Literature DB >> 1008055

Effect of sialidase on the viability of erythrocytes in circulation.

D Aminoff, W C Bell, I Fulton, N Ibgebrigtsen.   

Abstract

Sialic acid has been detected on the erythrocyte surface of a number of different species of animals. The objective of this investigation was to determine the physiological significance of these sialyl residues to the viability of erythrocytes in circulation. Methods have been described for the determination of total sialic acid on red blood cells and the conditions under which it may be released with sialidase. Chicken, dog, goat, and rabbit were chosen for these studies because of the differences in the amount (3 X 10(6) - 72 X 10(6) resides per erythrocyte), and type (N-acetyl-or N-glycolyl-neuraminic acids) of sialic acid found on the surface of their erythrocytes. Radioactive tagging with Na251CrO4 was used to monitor the effect of sialidase on the viability of erythrocytes upon autologous transfusion. By the two criteria used to assess the viability of erythrocytes-the percentage of erythrocytes surviving 24 hr after the autologous transfusion, and the half-life of those red blood cells in circulation that survive the first 24 h after the autologous transfusion, and the half-life of those red blood cells in circulation that survive the first 24 hr-it is apparent that the presence of sialic acid on the cell surface is crucial for the survival of nonnucleated mammalian erythrocytes. The loss of viability of dog erythrocytes can be elicited by the removal of approximately 10% of the total sialic acid. In marked contrast to the behavior of mammalian erythrocytes, sialidase-treated chicken erythrocytes appear to retain their viability in circulation.

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Year:  1976        PMID: 1008055     DOI: 10.1002/ajh.2830010407

Source DB:  PubMed          Journal:  Am J Hematol        ISSN: 0361-8609            Impact factor:   10.047


  18 in total

1.  Identification of differences between the surface proteins and glycoproteins of normal mouse (Balb/c) and human erythrocytes.

Authors:  R J Howard; P M Smith; G F Mitchell
Journal:  J Membr Biol       Date:  1979-08       Impact factor: 1.843

Review 2.  Use of mouse models to study the mechanisms and consequences of RBC clearance.

Authors:  E A Hod; S A Arinsburg; R O Francis; J E Hendrickson; J C Zimring; S L Spitalnik
Journal:  Vox Sang       Date:  2010-03-21       Impact factor: 2.144

3.  Abnormal blood-group-Ss-active sialoglycoproteins in the membrane of Miltenberger class III, IV and V human erythrocytes.

Authors:  D J Anstee; W J Mawby; M J Tanner
Journal:  Biochem J       Date:  1979-11-01       Impact factor: 3.857

4.  Role of sialic acid in survival of erythrocytes in the circulation: interaction of neuraminidase-treated and untreated erythrocytes with spleen and liver at the cellular level.

Authors:  D Aminoff; W F Bruegge; W C Bell; K Sarpolis; R Williams
Journal:  Proc Natl Acad Sci U S A       Date:  1977-04       Impact factor: 11.205

5.  Adhesion and erythrophagocytosis of human senescent erythrocytes by autologous monocytes and their inhibition by beta-galactosyl derivatives.

Authors:  J Vaysse; L Gattegno; D Bladier; D Aminoff
Journal:  Proc Natl Acad Sci U S A       Date:  1986-03       Impact factor: 11.205

6.  Detection of erythrocyte membrane proteins, sialoglycoproteins, and lipids in the same polyacrylamide gel using a double-staining technique.

Authors:  J K Dzandu; M E Deh; D L Barratt; G E Wise
Journal:  Proc Natl Acad Sci U S A       Date:  1984-03       Impact factor: 11.205

Review 7.  Antigenicity, storage, and aging: physiologic autoantibodies to cell membrane and serum proteins and the senescent cell antigen.

Authors:  M M Kay; K Sorensen; P Wong; P Bolton
Journal:  Mol Cell Biochem       Date:  1982-11-26       Impact factor: 3.396

8.  Identification of Mycoplasma pneumoniae proteins associated with hemadsorption and virulence.

Authors:  D C Krause; D K Leith; R M Wilson; J B Baseman
Journal:  Infect Immun       Date:  1982-03       Impact factor: 3.441

9.  Autosomal locus regulates inverse relationship between sialic acid content and capacity of mouse erythrocytes to activate human alternative complement pathway.

Authors:  U E Nydegger; D T Fearon; K F Austen
Journal:  Proc Natl Acad Sci U S A       Date:  1978-12       Impact factor: 11.205

10.  Human erythrocyte sialidase is linked to the plasma membrane by a glycosylphosphatidylinositol anchor and partly located on the outer surface.

Authors:  A Chiarini; A Fiorilli; L Di Francesco; B Venerando; G Tettamanti
Journal:  Glycoconj J       Date:  1993-02       Impact factor: 2.916

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