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The biochemical modification of the erythrocyte membranes from women with ovarian cancer.

The aim of our work was quantitative evaluation of the protein and phospholipid fractions of mature erythrocyte membranes separated from women with ovarian cancer. Blood was sampled from 30 women with ovarian cancer, aged 24-79 years, in the third stage of clinical progression of the disease. Phosph...

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Autores principales: Kopczyński, Z., Kuźniak, J., Thielemann, A., Kaczmarek, J., Rybczyńska, M.
Formato: Texto
Lenguaje:English
Publicado: Nature Publishing Group|1 1998
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2063097/
https://www.ncbi.nlm.nih.gov/pubmed/9716028
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author Kopczyński, Z.
Kuźniak, J.
Thielemann, A.
Kaczmarek, J.
Rybczyńska, M.
author_facet Kopczyński, Z.
Kuźniak, J.
Thielemann, A.
Kaczmarek, J.
Rybczyńska, M.
author_sort Kopczyński, Z.
collection PubMed
description The aim of our work was quantitative evaluation of the protein and phospholipid fractions of mature erythrocyte membranes separated from women with ovarian cancer. Blood was sampled from 30 women with ovarian cancer, aged 24-79 years, in the third stage of clinical progression of the disease. Phospholipids were separated from membranes by Müller's acidic extraction method and analysed in thin-layer two-dimensional chromatography. On the silica gel plates nine fractions of phospholipids were separated: sphingomyelin (SPH), phosphatidylethanolamine (PE), phosphatidlyserine (PS), phosphatidylcholine (PC), lysophosphatidylcholine (LPC), phosphatidic acid (PA), phosphatidylinositol (Ptd Ins), phosphatidylinositol-4-phosphate (Ptd Ins-4-P), phosphatidylinositol-4,5-diphosphate (Ptd Ins-4,5-P2). The activity of phospholipase C in erythrocyte membranes was determined by Akhrem's spectrophotometric method. Membrane proteins were separated by polyacrylamide gel electrophoresis, SDS-PAGE. It was shown that PS, SPH, LPC and PA fractions were significantly diminished. The concentration of Ptd Ins-4-P and Ptd Ins-4,5-P2 was significantly increased with simultaneous reduction in Ptd Ins level. The inhibition of phospholipase C reached 80%. The quantitative protein evaluation showed a statistically significant decrease in spectrin and a significant increase in 4.1 protein. The quantitative changes, observed in phospholipid and protein fractions, led to the restructuring of the erythrocyte membrane cytoskeleton, which may be connected to increased susceptibility to haemolysis of red blood cells. IMAGES:
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spelling pubmed-20630972009-09-10 The biochemical modification of the erythrocyte membranes from women with ovarian cancer. Kopczyński, Z. Kuźniak, J. Thielemann, A. Kaczmarek, J. Rybczyńska, M. Br J Cancer Research Article The aim of our work was quantitative evaluation of the protein and phospholipid fractions of mature erythrocyte membranes separated from women with ovarian cancer. Blood was sampled from 30 women with ovarian cancer, aged 24-79 years, in the third stage of clinical progression of the disease. Phospholipids were separated from membranes by Müller's acidic extraction method and analysed in thin-layer two-dimensional chromatography. On the silica gel plates nine fractions of phospholipids were separated: sphingomyelin (SPH), phosphatidylethanolamine (PE), phosphatidlyserine (PS), phosphatidylcholine (PC), lysophosphatidylcholine (LPC), phosphatidic acid (PA), phosphatidylinositol (Ptd Ins), phosphatidylinositol-4-phosphate (Ptd Ins-4-P), phosphatidylinositol-4,5-diphosphate (Ptd Ins-4,5-P2). The activity of phospholipase C in erythrocyte membranes was determined by Akhrem's spectrophotometric method. Membrane proteins were separated by polyacrylamide gel electrophoresis, SDS-PAGE. It was shown that PS, SPH, LPC and PA fractions were significantly diminished. The concentration of Ptd Ins-4-P and Ptd Ins-4,5-P2 was significantly increased with simultaneous reduction in Ptd Ins level. The inhibition of phospholipase C reached 80%. The quantitative protein evaluation showed a statistically significant decrease in spectrin and a significant increase in 4.1 protein. The quantitative changes, observed in phospholipid and protein fractions, led to the restructuring of the erythrocyte membrane cytoskeleton, which may be connected to increased susceptibility to haemolysis of red blood cells. IMAGES: Nature Publishing Group|1 1998-08 /pmc/articles/PMC2063097/ /pubmed/9716028 Text en https://creativecommons.org/licenses/by/4.0/This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit https://creativecommons.org/licenses/by/4.0/.
spellingShingle Research Article
Kopczyński, Z.
Kuźniak, J.
Thielemann, A.
Kaczmarek, J.
Rybczyńska, M.
The biochemical modification of the erythrocyte membranes from women with ovarian cancer.
title The biochemical modification of the erythrocyte membranes from women with ovarian cancer.
title_full The biochemical modification of the erythrocyte membranes from women with ovarian cancer.
title_fullStr The biochemical modification of the erythrocyte membranes from women with ovarian cancer.
title_full_unstemmed The biochemical modification of the erythrocyte membranes from women with ovarian cancer.
title_short The biochemical modification of the erythrocyte membranes from women with ovarian cancer.
title_sort biochemical modification of the erythrocyte membranes from women with ovarian cancer.
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2063097/
https://www.ncbi.nlm.nih.gov/pubmed/9716028
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