Age-related changes in a fiber cell-specific extrinsic membrane protein

Research output: Contribution to journalArticle

35 Citations (Scopus)

Abstract

Western blot analysis using a monoclonal antibody raised against a lens fiber cell-specific, extrinsic membrane protein reveals several immunologically related bands in fractions derived from bovine lens. Previous work suggests that the parent molecule is the Mr 115 species, and that lower molecular weight bands represent the products of a progressive, step-wise, posttranslational degradation. In this report we compare the extent of proteolytic degradation in extracts prepared from the lens cortex and lens nucleus, using both protease-suppressive and protease-permissive isolation protocols. The results suggest that the observed degradation is a result of in vivo post-translational modification of the Mr 115 antigen, and thus represents physiologic aging of this protein. This analysis also suggests that degradation alters the solubility and/or membrane affinity of this antigen, resulting in a progressive shift to the insoluble phase.

Original languageEnglish (US)
Pages (from-to)1255-1262
Number of pages8
JournalCurrent Eye Research
Volume7
Issue number12
DOIs
StatePublished - 1988

Fingerprint

Lenses
Membrane Proteins
Peptide Hydrolases
Antigens
Post Translational Protein Processing
Solubility
Molecular Weight
Western Blotting
Monoclonal Antibodies
Membranes
Proteins

ASJC Scopus subject areas

  • Ophthalmology
  • Sensory Systems
  • Cellular and Molecular Neuroscience

Cite this

Age-related changes in a fiber cell-specific extrinsic membrane protein. / FitzGerald, Paul G.

In: Current Eye Research, Vol. 7, No. 12, 1988, p. 1255-1262.

Research output: Contribution to journalArticle

@article{98c1e3aea91d45e8ac9aff0d20fc8c3b,
title = "Age-related changes in a fiber cell-specific extrinsic membrane protein",
abstract = "Western blot analysis using a monoclonal antibody raised against a lens fiber cell-specific, extrinsic membrane protein reveals several immunologically related bands in fractions derived from bovine lens. Previous work suggests that the parent molecule is the Mr 115 species, and that lower molecular weight bands represent the products of a progressive, step-wise, posttranslational degradation. In this report we compare the extent of proteolytic degradation in extracts prepared from the lens cortex and lens nucleus, using both protease-suppressive and protease-permissive isolation protocols. The results suggest that the observed degradation is a result of in vivo post-translational modification of the Mr 115 antigen, and thus represents physiologic aging of this protein. This analysis also suggests that degradation alters the solubility and/or membrane affinity of this antigen, resulting in a progressive shift to the insoluble phase.",
author = "FitzGerald, {Paul G}",
year = "1988",
doi = "10.3109/02713688809033229",
language = "English (US)",
volume = "7",
pages = "1255--1262",
journal = "Current Eye Research",
issn = "0271-3683",
publisher = "Informa Healthcare",
number = "12",

}

TY - JOUR

T1 - Age-related changes in a fiber cell-specific extrinsic membrane protein

AU - FitzGerald, Paul G

PY - 1988

Y1 - 1988

N2 - Western blot analysis using a monoclonal antibody raised against a lens fiber cell-specific, extrinsic membrane protein reveals several immunologically related bands in fractions derived from bovine lens. Previous work suggests that the parent molecule is the Mr 115 species, and that lower molecular weight bands represent the products of a progressive, step-wise, posttranslational degradation. In this report we compare the extent of proteolytic degradation in extracts prepared from the lens cortex and lens nucleus, using both protease-suppressive and protease-permissive isolation protocols. The results suggest that the observed degradation is a result of in vivo post-translational modification of the Mr 115 antigen, and thus represents physiologic aging of this protein. This analysis also suggests that degradation alters the solubility and/or membrane affinity of this antigen, resulting in a progressive shift to the insoluble phase.

AB - Western blot analysis using a monoclonal antibody raised against a lens fiber cell-specific, extrinsic membrane protein reveals several immunologically related bands in fractions derived from bovine lens. Previous work suggests that the parent molecule is the Mr 115 species, and that lower molecular weight bands represent the products of a progressive, step-wise, posttranslational degradation. In this report we compare the extent of proteolytic degradation in extracts prepared from the lens cortex and lens nucleus, using both protease-suppressive and protease-permissive isolation protocols. The results suggest that the observed degradation is a result of in vivo post-translational modification of the Mr 115 antigen, and thus represents physiologic aging of this protein. This analysis also suggests that degradation alters the solubility and/or membrane affinity of this antigen, resulting in a progressive shift to the insoluble phase.

UR - http://www.scopus.com/inward/record.url?scp=0024210122&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0024210122&partnerID=8YFLogxK

U2 - 10.3109/02713688809033229

DO - 10.3109/02713688809033229

M3 - Article

VL - 7

SP - 1255

EP - 1262

JO - Current Eye Research

JF - Current Eye Research

SN - 0271-3683

IS - 12

ER -