Age-related changes in human lens crystallins identified by two- dimensional electrophoresis and mass spectrometry

Kirsten Lampi, Zhixiang Ma, Stacy R A Hanson, Misuyoshi Azuma, Marjorie Shih, Thomas (Tom) Shearer, David L. Smith, Jean B. Smith, Larry David

Research output: Contribution to journalArticle

194 Citations (Scopus)

Abstract

The purpose of this study was to identify the major protein components in adult human lenses and to analyse the specific age-related changes in these proteins using two-dimensional electrophoresis, Edman sequencing, and in conjunction with the data in the accompanying manuscript, mass spectrometry. The majority of changes in the two-dimensional electrophoretic pattern of lens proteins occurred prior to 17 years of age, and included a decrease in proteins migrating to the original positions of βB1, βB3, βA3, γC and γD, and the appearance of many new species with apparent molecular weights on two-dimensional electrophoretic gels similar to βB2 and βS, but having more acidic pIs. These proteins were identified as deamidated forms of βB1 and βA3/A1 missing portions of their N-terminal extensions. With the exception of αB, deamidation was detected in all crystallin species. These data indicated that a major fraction of the water-soluble protein of the adult human lens is composed of truncated βB1 and βA3/A1 crystallins, and that nearly all human crystallins, including the β-crystallins, are susceptible to deamidation. The results also provided the most detailed map to date of the identities of protein species on two-dimensional electrophoresis gels of adult human lenses.

Original languageEnglish (US)
Pages (from-to)31-43
Number of pages13
JournalExperimental Eye Research
Volume67
Issue number1
DOIs
StatePublished - Jul 1998

Fingerprint

Crystallins
Lenses
Electrophoresis
Mass Spectrometry
Proteins
Manuscripts
Electrophoresis, Gel, Two-Dimensional
Molecular Weight
Gels
Water

Keywords

  • Aging
  • Crystallins
  • Deamidation
  • Human
  • Lens
  • Mass spectrometry
  • Proteolysis
  • Two-dimensional electrophoresis

ASJC Scopus subject areas

  • Ophthalmology
  • Sensory Systems

Cite this

Age-related changes in human lens crystallins identified by two- dimensional electrophoresis and mass spectrometry. / Lampi, Kirsten; Ma, Zhixiang; Hanson, Stacy R A; Azuma, Misuyoshi; Shih, Marjorie; Shearer, Thomas (Tom); Smith, David L.; Smith, Jean B.; David, Larry.

In: Experimental Eye Research, Vol. 67, No. 1, 07.1998, p. 31-43.

Research output: Contribution to journalArticle

Lampi, Kirsten ; Ma, Zhixiang ; Hanson, Stacy R A ; Azuma, Misuyoshi ; Shih, Marjorie ; Shearer, Thomas (Tom) ; Smith, David L. ; Smith, Jean B. ; David, Larry. / Age-related changes in human lens crystallins identified by two- dimensional electrophoresis and mass spectrometry. In: Experimental Eye Research. 1998 ; Vol. 67, No. 1. pp. 31-43.
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