Plasma membrane heterogeneity in ascites tumor cells. Isolation of a light and a heavy membrane fraction of the glycogen-free Ehrlich-Lettré substrain

Haeffner, E.W.; Kolbe, K.; Schroeter, D.; Paweletz, Neidhard

doi:10.1016/0005-2736(80)90389-2

Cited by 17 publications

(2 citation statements)

References 25 publications

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“…This yielded the post-nuclear plasma membrane-enriched fraction (PM). 17 From the correspondent supernatant, soluble cytoplasmic fractions were prepared, by ultracentrifugation at 200 000 Â g for 40 min. Detergent resistant membranes were isolated from the PM fraction, after treatment with cold Triton X-100 (1%) in MBS buffer (25 mM MES buffer, pH 6.5, 150 mM NaCl).…”

Section: Subcellular Fractionation and Microdomain Isolationmentioning

confidence: 99%

Protein profiling of microdomains purified from renal cell carcinoma and normal kidney tissue samples

et al. 2012

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Renal cell carcinoma (RCC) is representing about 3% of all adult cancers. A promising strategy for cancer biomarker discovery is subcellular comparative proteomics, allowing enriching specific cell compartments and assessing differences in protein expression patterns. We investigated the proteomic profile of a peculiar RCC subcellular compartment, plasma membrane microdomains (MD), involved in cell signalling, transport, proliferation and in many human diseases, such as cancer. Subcellular fractions were prepared by differential centrifugation from surgical samples of RCC and adjacent normal kidney (ANK). MD were isolated from plasma-membrane-enriched fractions after Triton X-100 treatment and sucrose density gradient ultracentrifugation. MD derived from RCC and ANK tissues were analyzed after SDS-PAGE separation by LC-ESI-MS/MS. We identified 93 proteins from MD isolated from RCC tissue, and 98 proteins from ANK MD. About 70% of the identified proteins are membrane-associated and about half of these are known as microdomain-associated. GRAVY scores assignment shows that most identified proteins (about 70%) are in the hydrophobic range. We chose a panel of proteins to validate their differential expression by WB. In conclusion, our work shows that RCC microdomain proteome is reproducibly different from ANK, and suggests that mining into such differences may support new biomarker discovery.

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Section: Subcellular Fractionation and Microdomain Isolationmentioning

confidence: 99%

Protein profiling of microdomains purified from renal cell carcinoma and normal kidney tissue samples

et al. 2012

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“…After a first centrifugation at 1,000 xg, for 10 min, followed by two washings, the nuclear pellet (P 1 ) was discarded and the three pooled supernatants were centrifuged at 14,500 xg for 15 min. This yielded the post-nuclear plasma membrane-enriched fraction (P 2 ) [22]. From the correspondent supernatant (Sn 2 ), soluble cytoplasmic (Sn 3 ) and microsomal-enriched fractions (P 3 ) were prepared, by ultracentrifugation at 200,000 xg for 40 min.…”

Section: Subcellular Fractionation and Microdomain Isolationmentioning

confidence: 99%

Caveolin-1 and Flotillin-1 Differential Expression in Clinical Samples of Renal Cell Carcinoma

Raimondo¹,

Valerio²,

Magni³

et al. 2008

TOPROTJ

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Abstract:Caveolin-1 and flotillin-1 belong to plasma membrane microdomains. They are characterized by peculiar lipid and protein composition and are involved in fundamental cellular events such as: signal transduction, cell adhesion, lipid/protein sorting, and human cancer. We addressed caveolin-1 and flotillin-1 expression in 30 human renal cell carcinoma (RCC) and adjacent normal kidney (ANK) samples by SDS-PAGE and immunoblotting with specific antibodies. Significant caveolin-1 and flotillin-1 over-expression was found in RCC tissues compared to ANK, and was confirmed by immunohistochemistry. Caveolin-1 and flotillin-1 protein levels were found by 1-D, 2-DE, and MS to be increased also in RCC microdomain-enriched subcellular fractions purified from paired RCC and ANK samples.

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Difference in plasma membrane structure between two sublines of ehrlich-lettrè ascites tumor cells

Haeffner

Heck

Kolbe

1982

Biochimica et Biophysica Acta (BBA) - Biomembranes

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Plasma membrane heterogeneity in ascites tumor cells. Isolation of a light and a heavy membrane fraction of the glycogen-free Ehrlich-Lettré substrain

Cited by 17 publications

References 25 publications

Protein profiling of microdomains purified from renal cell carcinoma and normal kidney tissue samples

Protein profiling of microdomains purified from renal cell carcinoma and normal kidney tissue samples

Caveolin-1 and Flotillin-1 Differential Expression in Clinical Samples of Renal Cell Carcinoma

Difference in plasma membrane structure between two sublines of ehrlich-lettrè ascites tumor cells

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