Effect of galactose oxidase, with and without prior sialidase treatment, on the viability of erythrocytes in circulation.

Bell, William C.; Levy, Gerald N.; Williams, Revius; Aminoff, David

doi:10.1073/pnas.74.10.4205

Cited by 13 publications

(4 citation statements)

References 32 publications

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“…The existence of unmasked galactosyl residues on the rabbit RBC was previously indicated by the reactivity of circulating rabbit erythrocytes to peanut agglutinin (27). These results were later confirmed by Bell et al (44), who further demonstrated that the major product obtained from intact rabbit RBC by galactosidase treatment was found to be D-galactose. These data may suggest that the GO-sensitive sites on the rabbit erythropoietic cells are terminal galactosyl, and not N-acetylgalactosaminyl, residues.…”

Section: Discussionsupporting

confidence: 76%

Cell-type-related segregation of surface galactosyl-containing components at an early developmental stage in hemopoietic bone marrow cells in the rabbit.

Skutelsky¹,

Bayer²

1983

The Journal of Cell Biology

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The avidin-biotin complex was used for the selective ultrastructural labeling of terminal cell surface galactosyl residues. Rabbit bone marrow cells were treated with the enzyme galactose oxidase in the presence of biotin hydrazide. Subsequent treatment with ferritin-avidin conjugates enabled the electron microscopic visualization of terminal membrane-based galactose and/or N-acetylgalactosamine on these cells. All stages of erythroid development were characterized by high levels of exposed cell surface galactose, whereas all leukoid cells in the same preparations were virtually unlabled by the above method. Modulations in the distribution of these surface determinants during differentiation and maturation of rabbit erythroid cells were found to concur in inverse fashion with respect to that of terminal sialic acids. Neuraminidase treatment, before the above labeling procedure, resulted in the exposure of additional galactosyl residues on the surface of all bone marrow cell types.The results indicate that a galactose-bearing glycoconjugate(s) may comprise an erythroidspecific membrane constituent of rabbit bone marrow cells. The high density of galactose on the surface of even the earliest erythroid precursors may eventually enable the identification and isolation of a stem cell, which already contains the erythroid-specific galactoconjugate(s). The results suggest that variations in the spectrum of cell surface carbohydrates may serve as recognition signals in the complex set of intercellular interactions which occur during the development and maturation of the erythrocyte. The occurrence of similar but species-specific variations in the complement of surface heterosaccharides during erythroid development of humans and other mammals supports this contention.A considerable body of evidence has been accumulated concerning the primary role of cell surface saccharides in the control of cellular behavior and fate of blood cells (1-3). For example, the integrity of surface sialic acids and their continuity with respect to the carrier molecule on the cell surface have been linked to the control of the survival of circulating erythrocytes (4--13) and the phagocytosis of extruded erythroid nuclei in most mammals (14,15). In addition, changes in the normal level and/or distribution of surface sialic acid and terminal galactosyl residues have been implicated in the maturation, the release into circulation, and the homing of lymphoid cells (16,17), as well as the turnover of circulating sialoglycoproteins (18) and the pathological expression in certain diseased blood cells (6,19).It is generally believed that cell surface sialic acids have a "protective" role owing to a masking of cryptic recognition sites, e.g. specific saccharides (20, 21) and antigenic sites (7,22). Since, in most cell membrane glycoconjugates, sialic acid is attached either to a galactose or to an N-acetylgalactosamine residue (23,24), the masking and unmasking of these constituents are believed to be particularly important in the abovemention...

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Section: Discussionsupporting

confidence: 76%

Cell-type-related segregation of surface galactosyl-containing components at an early developmental stage in hemopoietic bone marrow cells in the rabbit.

Skutelsky¹,

Bayer²

1983

The Journal of Cell Biology

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“…One difference between the mouse and human erythrocyte surface which could be relevant to this point is the presence of antigens of the major histocompatibility complex on the surface of mouse cells in addition to blood group antigens [81]. The correlations which have been shown to exist between experimental modification of the terminal sialic acid or galactose/N-acetylgalactosaminyl residues of erythrocytes from several species and changes in blood clearance times [1,2,20,30,31,34,42] indicate the potential importance of such a modification. We have observed differences in the minor labeled proteins after lactoperoxidase catalyzed radioiodinization of mouse erythrocytes from different inbred strains 6, and these differences may be paralleled by differences in the surface glycoproteins, (ii) there is a relatively small number of glycoproteins incorporated into the mouse erythrocyte membrane, and artifactual or in vivo modification of these molecules produces a spectrum of products at various stages of modification.…”

Section: Discussionmentioning

confidence: 99%

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

1979

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The topography of the external surface of the Balb/c mouse erythrocyte has been investigated and compared to the human erythrocyte by using a series of protein radiolabeling probes. After sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the pattern of Coomassie Blue stained proteins was very similar for mouse and human erythrocyte ghosts, as was the distribution of radioactivity in protein bands after lactoperoxidase catalyzed radioiodination. The mouse erythrocyte glycoproteins identified by periodic-acid-Schiff and 'Stains-All' reagents, sialic acid analysis of gel slices, binding of 125I-wheat germ agglutinin and 125I-concanavalin A to the gels, and glycoprotein radiolabeling techniques, differed markedly from the sets of proteins labeled by radioiodination, and also differed from the human erythrocyte glycoproteins. Instead of the PAS I to PAS IV series of sialoglycoproteins characteristic of human erythrocytes, the mouse erythrocyte possesses a broad band of sialoglycoproteins with several peaks ranging in mol wt from 65,000 to 32,000. The same group of sialoglycoproteins were labeled by the periodate/B3H4-technique specific for terminal sialic acid, and the galactose oxidase/B3H4-method (plus neuraminidase) specific for galactosyl/N-acetylgalactosaminyl residues penultimate to sialic acid. These results emphasize the necessity to employ a variety of protein radiolabeling probes based on different labeling specificities, to study the membrane topography of cells which are poorly understood compared to the human erythrocyte membrane.

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“…Treatment of rat erythrocytes with galactose oxidase alone, followed by iv or ip transfusion, results in their sequestration in both the liver and spleen (Table II), implicating terminal galactose or N-acetylgalactosamine residues in rat RBC that are susceptible to oxidation with a concomitant loss of viability [22]. Table I11 shows the distribution of radioactivity in the parenchymal and nonparenchymal cells of liver, 24 hr post ip transfusion of aRBC.…”

Section: R Es U Lts Effects Of Excess Na251cr04 Label On Viability Ofmentioning

confidence: 98%

Studies on the sequestration of chemically and enzymatically modified erythrocytes

Smedsrød

Aminoff

1983

American J Hematol

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We have developed an experimental animal model to establish the patterns of sequestration of untreated, as well as chemically and enzymatically modified red blood cells (RBC). The intraperitoneal route of transfusion provides a useful way of transferring large numbers of untreated RBC into small animals and assuring their introduction into the circulation within 24 hr. Moreover, this route "filters" some types of modified erythrocytes, eg, glutaraldehyde treated RBC. From the pattern of sequestration, the RBC in the peritoneal cavity then pass through the liver where other types of modified RBC are sequestered, eg, after trypsin, pronase, protease, or sialidase treatment. Some modified RBC show a preference for the spleen as the site of sequestration, eg, galactose oxidase or N-ethylmaleimide treated RBC. These appear in the spleen despite intraperitoneal transfusion. Relevant to this study is the observation that in the rat old RBC are sequestered both by liver and spleen, while asialoerythrocytes are sequestered by liver only. A possible reason for this difference is discussed in the text.

show abstract

Effect of galactose oxidase, with and without prior sialidase treatment, on the viability of erythrocytes in circulation.

Cited by 13 publications

References 32 publications

Cell-type-related segregation of surface galactosyl-containing components at an early developmental stage in hemopoietic bone marrow cells in the rabbit.

Cell-type-related segregation of surface galactosyl-containing components at an early developmental stage in hemopoietic bone marrow cells in the rabbit.

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

Studies on the sequestration of chemically and enzymatically modified erythrocytes

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