scholarly journals Structural organization of erythrocyte membrane microdomains and their relation with malaria susceptibility

2021 ◽  
Vol 4 (1) ◽  
Author(s):  
Anna Olivieri ◽  
Rebecca S. Lee ◽  
Federica Fratini ◽  
Cyrianne Keutcha ◽  
Mudit Chaand ◽  
...  
Keyword(s):  
Erythrocyte Membrane ◽  
Parasitophorous Vacuole ◽  
Protein Composition ◽  
Erythroid Cell ◽  
Membrane Microdomains ◽  
Associated Proteins ◽  
Endemic Population ◽  
Membrane Compartments ◽  
Adp Ribosyltransferase ◽  
Specific Cluster

AbstractCholesterol-rich microdomains are membrane compartments characterized by specific lipid and protein composition. These dynamic assemblies are involved in several biological processes, including infection by intracellular pathogens. This work provides a comprehensive analysis of the composition of human erythrocyte membrane microdomains. Based on their floating properties, we also categorized the microdomain-associated proteins into clusters. Interestingly, erythrocyte microdomains include the vast majority of the proteins known to be involved in invasion by the malaria parasite Plasmodium falciparum. We show here that the Ecto-ADP-ribosyltransferase 4 (ART4) and Aquaporin 1 (AQP1), found within one specific cluster, containing the essential host determinant CD55, are recruited to the site of parasite entry and then internalized to the newly formed parasitophorous vacuole membrane. By generating null erythroid cell lines, we showed that one of these proteins, ART4, plays a role in P. falciparum invasion. We also found that genetic variants in both ART4 and AQP1 are associated with susceptibility to the disease in a malaria-endemic population.

scholarly journals Structural membrane proteins and loosely associated proteins of the sarcoplasmic reticulum

1974 ◽  
Vol 139 (3) ◽  
pp. 509-513 ◽  
Author(s):  
A. Margreth ◽  
U. Carraro ◽  
G. Salviati
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Membrane Proteins ◽  
Osmotic Shock ◽  
Protein Composition ◽  
Polyacrylamide Gels ◽  
Associated Proteins

The protein composition of sarcoplasmic-reticulum vesicles, either unpurified or after fractionation on sucrose gradients, and with or without previous osmotic shock and sonication, was investigated by electrophoresis in acid polyacrylamide gels. The pattern of release of loosely bound proteins is discussed with respect to their localization in the interior of the vesicles.

scholarly journals Erythrocyte entry by malarial parasites. A moving junction between erythrocyte and parasite

1978 ◽  
Vol 77 (1) ◽  
pp. 72-82 ◽  
Author(s):  
M Aikawa ◽  
LH Miller ◽  
J Johnson ◽  
J Rabbege
Keyword(s):  
Electron Microscopy ◽  
Plasma Membrane ◽  
Erythrocyte Membrane ◽  
Plasmodium Knowlesi ◽  
Parasitophorous Vacuole ◽  
Initial Contact ◽  
Surface Coat ◽  
Iris Diaphragm ◽  
Erythrocyte Surface

Invasion of erythrocytes by merozoites of the monkey malaria, Plasmodium knowlesi, was investigated by electron microscopy. The apical end of the merozoite makes initial contact with the erythrocyte, creating a small depression in the erythrocyte membrane. The area of the erythrocyte membrane to which the merozoite is attached becomes thickened and forms a junction with the plasma membrane of the merozoite. As the merozoite enters the invagination in the erythrocyte surface, the junction, which is in the form of a circumferential zone of attachment between the erythrocyte and merozoite, moves along the confronted membranes to maintain its position at the orifice of the invagination. When entry is completed, the orifice closes behind the parasite in the fashion of an iris diaphragm, and the junction becomes a part of the parasitophorous vacuole. The movement of the junction during invasion is an important component of the mechanism by which the merozoite enters the erythrocyte. The extracellular merozoite is covered with a prominent surface coat. During invasion, this coat appears to be absent from the portion of the merozoite within the erythrocyte invagination, but the density of the surface coat outside the invagination (beyond the junction) is unaltered.

Altered erythrocyte membrane protein composition mirrors pleiotropic effects of hypertension susceptibility genes and disease pathogenesis

2015 ◽  
Vol 33 (11) ◽  
pp. 2265-2277 ◽  
Author(s):  
Alexey V. Polonikov ◽  
Dmitry V. Ushachev ◽  
Vladimir P. Ivanov ◽  
Mikhail I. Churnosov ◽  
Maxim B. Freidin ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Erythrocyte Membrane ◽  
Protein Composition ◽  
Susceptibility Genes ◽  
Pleiotropic Effects ◽  
Disease Pathogenesis ◽  
Erythrocyte Membrane Protein

scholarly journals Dynamics of putative raft-associated proteins at the cell surface

2004 ◽  
Vol 165 (5) ◽  
pp. 735-746 ◽  
Author(s):  
Anne K. Kenworthy ◽  
Benjamin J. Nichols ◽  
Catha L. Remmert ◽  
Glenn M. Hendrix ◽  
Mukesh Kumar ◽  
...  
Keyword(s):  
Cell Surface ◽  
Lipid Rafts ◽  
Long Range ◽  
Dominant Factor ◽  
Membrane Microdomains ◽  
Cholesterol Depletion ◽  
Biochemical Fractionation ◽  
Associated Proteins ◽  
Raft Domains

Lipid rafts are conceptualized as membrane microdomains enriched in cholesterol and glycosphingolipid that serve as platforms for protein segregation and signaling. The properties of these domains in vivo are unclear. Here, we use fluorescence recovery after photobleaching to test if raft association affects a protein's ability to laterally diffuse large distances across the cell surface. The diffusion coefficients (D) of several types of putative raft and nonraft proteins were systematically measured under steady-state conditions and in response to raft perturbations. Raft proteins diffused freely over large distances (>4 μm), exhibiting Ds that varied 10-fold. This finding indicates that raft proteins do not undergo long-range diffusion as part of discrete, stable raft domains. Perturbations reported to affect lipid rafts in model membrane systems or by biochemical fractionation (cholesterol depletion, decreased temperature, and cholesterol loading) had similar effects on the diffusional mobility of raft and nonraft proteins. Thus, raft association is not the dominant factor in determining long-range protein mobility at the cell surface.

scholarly journals Stable complexes of axoplasmic vesicles and microtubules: protein composition and ATPase activity.

1986 ◽  
Vol 103 (3) ◽  
pp. 957-968 ◽  
Author(s):  
M M Pratt
Keyword(s):  
Atpase Activity ◽  
Protein Composition ◽  
Giant Axon ◽  
High Molecular Mass ◽  
Macromolecular Complexes ◽  
Distinct Subset ◽  
Associated Proteins ◽  
Fast Transport ◽  
Loligo Pealei

Fast transport of axonal vesicles and organelles is a microtubule-associated movement (Griffin, J. W., K. E. Fahnestock, L. Price, and P. N. Hoffman, 1983, J. Neuroscience, 3:557-566; Schnapp, B. J., R. D. Vale, M. P. Sheetz, and T. S. Reese, 1984, Cell, 40:455-462; Allen, R. D., D. G. Weiss, J. H. Hayden, D. T. Brown, H. Fujiwake, and M. Simpson, 1985, J. Cell Biol., 100:1736-1752). Proteins that mediate the interactions of axoplasmic vesicles and microtubules were studied using stable complexes of microtubules and vesicles (MtVC). These complexes formed spontaneously in vitro when taxol-stabilized microtubules were mixed with sonically disrupted axoplasm from the giant axon of the squid Loligo pealei. The isolated MtVCs contain a distinct subset of axoplasmic proteins, and are composed primarily of microtubules and attached membranous vesicles. The MtVC also contains nonmitochondrial ATPase activity. The binding of one high molecular mass polypeptide to the complex is significantly enhanced by ATP or adenyl imidodiphosphate. All of the axoplasmic proteins and ATPase activity that bind to microtubules are found in macromolecular complexes and appear to be vesicle-associated. These data allow the identification of several vesicle-associated proteins of the squid giant axon and suggest that one or more of these polypeptides mediates vesicle binding to microtubules.

Subcellular distribution of 3 functional platelet SNARE proteins: human cellubrevin, SNAP-23, and syntaxin 2

Blood ◽  
2002 ◽  
Vol 99 (11) ◽  
pp. 4006-4014 ◽  
Author(s):  
Dian Feng ◽  
Katharine Crane ◽  
Nataliya Rozenvayn ◽  
Ann M. Dvorak ◽  
Robert Flaumenhaft
Keyword(s):  
Plasma Membrane ◽  
Subcellular Distribution ◽  
Molecular Mechanisms ◽  
Protein Composition ◽  
Immunoblot Analysis ◽  
Snare Proteins ◽  
Ultrastructural Studies ◽  
Streptolysin O ◽  
Membrane Compartments ◽  
Granule Secretion

Morphologic studies have demonstrated a process by which α-granule contents are released from platelets. Studies aimed at defining the molecular mechanisms of this release have demonstrated that SNARE proteins are required for α-granule secretion. These observations raise the possibility that morphologic features of α-granule secretion may be influenced by the subcellular distribution of SNARE proteins in the platelet. To evaluate this possibility, we analyzed the subcellular distribution of 3 functional platelet SNARE proteins—human cellubrevin, SNAP-23, and syntaxin 2. Exposure of streptolysin O-permeabilized platelets to antihuman cellubrevin antibody inhibited Ca++-induced α-granule secretion by approximately 50%. Inhibition of α-granule secretion by antihuman cellubrevin was reversed by a blocking peptide. Syntaxin 2 and SNAP-23 have previously been demonstrated to mediate platelet granule secretion. The subcellular localization of the 3 SNARE proteins was determined by ultrastructural studies, using a pre-embedding immunonanogold method, and by immunoblot analysis of subcellular fractions. Immunonanogold localization demonstrated that approximately 80% of human cellubrevin in resting platelets was localized to platelet granule membranes. In contrast, SNAP-23 localized predominantly to plasma membrane, whereas syntaxin 2 was more evenly distributed among membranes of α-granules, the open canalicular system, and plasma membrane. Thus, each of these SNARE proteins has a distinct subcellular distribution in platelets, and each of these membrane compartments demonstrates a unique SNARE protein composition. This distribution provides a basis for several characteristics of α-granule secretion that include homotypic α-granule fusion and the fusion of α-granules with the open canalicular system and plasma membrane.

scholarly journals Controlled Signaling—Insulin-Like Growth Factor Receptor Endocytosis and Presence at Intracellular Compartments

2021 ◽  
Vol 11 ◽  
Author(s):  
Leonie Rieger ◽  
Rosemary O’Connor
Keyword(s):  
Golgi Apparatus ◽  
Cancer Cells ◽  
Growth Factor Receptor ◽  
Cell Types ◽  
Specific Cell ◽  
Receptor Endocytosis ◽  
Intracellular Compartments ◽  
Associated Proteins ◽  
Membrane Compartments ◽  
And Function

Ligand-induced activation of the IGF-1 receptor triggers plasma-membrane-derived signal transduction but also triggers receptor endocytosis, which was previously thought to limit signaling. However, it is becoming ever more clear that IGF-1R endocytosis and trafficking to specific subcellular locations can define specific signaling responses that are important for key biological processes in normal cells and cancer cells. In different cell types, specific cell adhesion receptors and associated proteins can regulate IGF-1R endocytosis and trafficking. Once internalized, the IGF-1R may be recycled, degraded or translocated to the intracellular membrane compartments of the Golgi apparatus or the nucleus. The IGF-1R is present in the Golgi apparatus of migratory cancer cells where its signaling contributes to aggressive cancer behaviors including cell migration. The IGF-1R is also found in the nucleus of certain cancer cells where it can regulate gene expression. Nuclear IGF-1R is associated with poor clinical outcomes. IGF-1R signaling has also been shown to support mitochondrial biogenesis and function, and IGF-1R inhibition causes mitochondrial dysfunction. How IGF-1R intracellular trafficking and compartmentalized signaling is controlled is still unknown. This is an important area for further study, particularly in cancer.

scholarly journals RaftProt V2: understanding membrane microdomain function through lipid raft proteomes

2018 ◽  
Author(s):  
Ahmed Mohamed ◽  
Anup Shah ◽  
David Chen ◽  
Michelle M. Hill
Keyword(s):  
Experimental Evidence ◽  
Lipid Rafts ◽  
Lipid Raft ◽  
Protein Composition ◽  
Biological Data ◽  
Tissue Type ◽  
Membrane Microdomains ◽  
Membrane Rafts ◽  
Link Type ◽  
Membrane Microdomain

ABSTRACTCellular membranes feature dynamic submicrometer-scale lateral membrane domainsvariously referred to as lipid rafts, membrane rafts or glycosphingolipid-enriched microdomains (GEM). In order to understand the molecular functions of lipid rafts, numerous studies have utilized various biochemical methods to isolate and examine the protein composition of membrane rafts. However, interpretation of individual raft proteomics studies are confounded by the limitations of isolation methods and the dynamic nature of rafts. Knowledge-based approaches can facilitate biological data interpretation by integrating experimental evidence from existing studies. To this end, we previously developed RaftProt (http://lipid-raft-database.di.uq.edu.au/), a searchable database of mammalian lipid raft-associated proteins. Despite being a valuable and highly used resource, improvements in search capabilities and visualisation were still needed. Here, we present RaftProt V2 (http://raftprot.org), an improved update of RaftProt, enabling interrogation and integration of datasets at the cell/tissue type and UniRef/Gene level. Besides the addition of new datasets and re-mapping of all entries to both UniProt and UniRef IDs, we have annotated the level of experimental evidence for each protein entry. The search engine now allows for multiple protein or experiment searches where correlations, interactions or overlaps can be investigated. The web-interface has been completely re-designed and offers new interactive tools for data and subset selection, correlation analysis and network visualization. Overall, RaftProt aims to advance our understanding of lipid raft function by revealing the proteomes and pathways that are associated with membrane microdomains in diverse tissue and conditions.Database URL: http://raftprot.org

scholarly journals Toxic effect of puromycin on erythrocyte membranes which is unrelated to inhibition of protein synthesis

Blood ◽  
1975 ◽  
Vol 45 (1) ◽  
pp. 21-27 ◽  
Author(s):  
ER Burka ◽  
SK Ballas ◽  
SM Sabesin
Keyword(s):  
Protein Synthesis ◽  
Cell Membrane ◽  
Toxic Effect ◽  
Erythrocyte Membrane ◽  
Membrane Damage ◽  
Erythrocyte Membranes ◽  
Erythroid Cell ◽  
Ultrastructural Changes ◽  
Direct Toxic Effect ◽  
Increased Susceptibility

Abstract Exposure of rabbit or human erythrocytes to concentrations of puromycin as low as 7 x 10(-4)M for 2 hr causes damage to the cell membrane, as evidenced by increased susceptibility of the cells to hyposmotic lysis, increased cell rigidity, and ultrastructural changes consistent with severe membrane damage. Puromycin causes a concentration-dependent internalization of the erythrocyte membrane, resulting in vacuolization of the cells, at concentrations between 7 x 10(-4) M and 10(-2) M. Since the erythrocyte does not synthesize protein, the data indicate that puromycin has a direct toxic effect on erythroid cell membranes which is unrelated to its action in inhibiting the synthesis of protein.

Identification of the Dombrock blood group glycoprotein as a polymorphic member of the ADP-ribosyltransferase gene family

Blood ◽  
2000 ◽  
Vol 96 (7) ◽  
pp. 2621-2627 ◽  
Author(s):  
Alexander N. Gubin ◽  
J. Muthoni Njoroge ◽  
Urszula Wojda ◽  
Svetlana D. Pack ◽  
Maria Rios ◽  
...  
Keyword(s):  
Gene Family ◽  
Blood Group ◽  
Cell Biology ◽  
Specific Binding ◽  
Fetal Liver ◽  
Erythroid Differentiation ◽  
Single Amino Acid ◽  
Erythroid Cell ◽  
Blood Group System ◽  
Adp Ribosyltransferase

Abstract Identification of the 25 known human blood group molecules is of fundamental importance for the fields of erythroid cell biology and transfusion medicine. Here we provide the first molecular description of the “Dombrock” blood group system. A candidate gene was identified by in silico analyses of approximately 5000 expressed sequence tags (ESTs) from terminally differentiating human erythroid cells. Transfection experiments demonstrated specific binding of anti-Dombrock and confirmed glycosylphosphatidylinositol membrane attachment. Dombrock expression is developmentally regulated during erythroid differentiation and occurs at highest levels in the fetal liver. Homology studies suggest that the Dombrock molecule is a member of the adenosine 5′-diphosphate (ADP)–ribosyltransferase ectoenzyme gene family. Genotypic comparisons suggest Doa versus Dob antigenicity results from a single amino acid substitution within an encoded arginine-glycine-aspartic acid (RGD) motif of the molecule.

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