Literature DB >> 6712654

Identification of spectrin and protein 4.1-like proteins in mammalian lens.

J C Aster, M J Welsh, G J Brewer, H Maisel.   

Abstract

Human, bovine, canine, and rabbit lenses were found to contain proteins which cross-react with anti-4.1 serum and which have molecular weights similar to erythrocyte proteins 4.1a and 4.1b (approximately 80 kd). Additionally, bovine, canine, and rabbit lenses contain a 4.1-like protein of approximately 125 kd which is absent from human lens. Proteins which cross-react with antibody to human erythrocyte spectrin were also detected. The human lens showed weak cross-reaction of bands of 240 kd and 225 kd, and a more intense cross-reaction of a band of 235 kd. Canine and bovine lenses showed weak cross-reaction with only the bands at 240 kd and 235 kd. The lens 240 kd band of all species also demonstrated calcium-dependent binding of calmodulin. Our results indicate that proteins related to, but distinct from, erythrocyte protein 4.1 and spectrin are found in mammalian lens.

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Year:  1984        PMID: 6712654     DOI: 10.1016/s0006-291x(84)80311-3

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  14 in total

1.  Selective expression of an erythroid-specific isoform of protein 4.1.

Authors:  T K Tang; T L Leto; I Correas; M A Alonso; V T Marchesi; E J Benz
Journal:  Proc Natl Acad Sci U S A       Date:  1988-06       Impact factor: 11.205

2.  Molecular analysis of insertion/deletion mutations in protein 4.1 in elliptocytosis. I. Biochemical identification of rearrangements in the spectrin/actin binding domain and functional characterizations.

Authors:  S L Marchesi; J Conboy; P Agre; J T Letsinger; V T Marchesi; D W Speicher; N Mohandas
Journal:  J Clin Invest       Date:  1990-08       Impact factor: 14.808

Review 3.  The lens actin filament cytoskeleton: Diverse structures for complex functions.

Authors:  Catherine Cheng; Roberta B Nowak; Velia M Fowler
Journal:  Exp Eye Res       Date:  2016-03-10       Impact factor: 3.467

4.  Regulated expression of multiple chicken erythroid membrane skeletal protein 4.1 variants is governed by differential RNA processing and translational control.

Authors:  J Ngai; J H Stack; R T Moon; E Lazarides
Journal:  Proc Natl Acad Sci U S A       Date:  1987-07       Impact factor: 11.205

5.  Characterization of isoforms of protein 4.1 present in the nucleus.

Authors:  I Correas
Journal:  Biochem J       Date:  1991-10-15       Impact factor: 3.857

6.  Modulation of erythrocyte membrane material properties by Ca2+ and calmodulin. Implications for their role in regulation of skeletal protein interactions.

Authors:  Y Takakuwa; N Mohandas
Journal:  J Clin Invest       Date:  1988-08       Impact factor: 14.808

7.  Band 4.1-like proteins of the bovine lens. Effects of differentiation, distribution and extraction characteristics.

Authors:  J C Aster; G J Brewer; S M Hanash; H Maisel
Journal:  Biochem J       Date:  1984-12-01       Impact factor: 3.857

8.  Restoration of normal membrane stability to unstable protein 4.1-deficient erythrocyte membranes by incorporation of purified protein 4.1.

Authors:  Y Takakuwa; G Tchernia; M Rossi; M Benabadji; N Mohandas
Journal:  J Clin Invest       Date:  1986-07       Impact factor: 14.808

9.  Cloning and structural characterization of a human non-erythroid band 3-like protein.

Authors:  D R Demuth; L C Showe; M Ballantine; A Palumbo; P J Fraser; L Cioe; G Rovera; P J Curtis
Journal:  EMBO J       Date:  1986-06       Impact factor: 11.598

10.  The 47-kD lens-specific protein phakinin is a tailless intermediate filament protein and an assembly partner of filensin.

Authors:  A Merdes; F Gounari; S D Georgatos
Journal:  J Cell Biol       Date:  1993-12       Impact factor: 10.539

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