scholarly journals Lipid composition and fluidity of the erythrocyte membrane in copper-deficient rats

1992 ◽  
Vol 68 (2) ◽  
pp. 435-443 ◽  
Author(s):  
K. M. Abu-Salah ◽  
A. A. Alothman ◽  
K. Y. Lei
Keyword(s):  
Fatty Acid ◽  
Membrane Proteins ◽  
Erythrocyte Membrane ◽  
Lipid Composition ◽  
Phospholipid Fatty Acid ◽  
Sodium Dodecyl ◽  
Erythrocyte Membranes ◽  
Molar Ratio ◽  
Excimer Fluorescence ◽  
Cu Deficiency

The influence of dietary copper on lipid composition, phospholipid-fatty acid and protein profiles and fluidity of the erythrocyte membranes of rats is reported. In general Cu deficiency in rats induced some changes in the phospholipid-fatty acid profile of erythrocyte membranes when compared with Cu-adequate animals. Stearic (18:0) and docosadienoic (22:2n-3) acids contents, for example, were significantly increased (P< 0.001) while oleic (18:1n-9) and linolenic (18:3n-3) acid contents were significantly depressed (P< 0.001) as a result of Cu deficiency. Moreover the cholesterol:phospholipids molar ratio and the cholesterol (mol):membrane proteins (mg) ratio in Cu-deficient rats were, to different degrees, significantly lower than in animals fed on Cu-adequate diets. In addition, diets deficient in Cu led to a reduction in erythrocyte membrane fluidity (P< 0.001) as assessed by the intramolecular excimer fluorescence of 1,3-di(1-pyrenyI) propane. However, no significant alteration in the phospholipid:protein ratio was observed as a result of differences in dietary treatment. The pattern of erythrocyte membrane proteins obtained with sodium dodecyl sulphate-polyacrylamide gel electro-phoresis did not seem to be influenced by Cu-deficient diets.

scholarly journals Association of human erythrocyte membrane glycoproteins with blood-group Cad specificity

1982 ◽  
Vol 207 (3) ◽  
pp. 497-504 ◽  
Author(s):  
J P Cartron ◽  
D Blanchard
Keyword(s):  
Blood Group ◽  
Erythrocyte Membrane ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Membrane Receptors ◽  
Erythrocyte Membranes ◽  
Molar Ratio ◽  
Membrane Glycoproteins ◽  
Acetylneuraminic Acid ◽  
Group B

Sodium dodecyl sulphate/polyacrylamide-gel electrophoresis of erythrocyte membranes from a blood-group-B individual with the rare Cad phenotype indicates a lower-than-normal mobility of the main sialoglycoproteins, suggesting an increase in apparent molecular mass of 3kDa and 2kDa respectively for glycoprotein alpha (synonym glycophorin A) and glycoprotein delta (synonym glycophorin B). Since the chief structural determinant of Cad specificity is N-acetylgalactosamine, the membrane receptors have been isolated by affinity binding on immobilized Dolichos biflorus (horse gram) lectin. The predominant species eluted from the gel was the abnormal glycoprotein alpha, whereas in control experiments no material could be recovered from the adsorbent incubated with group-B Cad-negative erythrocyte membranes. After partition of the membranes with organic solvents, the blood-group-Cad activity was found in aqueous phases containing the sialoglycoproteins, but not in the organic phases containing simple or complex glycolipids, which, however, retained the blood-group-B activity. The carbohydrate composition of highly purified lipid-free glycoprotein alpha molecules prepared from Cad and control erythrocytes was determined. Interestingly the molar ratio of N-acetylneuraminic acid to N-acetylgalactosamine was equal to 2:1 in the case of controls and equal to 1:1 in the case of Cad erythrocytes. Taken together these results suggest that Cad specificity is defined by N-acetylgalactosamine residues carried by the alkali-labile oligosaccharide chains attached to the erythrocyte membrane sialo-glycoproteins.

Mo1138 Erythrocyte Membrane Phospholipid Fatty Acid Concentrations and Colorectal Adenomas: A Case Control in Tennessee

2014 ◽  
Vol 146 (5) ◽  
pp. S-568 ◽  
Author(s):  
Samara Rifkin ◽  
Martha J. Shrubsole ◽  
Qiuyin Cai ◽  
Walter E. Smalley ◽  
Reid Ness ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Erythrocyte Membrane ◽  
Phospholipid Fatty Acid ◽  
Case Control ◽  
Colorectal Adenomas ◽  
Membrane Phospholipid

scholarly journals Novel pathogenic XK mutations in McLeod syndrome and interaction between XK protein and chorein

2019 ◽  
Vol 5 (3) ◽  
pp. e328 ◽  
Author(s):  
Yuka Urata ◽  
Masayuki Nakamura ◽  
Natsuki Sasaki ◽  
Nari Shiokawa ◽  
Yoshiaki Nishida ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Erythrocyte Membrane ◽  
Molecular Analysis ◽  
Cultured Cells ◽  
Immunoblot Analysis ◽  
Erythrocyte Membranes ◽  
Onset Age ◽  
Novel Mutations ◽  
Erythrocyte Membrane Proteins ◽  
Normal Controls

ObjectiveTo identify XK pathologic mutations in 6 patients with suspected McLeod syndrome (MLS) and a possible interaction between the chorea-acanthocytosis (ChAc)- and MLS-responsible proteins: chorein and XK protein.MethodsErythrocyte membrane proteins from patients with suspected MLS and patients with ChAc, ChAc mutant carriers, and normal controls were analyzed by XK and chorein immunoblotting. We performed mutation analysis and XK immunoblotting to molecularly diagnose the patients with suspected MLS. Lysates of cultured cells were co-immunoprecipitated with anti-XK and anti-chorein antibodies.ResultsAll suspected MLS cases were molecularly diagnosed with MLS, and novel mutations were identified. The average onset age was 46.8 ± 8 years, which was older than that of the patients with ChAc. The immunoblot analysis revealed remarkably reduced chorein immunoreactivity in all patients with MLS. The immunoprecipitation analysis indicated a direct or indirect chorein-XK interaction.ConclusionsIn this study, XK pathogenic mutations were identified in all 6 MLS cases, including novel mutations. Chorein immunoreactions were significantly reduced in MLS erythrocyte membranes. In addition, we demonstrated a possible interaction between the chorein and XK protein via molecular analysis. The reduction in chorein expression is similar to that between Kell antigens and XK protein, although the chorein-XK interaction is a possibly noncovalent binding unlike the covalent Kell-XK complex. Our results suggest that reduced chorein levels following lack of XK protein are possibly associated with molecular pathogenesis in MLS.

Circular Dichroism Analysis of Native and Reaggregated Mycoplasma Membranes

1973 ◽  
Vol 51 (5) ◽  
pp. 632-636 ◽  
Author(s):  
Shlomo Rottem ◽  
Leonard Hayflick
Keyword(s):  
Circular Dichroism ◽  
Membrane Proteins ◽  
Sodium Dodecyl Sulfate ◽  
Lipid Composition ◽  
Sodium Dodecyl ◽  
Growth Cycle ◽  
Membrane Material ◽  
Α Helix ◽  
Low Amplitude ◽  
Circular Dichroïsm

Circular dichroism analyses of Acholeplasma laidlawii membranes solubilized by sodium dodecyl sulfate showed a typical α-helix spectrum. The estimated α-helix content was of the order of 35% calculated from the ellipticity at 208 nm of membranes solubilized by 20 mM SDS. Reaggregation of the solubilized membrane material to a membrane-like structure resulted in a distorted spectrum with low amplitude and red-shifted extrema like that of the native membranes. Throughout the growth cycle the circular dichroism spectra of membrane proteins remained the same despite the marked differences in membrane densities. The optical activity of the membranes was not affected by changing the lipid composition or extraction of over 90% of the lipids, although the latter resulted in marked destabilization of the proteins.

scholarly journals Incorporation and Clearance of Omega-3 Fatty Acids in Erythrocyte Membranes and Plasma Phospholipids

2006 ◽  
Vol 52 (12) ◽  
pp. 2265-2272 ◽  
Author(s):  
Jing Cao ◽  
Kerry A Schwichtenberg ◽  
Naomi Q Hanson ◽  
Michael Y Tsai
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Fish Oil ◽  
Erythrocyte Membrane ◽  
Flaxseed Oil ◽  
Erythrocyte Membranes ◽  
Omega 3 Fatty Acids ◽  
Omega 3 ◽  
Fatty Acid Supplementation ◽  
Plasma Phospholipids

Abstract Background: The sum of eicosapentaenoic acid (EPA, 20:5 ω3) and docosahexaenoic acid (DHA, 22:6 ω3) in erythrocyte membranes, termed the omega-3 index, can indicate suboptimal intake of omega-3 fatty acids, a risk factor for cardiovascular disease (CVD). To study the effects of fatty acid supplementation, we investigated the rate of incorporation and clearance of these fatty acids in erythrocyte membranes and plasma after intake of supplements. Methods: Twenty study participants received supplementation with either fish oil (1296 mg EPA + 864 mg DHA/day) or flaxseed oil (3510 mg alpha-linolenic acid + 900 mg linoleic acid/day) for 8 weeks. We obtained erythrocyte membrane and plasma samples at weeks 0, 4, 8, 10, 12, 14, 16, and 24 and extracted and analyzed fatty acids by gas chromatography. Results: After 8 weeks of fish oil supplementation, erythrocyte membrane EPA and DHA increased 300% (P &lt;0.001) and 42% (P &lt;0.001), respectively. The mean erythrocyte omega-3 index reached a near optimal value of 7.8%, and remained relatively high until week 12. EPA and DHA showed greater increases and more rapid washout period decreases in plasma phospholipids than in erythrocyte membranes. Flaxseed oil supplementation increased erythrocyte membrane EPA to 133% (P &lt;0.05) and docosapentaenoic acid (DPA, 22:5 ω3) to 120% (P &lt;0.01) of baseline, but DHA was unchanged. In plasma phospholipids, EPA, DPA, and DHA showed a slight but statistically insignificant increase. Conclusions: Erythrocyte membrane EPA+DHA increases during relatively short intervals in response to supplementation at rates related to amount of supplementation. These results may be useful to establish appropriate dosage for omega-3 fatty acid supplementation.

Erythrocyte membrane phospholipid fatty acid changes in cerebral palsy patients during nutritional rehabilitation—A response

Lipids ◽  
1993 ◽  
Vol 28 (10) ◽  
pp. 959-959
Author(s):  
Mary Ellen Harper ◽  
John Patrick ◽  
John K. G. Kramer ◽  
Mark S. Wolynetz
Keyword(s):  
Cerebral Palsy ◽  
Fatty Acid ◽  
Erythrocyte Membrane ◽  
Phospholipid Fatty Acid ◽  
Membrane Phospholipid ◽  
Nutritional Rehabilitation

scholarly journals Erythrocyte Membrane Phospholipid Fatty Acid Concentrations and Risk of Colorectal Adenomas: A Case–Control Nested in the French E3N-EPIC Cohort Study

2013 ◽  
Vol 22 (8) ◽  
pp. 1417-1427 ◽  
Author(s):  
Vanessa Cottet ◽  
Mélanie Collin ◽  
Anne-Sophie Gross ◽  
Marie-Christine Boutron-Ruault ◽  
Sophie Morois ◽  
...  
Keyword(s):  
Cohort Study ◽  
Fatty Acid ◽  
Erythrocyte Membrane ◽  
Phospholipid Fatty Acid ◽  
Case Control ◽  
Colorectal Adenomas ◽  
Membrane Phospholipid

Coisolation of glycophorin A and polyphosphoinositides from human erythrocyte membranes

1978 ◽  
Vol 56 (5) ◽  
pp. 349-351 ◽  
Author(s):  
J. Thomas Buckley
Keyword(s):  
Membrane Protein ◽  
Erythrocyte Membrane ◽  
Lipid Composition ◽  
Human Erythrocyte ◽  
Erythrocyte Membranes ◽  
Glycophorin A ◽  
Firm Conclusion ◽  
Membrane Phospholipids ◽  
Human Erythrocyte Membranes ◽  
Significant Enrichment

The lipid composition of purified erythrocyte membrane glycophorin was measured. Diphosphoinositide, triphosphoinositide, and phosphatidylserine are the major phospholipids in glycophorin preparations. Nearly all of the radioactive diphosphoinositide and triphosphoinositide extracted from erythrocyte membranes by lithium diiodosalicylate are recovered in purified glycophorin. There appeared to be no significant enrichment of other acidic membrane phospholipids in the protein. The results do not permit a firm conclusion as to whether the polyphosphoinositides are associated specifically with the membrane protein or whether fortuitous binding has occurred during purification.

Proteins of Marsupial Erythrocyte Membranes

1985 ◽  
Vol 38 (1) ◽  
pp. 121 ◽  
Author(s):  
GB Ralston
Keyword(s):  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Sodium Dodecyl ◽  
Tammar Wallaby ◽  
Erythrocyte Membranes ◽  
Blue Staining ◽  
Human Erythrocyte Membrane ◽  
Coomassie Blue Staining ◽  
Red Kangaroo ◽  
Western Grey Kangaroo

The proteins of erythrocyte membranes from the red kangaroo, western grey kangaroo, eastern grey wallaroo (euro), red-necked wallaby, Tammar wallaby, and brush-tail possum have been fractionated on acrylamide gels in the presence of sodium dodecyl sulfate. The pattern of proteins was remarkably similar between the different marsupial species. The pattern of Coomassie blue-staining proteins in the membranes of these species was also very similar to that of the human erythrocyte membrane. However, the glycoproteins in the marsupial erythrocyte membranes were markedly less conspicuous than those of the human erythrocyte membrane. Furthermore, the mobilities of the glycoproteins from the marsupials were different from those of the human erythrocyte membrane.

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