Literature DB >> 6517866

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

J C Aster, G J Brewer, S M Hanash, H Maisel.   

Abstract

Bovine lens epithelium, cortex and nucleus were screened for the presence of red-cell-membrane band 4.1-like proteins by using an immunoblot method. Lens epithelial cells were found to contain proteins of Mr 78 000 and higher (approximately 150 000) that cross-reacted with anti-(protein 4.1) sera. Fibre cells of the superficial cortex were also found to contain these two proteins, as well as an additional protein of approx. 80 000 Mr. In contrast, deep layers of the cortex and the lens nucleus contained no detectable cross-reactive protein at these Mr values. Treatment of a crude membrane fraction prepared from superficial bovine cortices with a low-ionic-strength buffer resulted in release of the high-Mr band 4.1-like protein. The 80 000- and 78 000-Mr proteins remained with the membrane fraction in low-ionic-strength buffer, but were released into solution by high-ionic-strength-buffer treatment. We have also demonstrated that the human red-blood-cell membrane, like lens epithelial cells and fibre cells, also contains a high-Mr band 4.1-like protein that is released from membranes by low-ionic-strength-buffer treatment.

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Year:  1984        PMID: 6517866      PMCID: PMC1144471          DOI: 10.1042/bj2240609

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  49 in total

1.  Spectrin-actin associations studied by electron microscopy of shadowed preparations.

Authors:  C M Cohen; J M Tyler; D Branton
Journal:  Cell       Date:  1980-10       Impact factor: 41.582

2.  Band 4.1 causes spectrin-actin gels to become thixiotropic.

Authors:  C M Cohen; C Korsgren
Journal:  Biochem Biophys Res Commun       Date:  1980-12-31       Impact factor: 3.575

3.  Associations of erythrocyte membrane proteins. Binding of purified bands 2.1 and 4.1 to spectrin.

Authors:  J M Tyler; B N Reinhardt; D Branton
Journal:  J Biol Chem       Date:  1980-07-25       Impact factor: 5.157

4.  Association between ankyrin and the cytoplasmic domain of band 3 isolated from the human erythrocyte membrane.

Authors:  V Bennett; P J Stenbuck
Journal:  J Biol Chem       Date:  1980-07-10       Impact factor: 5.157

5.  Reassociation of ankyrin with band 3 in erythrocyte membranes and in lipid vesicles.

Authors:  W R Hargreaves; K N Giedd; A Verkleij; D Branton
Journal:  J Biol Chem       Date:  1980-12-25       Impact factor: 5.157

6.  Regional differences in the composition of the bovine lens urea-soluble protein.

Authors:  S Nasser; R Bradley; J Alcala; H Maisel
Journal:  Exp Eye Res       Date:  1980-01       Impact factor: 3.467

7.  A photochemical crosslinking study of the subunit structure of membrane-associated spectrin.

Authors:  C R Middaugh; T H Ji
Journal:  Eur J Biochem       Date:  1980-09

8.  Red cell membrane in hemolytic disease. Studies on variables affecting electrophoretic analysis.

Authors:  N Sauberman; N L Fortier; G Fairbanks; R J O'Connor; L M Snyder
Journal:  Biochim Biophys Acta       Date:  1979-09-21

9.  Spectrin plus band 4.1 cross-link actin. Regulation by micromolar calcium.

Authors:  V Fowler; D L Taylor
Journal:  J Cell Biol       Date:  1980-05       Impact factor: 10.539

10.  Spectrin-dependent and -independent association of F-actin with the erythrocyte membrane.

Authors:  C M Cohen; S F Foley
Journal:  J Cell Biol       Date:  1980-08       Impact factor: 10.539

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  5 in total

1.  Aquaporin-0 interacts with the FERM domain of ezrin/radixin/moesin proteins in the ocular lens.

Authors:  Zhen Wang; Kevin L Schey
Journal:  Invest Ophthalmol Vis Sci       Date:  2011-07-07       Impact factor: 4.799

2.  Presence and localization of proteins immunologically related to erythrocyte protein 4.1 in human skin.

Authors:  T Shimizu; Y Takakuwa; H Koizumi; T Ishibashi; A Ohkawara
Journal:  Histochemistry       Date:  1991

3.  The 4.1-like proteins of the bovine lens: spectrin-binding proteins closely related in structure to red blood cell protein 4.1.

Authors:  J C Aster; G J Brewer; H Maisel
Journal:  J Cell Biol       Date:  1986-07       Impact factor: 10.539

4.  Lymphoma Thy-1 glycoprotein is linked to the cytoskeleton via a 4.1-like protein.

Authors:  L Y Bourguignon; S J Suchard; E L Kalomiris
Journal:  J Cell Biol       Date:  1986-12       Impact factor: 10.539

5.  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

  5 in total

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