

SP - 757

EP - 770

JO - Experimental Eye Research

JF - Experimental Eye Research

SN - 0014-4835

IS - 6

ER -