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

Kay, Marguerite M. B.; Sørensen, Keld E.; Wong, Patrick; Bolton, Peter

doi:10.1007/bf00242486

Cited by 51 publications

(52 citation statements)

References 84 publications

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“…However, they do not agree on the molecular changes responsible for generating the antigen. Our evidence suggests that senescent-cell antigen is derived from band 3, probably by degradation (10,(25)(26)(27)(28)(29)(30)(31); Lutz and his colleagues have suggested that senescent-cell antigen is a dimer ofband 3 (32); Sayare et al (33) have shown that band 3 can cross-link with hemoglobin under oxidative conditions; and Low et al (34) have presented evidence that clustered band 3 can generate senescent-cell antigen. These membrane events are not mutually exclusive.…”

mentioning

confidence: 65%

“…One hypothesis for the removal of senescent erythrocytes is that a "neo-antigen" appears on the surface of senescent cells leading to IgG binding and cellular removal (1)(2)(3)(4)(5)(6)(7)(8)(9)(10). The "neo-antigen" is recognized by the antigen binding, Fab, region (3,10,11) of a specific IgG autoantibody in serum that attaches to it and initiates the removal of cells by macrophages (1)(2)(3)(4).…”

mentioning

confidence: 99%

“…The "neo-antigen" is recognized by the antigen binding, Fab, region (3,10,11) of a specific IgG autoantibody in serum that attaches to it and initiates the removal of cells by macrophages (1)(2)(3)(4). A number of studies performed by us (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11) and by others have demonstrated the presence of IgG on senescent, damaged, and stored erythrocytes (12)(13)(14)(15)(16)(17)(18)(19)(20)1). In addition, workers in several laboratories have recently presented evidence that IgG binding is also involved in the removal of erythrocytes in diseases such as thalassemia (21) and sickle cell anemia (22,23).…”

mentioning

confidence: 99%

“…Senescent-cell antigen is a glycosylated 4.5 region polypeptide that appears to be derived from band 3 (5,8,10,(25)(26)(27). Senescent-cell antigen is located on an extracellular portion of band 3 that includes most ofthe 38-kDa carboxyl-terminal segment and 30% ofthe anion-transport region (27).…”

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confidence: 99%

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Oxidation as a possible mechanism of cellular aging: vitamin E deficiency causes premature aging and IgG binding to erythrocytes.

Kay¹,

Bosman²,

Shapiro³

et al. 1986

Proc. Natl. Acad. Sci. U.S.A.

102

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Senescent-cell antigen is a "neo-antigen" that appears on the surface of senescent cells and initiates IgG binding and cellular removal. As an approach to evaluating oxidation as a possible mechanism for generation of senescentcell antigen, we studied erythrocytes from vitamin E-deficient rats. Vitamin E is localized primarily in cellular membranes. Its major role is the termination of free-radical chain reactions propagated by the polyunsaturated fatty acids of membrane phospholipids. Results of our studies indicate that erythrocytes of all ages from vitamin E-deficient rats behave like old erythrocytes from normal rats, as determined by their susceptibility to phagocytosis, IgG binding, anion transport ability, and glyceraldehyde-3-phosphate dehydrogenase activity. Increased breakdown products of band 3 were observed with immunoblotting in membranes of erythrocytes from vitamin E-deficient rats. Breakdown products of band 3 are known to increase as cells age in normal individuals. The data suggest that oxidation may be a possible mechanism for erythrocyte aging and generation of senescent-cell antigen in vivo.

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confidence: 65%

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confidence: 99%

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confidence: 99%

mentioning

confidence: 99%

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Oxidation as a possible mechanism of cellular aging: vitamin E deficiency causes premature aging and IgG binding to erythrocytes.

Kay¹,

Bosman²,

Shapiro³

et al. 1986

Proc. Natl. Acad. Sci. U.S.A.

102

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“…Enzymatic fragments of erythrocytes were generated by standard methods (4,13,14). Rabbit antibody to band 3 and antibody 980, a rabbit antibody to aged band 3 (precursor to senescent cell antigen), were prepared as described (15)(16)(17). Monoclonal antibodies were a gift from Michael Jennings (University of Texas at Galveston).…”

mentioning

confidence: 99%

Alteration in membrane protein band 3 associated with accelerated erythrocyte aging.

Kay

Flowers

Goodman

et al. 1989

Proc. Natl. Acad. Sci. U.S.A.

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We report a human band 3 alteration that is associated with anemia as determined by a reticulocyte count of 20%. Erythrocyte defects included increased IgG binding, increased breakdown products of band 3, and altered anionand glucose-transport activity in middle-aged cells. These changes were observed during normal erythrocyte aging in situ. Binding of ankyrin to band 3 was normal. Serum/cell crossover studies indicated that a neoantigen appears on the propositus' erythrocytes to which IgG from both propositus and control serum binds as measured with a protein A binding assay. IgG eluted from the propositus' erythrocytes appeared to have a specificity for senescent cell antigen as determined by a phagocytosis inhibition assay. Immunoelectron microscopy showed that antibodies to band 3, which do not normally bind to intact erythrocytes, bound to the propositus' erythrocytes. Antibody 980 binds to normal old cells but not young or middle-aged cells. It also binds to a distinct region of band 3 in immunoblots of membranes from the propositus' middle-aged cells. Cells from both of the propositus' parents exhibited increased IgG binding and altered anion and glucose transport. The results of these studies suggest that (i) band 3 is aging prematurely in erythrocytes from the propositus, (it) senescent cell antigen appears on the propositus' middle-aged red cells, and (Ui) band 3 alterations observed in the propositus may have a genetic component.As part of our ongoing studies on mechanisms of cellular aging, we searched for models of accelerated and decelerated cellular aging. We anticipated that such models would allow us to dissect molecular aging and provide insight into mechanisms. Initially, we investigated models for aging in vitro (1).We subjected intact human erythrocytes to treatments that have been reported to result in changes in band 3 (the major anion-transport polypeptide) and/or to mimic aging in vitro.

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Molecular mechanism for the red blood cell senescence clock

Badior

Casey

2017

IUBMB Life

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Lacking protein synthesis machinery and organelles necessary for autophagy or apoptosis, aged red blood cells (RBCs) are marked by circulating auto-antibodies for macrophagemediated clearance. The antigen recognized by these autoantibodies is the major protein of the RBC membrane, Band 3. To ensure regulation and specificity in clearance, the molecular "clock" must mark senescent cells in a way that differentiates them from younger cells, to prevent premature clearance. Predominant models of Band 3 senescence signaling are reviewed, and merits are discussed in light of the recently published crystal structure of the Band 3 membrane domain.

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

Cited by 51 publications

References 84 publications

Oxidation as a possible mechanism of cellular aging: vitamin E deficiency causes premature aging and IgG binding to erythrocytes.

Oxidation as a possible mechanism of cellular aging: vitamin E deficiency causes premature aging and IgG binding to erythrocytes.

Alteration in membrane protein band 3 associated with accelerated erythrocyte aging.

Molecular mechanism for the red blood cell senescence clock

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