Phospholipid scramblase 3: a latent mediator connecting mitochondria and heavy metal apoptosis.

Lead and mercury are the ubiquitous heavy metals triggering toxicity and initiating apoptosis in cells. Though the toxic effects of heavy metals on various organs are known, there is a paucity of information on the mechanisms that instigate the current study. A plausible role of phospholipid scramblase 3 (PLSCR3) in Pb and Hg induced apoptosis was investigated with human embryonic kidney (HEK 293) cells.

Are cysteine residues of human phospholipid scramblase 1 essential for Pb and Hg binding-induced scrambling of phospholipids?

Lead and mercury being common environmental pollutants are often associated with erythrocytes, where phosphatidylserine (PS) exposure-mediated procoagulant activation is induced. Human phospholipid scramblase 1 (hPLSCR1) identified in the erythrocyte membrane is a type II transmembrane protein involved in Ca-dependent bidirectional scrambling of phospholipids (PL) during blood coagulation, cell activation, and apoptosis. The prominent role of hPLSCR1 in Pb and Hg poisoning was demonstrated by a biochemical assay, where recombinant hPLSCR1 induced PL scrambling across bilayer with a higher binding affinity (K) towards Hg (4.

Polystyrene adsorbents: rapid and efficient surrogate for dialysis in membrane protein purification.

Membrane protein purification is a laborious, expensive, and protracted process involving detergents for its extraction. Purifying functionally active form of membrane protein in sufficient quantity is a major bottleneck in establishing its structure and understanding the functional mechanism. Although overexpression of the membrane proteins has been achieved by recombinant DNA technology, a majority of the protein remains insoluble as inclusion bodies, which is extracted by detergents.

Plant extract mediated synthesis enhanced the functional properties of silver ferrite nanoparticles over chemical mediated synthesis.

In this study, the antibacterial, antioxidant and cytotoxicity behaviour of silver ferrite nanoparticles (AgFeO2 NPs) synthesized through chemical and green routes were compared. Green synthesis (Bio) of AgFeO2 NPs were prepared by precipitation method using Amaranthus blitum leaves extract as a reducing agent. Chemical synthesis (Che) of AgFeO2 NPs was mediated by sodium borohydride as a reducing agent.

Heavy-Metals-Mediated Phospholipids Scrambling by Human Phospholipid Scramblase 3: A Probable Role in Mitochondrial Apoptosis.

Human phospholipid scramblases are a family of four homologous transmembrane proteins (hPLSCR1-4) mediating phospholipids (PLs) translocation in plasma membrane upon Ca activation. hPLSCR3, the only homologue localized to mitochondria, plays a vital role in mitochondrial structure, function, maintenance, and apoptosis. Upon Ca activation, hPLSCR3 mediates PL translocation at the mitochondrial membrane enhancing t-bid-induced cytochrome c release and apoptosis.

Rapid method for an enhanced recovery of biologically active human phospholipid scramblase1 from inclusion bodies.

Human phospholipid scramblase 1 (hPLSCR1) is an ATP independent, Ca dependent transmembrane protein mediating bidirectional translocation of phospholipids across the lipid bilayer but the mechanism of scrambling is unknown. Determination of the hPLSCR1 structure would help understand the mechanism and its multi-functional property. Recombinant hPLSCR1 forms inclusion bodies (IBs), when over-expressed in E.

In vitro reconstitution and biochemical characterization of human phospholipid scramblase 3: phospholipid specificity and metal ion binding studies.

Human phospholipid scramblase 3 (hPLSCR3) is a single pass transmembrane protein that plays a vital role in fat metabolism, mitochondrial function, structure, maintenance and apoptosis. The mechanism of action of scramblases remains still unknown, and the role of scramblases in phospholipid translocation is heavily debated. hPLSCR3 is the only member of scramblase family localized to mitochondria and is involved in cardiolipin translocation at the mitochondrial membrane.

The role of human phospholipid scramblases in apoptosis: An overview.

Human phospholipid scramblases (hPLSCRs) are a family of four homologous single pass transmembrane proteins (hPLSCR1-4) initially identified as the proteins responsible for Ca mediated bidirectional phospholipid translocation in plasma membrane. Though in-vitro assays had provided evidence, the role of hPLSCRs in phospholipid translocation is still debated. Recent reports revealed a new class of proteins, TMEM16 and Xkr8 to exhibit scramblase activity challenging the function of hPLSCRs.