Literature DB >> 18070278

Functions of red cell surface proteins.

G Daniels1.   

Abstract

The external membrane of the red cell contains numerous proteins that either cross the lipid bilayer one or more times or are anchored to it through a lipid tail. Many of these proteins express blood group activity. The functions of some of these proteins are known; in others their function can only be surmised from the protein structure or from limited experimental evidence. They are loosely divided into four categories based on their functions: membrane transporters; adhesion molecules and receptors; enzymes; and structural proteins that link the membrane with the membrane skeleton. Some of the proteins carry out more than one of these functions. Some proteins may complete their major functions during erythropoiesis or may only be important under adverse physiological conditions. Furthermore, some might be evolutionary relics and may no longer have significant functions. Polymorphisms or rare changes in red cell surface proteins are often responsible for blood groups. The biological significance of these polymorphisms or the selective pressures responsible for their stability within populations are mostly not known, although exploitation of the proteins by pathogenic micro-organisms has probably played a major role.

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Year:  2007        PMID: 18070278     DOI: 10.1111/j.1423-0410.2007.00970.x

Source DB:  PubMed          Journal:  Vox Sang        ISSN: 0042-9007            Impact factor:   2.144


  14 in total

1.  DARC, Glycophorin A, Band 3, and GLUT1 Diffusion in Erythrocytes: Insights into Membrane Complexes.

Authors:  Gayani C Kodippili; Katie Giger; Karson S Putt; Philip S Low
Journal:  Biophys J       Date:  2020-09-23       Impact factor: 4.033

2.  The Lombardy Rare Donor Programme.

Authors:  Nicoletta Revelli; Maria Antonietta Villa; Cinzia Paccapelo; Maria Cristina Manera; Paolo Rebulla; Anna Rita Migliaccio; Maurizio Marconi
Journal:  Blood Transfus       Date:  2013-02-21       Impact factor: 3.443

Review 3.  The molecular genetics of blood group polymorphism.

Authors:  Geoff Daniels
Journal:  Hum Genet       Date:  2009-08-29       Impact factor: 4.132

4.  Erythrocyte membrane proteins involved in the immune response to Plasmodium falciparum and Plasmodium vivax infection.

Authors:  Cristian Castro-Salguedo; Darío Mendez-Cuadro; Carlos Moneriz
Journal:  Parasitol Res       Date:  2021-04-02       Impact factor: 2.289

5.  Expression of the gene encoding secretor type galactoside 2 α fucosyltransferase (FUT2) and ABH antigens in patients with oral lesions.

Authors:  Carlos Campi; Livia Escovich; Alejandra Moreno; Liliana Racca; Amelia Racca; Carlos Cotorruelo; Claudia Biondi
Journal:  Med Oral Patol Oral Cir Bucal       Date:  2012-01-01

6.  Erythrocyte stiffness during morphological remodeling induced by carbon ion radiation.

Authors:  Baoping Zhang; Bin Liu; Hong Zhang; Jizeng Wang
Journal:  PLoS One       Date:  2014-11-17       Impact factor: 3.240

7.  Metabolism of the prodrug lisdexamfetamine dimesylate in human red blood cells from normal and sickle cell disease donors.

Authors:  Michael Pennick
Journal:  J Drug Assess       Date:  2013-02-13

Review 8.  Bio-inspired nanomaterials as novel options for the treatment of cardiovascular disease.

Authors:  Rajendran Jc Bose; Khan Ha; Jason R McCarthy
Journal:  Drug Discov Today       Date:  2021-02-06       Impact factor: 7.851

Review 9.  Acetylcholinesterase as a biomarker in environmental and occupational medicine: new insights and future perspectives.

Authors:  Maria Giulia Lionetto; Roberto Caricato; Antonio Calisi; Maria Elena Giordano; Trifone Schettino
Journal:  Biomed Res Int       Date:  2013-07-11       Impact factor: 3.411

10.  Apoptosis of non-parasitised red blood cells in Plasmodium yoelii malaria.

Authors:  Paulo Renato Rivas Totino; Raquel Alves Pinna; Ana Cecilia Amado Xavier de Oliveira; Dalma Maria Banic; Cláudio Tadeu Daniel-Ribeiro; Maria de Fátima Ferreira-da-Cruz
Journal:  Mem Inst Oswaldo Cruz       Date:  2013-09       Impact factor: 2.743

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