Sequence analysis of lens β-crystallins suggests involvement of calpain in cataract formation

Research output: Contribution to journalArticle

108 Citations (Scopus)

Abstract

Abnormal activation of the protease calpain in the lens may be a cause of cataracts. Cataracts were induced in 10-day-old rats by a single overdose of sodium selenite. The water-insoluble protein from the opaque lens nucleus was separated by two-dimensional electrophoresis, electroblotted onto membranes, and the NH2-terminal sequence of partially degraded β-crystallin polypeptides determined. Selenite cataractous lenses contained four major structural proteins, βB1, βB3, βA3/A1, and βA4 crystalline, missing from 5 to 49 amino acids from their NH2 termini. Incubation of intact β-crystallins with calpain II in vitro produced identical cleavage sites. This provided further evidence for the role of calpain in the production of light scattering insoluble protein in cataractous lenses and also suggested that a similar process may lead to lens protein insolubilization during aging.

Original languageEnglish (US)
Pages (from-to)1937-1940
Number of pages4
JournalJournal of Biological Chemistry
Volume268
Issue number3
StatePublished - Jan 25 1993

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Crystallins
Calpain
Cataract
Lenses
Sequence Analysis
Sodium Selenite
Selenious Acid
Proteins
Electrophoresis
Light scattering
Rats
Peptide Hydrolases
Aging of materials
Chemical activation
Crystalline materials
Membranes
Light
Amino Acids
Peptides
Water

ASJC Scopus subject areas

  • Biochemistry

Cite this

Sequence analysis of lens β-crystallins suggests involvement of calpain in cataract formation. / David, Larry; Shearer, Thomas (Tom); Shih, Marjorie.

In: Journal of Biological Chemistry, Vol. 268, No. 3, 25.01.1993, p. 1937-1940.

Research output: Contribution to journalArticle

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