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

1984 ◽  
Vol 224 (2) ◽  
pp. 609-616 ◽  
Author(s):  
J C Aster ◽  
G J Brewer ◽  
S M Hanash ◽  
H Maisel
Keyword(s):  
Ionic Strength ◽  
Epithelial Cells ◽  
Cell Membrane ◽  
Membrane Fraction ◽  
Lens Epithelial Cells ◽  
Red Cell Membrane ◽  
Bovine Lens ◽  
Deep Layers ◽  
Additional Protein ◽  
Low Ionic Strength

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.

scholarly journals Spectrin tetramer-dimer equilibrium in hereditary elliptocytosis

Blood ◽  
1982 ◽  
Vol 59 (5) ◽  
pp. 900-905 ◽  
Author(s):  
T Coetzer ◽  
S Zail
Keyword(s):  
Ionic Strength ◽  
Cell Membrane ◽  
Cell Membranes ◽  
Thermal Sensitivity ◽  
Red Cells ◽  
Red Cell ◽  
Red Cell Membrane ◽  
Hereditary Elliptocytosis ◽  
Red Cell Membranes ◽  
Low Ionic Strength

The proportion of spectrin tetramers and dimers in 4 degrees C low ionic strength extracts of red cell membranes of 9 subjects with 4 different variants of hereditary elliptocytosis (HE) and 2 subjects with hereditary spherocytosis (HS) was determined by nondenaturing gel electrophoresis. Such extracts reflect the native oligomeric state of spectrin in the red cell membrane. In two hemolytic HE variants (an unclassified adult with increased thermal sensitivity of red cells and an infant also showing increased thermal sensitivity of red cells), the proportion of dimers was increased, whereas the remaining subjects had values within the control range. Conversion of spectrin tetramers to dimers under isotonic conditions at 37 degrees C, or spectrin dimers to tetramers at 30 degrees C, resulted in a high proportion of dimers in the above two HE variants, as well as in a third variant with probable mild HE and sporadic hemolysis. The mother of the infant with elliptocytosis and increased thermal sensitivity of red cells, although hematologically normal, had an increased proportion of dimers in 4 degrees C low ionic strength extracts of her red cell membranes. These findings reflect an underlying primary or secondary abnormality of spectrin in these subjects that affects the association state of spectrin in the red cell membrane. Their exact relationship to the pathogenesis of the elliptical shape of the red cell, or to the presence of hemolysis, is at present unclear.

scholarly journals Spectrin tetramer-dimer equilibrium in hereditary elliptocytosis

Blood ◽  
1982 ◽  
Vol 59 (5) ◽  
pp. 900-905 ◽  
Author(s):  
T Coetzer ◽  
S Zail
Keyword(s):  
Ionic Strength ◽  
Cell Membrane ◽  
Cell Membranes ◽  
Thermal Sensitivity ◽  
Red Cells ◽  
Red Cell ◽  
Red Cell Membrane ◽  
Hereditary Elliptocytosis ◽  
Red Cell Membranes ◽  
Low Ionic Strength

Abstract The proportion of spectrin tetramers and dimers in 4 degrees C low ionic strength extracts of red cell membranes of 9 subjects with 4 different variants of hereditary elliptocytosis (HE) and 2 subjects with hereditary spherocytosis (HS) was determined by nondenaturing gel electrophoresis. Such extracts reflect the native oligomeric state of spectrin in the red cell membrane. In two hemolytic HE variants (an unclassified adult with increased thermal sensitivity of red cells and an infant also showing increased thermal sensitivity of red cells), the proportion of dimers was increased, whereas the remaining subjects had values within the control range. Conversion of spectrin tetramers to dimers under isotonic conditions at 37 degrees C, or spectrin dimers to tetramers at 30 degrees C, resulted in a high proportion of dimers in the above two HE variants, as well as in a third variant with probable mild HE and sporadic hemolysis. The mother of the infant with elliptocytosis and increased thermal sensitivity of red cells, although hematologically normal, had an increased proportion of dimers in 4 degrees C low ionic strength extracts of her red cell membranes. These findings reflect an underlying primary or secondary abnormality of spectrin in these subjects that affects the association state of spectrin in the red cell membrane. Their exact relationship to the pathogenesis of the elliptical shape of the red cell, or to the presence of hemolysis, is at present unclear.

Evidence for ATP and ubiquitin dependent degradation of proteins in cultured bovine lens epithelial cells

1991 ◽  
Vol 52 (3) ◽  
pp. 341-347 ◽  
Author(s):  
Jessica Jahngen-Hodge ◽  
Eric Laxman ◽  
Antoinette Zuliani ◽  
Allen Taylor
Keyword(s):  
Epithelial Cells ◽  
Lens Epithelial Cells ◽  
Bovine Lens

Effect of Rabbit Aqueous Humor Obtained after Cataract Surgery on Collagen Gel Contraction Induced by Bovine Lens Epithelial Cells

2000 ◽  
Vol 32 (2-3) ◽  
pp. 94-99 ◽  
Author(s):  
Daijiro Kurosaka ◽  
Katsuhiko Kato ◽  
Takeshi Oshima ◽  
Hiroyo Kurosaka ◽  
Mami Yoshino ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Cataract Surgery ◽  
Aqueous Humor ◽  
Collagen Gel ◽  
Lens Epithelial Cells ◽  
Bovine Lens ◽  
Collagen Gel Contraction

Hydrogen peroxide-induced DNA damage in bovine lens epithelial cells

1990 ◽  
Vol 240 (1) ◽  
pp. 35-45 ◽  
Author(s):  
Norman J. Kleiman ◽  
Ren-Rong Wang ◽  
Abraham Spector
Keyword(s):  
Hydrogen Peroxide ◽  
Dna Damage ◽  
Epithelial Cells ◽  
Lens Epithelial Cells ◽  
Bovine Lens
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