Phospholipids in animal eukaryotic membranes: transverse asymmetry and movement

Zachowski, Alain

doi:10.1042/bj2940001

Cited by 778 publications

(596 citation statements)

References 210 publications

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“…Apparently, the cellular potential is critical for peptide channel formation in tumor cell membranes and could determine the selective killing of tumor cells by CAPs (Cruciani et al 1991). The interaction between CAPs and normal cells is not favored because of the overall neutral charge conferred by the zwitterionic major membrane components, such as sphingomyelin, phosphatidylethanolamine and phosphatidylcholine (Zachowski 1993).…”

Section: Antitumor Peptidesmentioning

confidence: 99%

Antifungal and antitumor models of bioactive protective peptides

Rodrigues

Dobroff

Taborda

et al. 2009

An. Acad. Bras. Ciênc.

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Peptides are remarkably reactive molecules produced by a great variety of species and able to display a number of functions in uni-and multicellular organisms as mediators, agonists and regulating substances. Some of them exert cytotoxic effects on cells other than those that produced them, and may have a role in controlling subpopulations and protecting certain species or cell types. Presently, we focus on antifungal and antitumor peptides and discuss a few models in which specific sequences and structures exerted direct inhibitory effects or stimulated a protective immune response. The killer peptide, deduced from an antiidiotypic antibody, with several antimicrobial activities and other Ig-derived peptides with cytotoxic activities including antitumor effects, are models studied in vitro and in vivo. Peptide 10 from gp43 of P. brasiliensis (P10) and the vaccine perspective against paracoccidioidomycosis is another topic illustrating the protective effect in vivo against a pathogenic fungus. The cationic antimicrobial peptides with antitumor activities are mostly reviewed here. Local treatment of murine melanoma by the peptide gomesin is another model studied at the Experimental Oncology Unit of UNIFESP.

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Section: Antitumor Peptidesmentioning

confidence: 99%

Antifungal and antitumor models of bioactive protective peptides

Rodrigues

Dobroff

Taborda

et al. 2009

An. Acad. Bras. Ciênc.

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“…Cells undergoing Fas-mediated apoptosis show externalization of phosphatidylserine (PS) (Martin et al, , 1996bConrad Liles et al, 1996), a phospholipid which is normally confined to the cytoplasmic leaflet of the membrane bilayer (Zachowski, 1993;Zwaal and Schroit, 1997), prior to other changes observed in apoptotic cells . To examine the occurrence of PS externalization upon influenza virus infection, cells were treated with fluorescein isothiocyanate (FITC)-labeled annexin V and propidium iodide (PI), and analyzed in a flow cytometer.…”

Section: Externalization Of Phosphatidylserine On the Surface Of Inflmentioning

confidence: 99%

Co-expression of Fas and Fas-ligand on the surface of influenza virus-infected cells

et al. 1998

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Influenza virus-infected cultured cells undergo apoptosis after an increment of Fas (APO-1/CD95) on the cell surface. By flow cytometry, cell surface Fas-ligand was detected in virusinfected cells with a time course similar to that of Fas. Moreover, Fas and Fas-ligand were co-expressed in those cells. The mode of induction, however, appeared to be distinct for the two proteins. Influenza virus infection induced the externalization of phosphatidylserine on the cell surface at the early stage of apoptosis, an event that has been observed in cells undergoing Fas-mediated apoptosis. In fact, apoptosis of the virus-infected cells was inhibited in the presence of an antagonistic anti-Fas-ligand monoclonal antibody. These results suggest that influenza virus infection causes augmented expression of both Fas and Fas-ligand and apoptosis is induced when the infected cells come into contact with each other.

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“…4 The unique feature of PM is the maintenance of membrane asymmetry by phosphatidylcholine and sphingomyelin, which are localized in the outer leaflet, whereas aminophospholipids such as phosphatidylserine (PS) and phosphatidylethanolamine are predominant in the inner leaflet of PM. This asymmetry is maintained by the concerted action of energy (ATP)-dependent phospholipid (PL) translocators, which include flippases and floppases (1)(2)(3)(4)(5). PM of eukaryotic cells is also equipped with a special class of PL translocators called human phospholipid scramblase 1(hPLSCR1).…”

mentioning

confidence: 99%

N-terminal Proline-rich Domain Is Required for Scrambling Activity of Human Phospholipid Scramblases

Rayala¹,

Francis²,

Sivagnanam³

et al. 2014

Journal of Biological Chemistry

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Background:The role of PRD in scrambling of phospholipids by hPLSCR1 is not known. Results:The addition of PRD of hPLSCR1 to hPLSCR2 restored its PL scrambling activity, which in turn leads to aggregation of the protein. Conclusion: PRD is crucial for PL scrambling activity and could probably mediate its function by metal ion-dependent oligomerization. Significance: The results provide an insight in understanding the mechanism of scramblases.

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Phospholipids in animal eukaryotic membranes: transverse asymmetry and movement

Cited by 778 publications

References 210 publications

Antifungal and antitumor models of bioactive protective peptides

Antifungal and antitumor models of bioactive protective peptides

Co-expression of Fas and Fas-ligand on the surface of influenza virus-infected cells

N-terminal Proline-rich Domain Is Required for Scrambling Activity of Human Phospholipid Scramblases

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