The Biological Life of the Red Cell

Berlin, Nathaniel I.; Berk, Paul D.

doi:10.1016/b978-0-12-677202-9.50017-4

Cited by 49 publications

(38 citation statements)

References 247 publications

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“…It remains largely unknown how macrophages are able to distinguish young and normal RBCs from damaged or senescent RBCs. [1][2][3] However, the CD47-SHPS-1 system potentially participates in such regulation. In addition, enhancement of CD47-SHPS-1 signal would be useful for the therapy of various types of anemia such as hemolytic anemia, which is caused by enhanced destruction of RBCs in the spleen.…”

Section: Discussionmentioning

confidence: 99%

“…We transfused CFSE-labeled RBCs from WT donor mice into 1,46,47 Whereas the half-life of transfused RBCs in WT mice was 330 Ϯ 31 hours, it was only 180 Ϯ 32 hours in SHPS-1 mutant mice (means Ϯ SE, n ϭ 5, P Ͻ .05). Transfusion of CFSE-labeled RBCs from SHPS-1 mutant donor mice revealed that the half-life of the labeled RBCs in WT recipients (326 Ϯ 32 hours, n ϭ 5) was similar to that of WT donor cells in WT recipients.…”

Section: Shortened Lifespan Of Circulating Rbcs In Shps-1 Mutant Micementioning

confidence: 99%

“…[1][2][3] The production of RBCs is controlled by the primary erythropoietic regulator erythropoietin, 2,4 whereas clearance of old RBCs by the spleen is achieved mostly as a result of their specific recognition and phagocytosis by splenic macrophages. 5,6 The precise molecular mechanism by which splenic macrophages recognize senescent RBCs for phagocytosis is largely unknown, however.…”

Section: Introductionmentioning

confidence: 99%

“…5,6 The precise molecular mechanism by which splenic macrophages recognize senescent RBCs for phagocytosis is largely unknown, however. [1][2][3] Src homology 2 domain-containing protein tyrosine phosphatase substrate-1 (SHPS-1), 7,8 also known as signal-regulatory protein ␣, 9 brain immunoglobulin (Ig)-like molecule with tyrosinebased activation motifs, 10 and p84 neural adhesion molecule, 11 is a transmembrane protein that is especially abundant in macrophages. [12][13][14] The putative extracellular region of SHPS-1 comprises 3 Ig-like domains, and its cytoplasmic region contains 4 tyrosine phosphorylation sites that mediate the binding of Src homology 2 domain-containing protein tyrosine phosphatases designated SHP-1 and SHP-2.…”

Section: Introductionmentioning

confidence: 99%

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SHPS-1 promotes the survival of circulating erythrocytes through inhibition of phagocytosis by splenic macrophages

Ishikawa-Sekigami

Kaneko

Okazawa

et al. 2006

Blood

111

112

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IntroductionThe lifespan of circulating red blood cells (RBCs) is approximately 120 and 40 days in humans and mice, respectively, and is determined by their production in bone marrow (BM) and their clearance from the peripheral circulation, predominantly in the spleen and liver. [1][2][3] The production of RBCs is controlled by the primary erythropoietic regulator erythropoietin, 2,4 whereas clearance of old RBCs by the spleen is achieved mostly as a result of their specific recognition and phagocytosis by splenic macrophages. 5,6 The precise molecular mechanism by which splenic macrophages recognize senescent RBCs for phagocytosis is largely unknown, however. [1][2][3] Src homology 2 domain-containing protein tyrosine phosphatase substrate-1 (SHPS-1), 7,8 also known as signal-regulatory protein ␣, 9 brain immunoglobulin (Ig)-like molecule with tyrosinebased activation motifs, 10 and p84 neural adhesion molecule, 11 is a transmembrane protein that is especially abundant in macrophages. [12][13][14] The putative extracellular region of SHPS-1 comprises 3 Ig-like domains, and its cytoplasmic region contains 4 tyrosine phosphorylation sites that mediate the binding of Src homology 2 domain-containing protein tyrosine phosphatases designated SHP-1 and SHP-2. 7,9 Tyrosine phosphorylation of SHPS-1 is regulated by various growth factors and cytokines as well as by integrinmediated cell adhesion to extracellular matrix proteins. 7,9,[15][16][17][18] SHPS-1 thus functions as a docking protein to recruit and activate SHP-1 or SHP-2 at the cell membrane in response to extracellular stimuli. In macrophages, tyrosine-phosphorylated SHPS-1 binds SHP-1, 12,19,20 which is implicated in negative regulation of the functions of a variety of hematopoietic cells. [21][22][23] The complex of SHPS-1 and SHP-1 is thus thought to regulate macrophage functions in a negative manner.CD47 is a ligand for the extracellular region of SHPS-1. 24,25 This protein, which was originally identified in association with ␣v␤3 integrin, is also a member of the Ig superfamily, possessing an Ig-V-like extracellular domain, 5 putative membrane-spanning segments, and a short cytoplasmic tail. 26 CD47 and SHPS-1 constitute a cell-cell communication system (the CD47-SHPS-1 system) that plays important roles in a variety of cellular processes including cell migration, 27,28 adhesion of B cells, 29 and T-cell activation. 14,30 In addition, the CD47-SHPS-1 system is implicated in negative regulation of phagocytosis by macrophages. CD47 is highly expressed on the surface of RBCs, where it associates with the Rh protein complex instead of with integrins. 31 The rate of clearance of CD47-deficient RBCs from the bloodstream was found to be markedly increased compared with that of wild-type (WT) cells. 6,32 Furthermore, the phagocytosis of CD47-deficient RBCs by splenic or BM-derived macrophages was greatly enhanced Supported by a Grant-in-Aid for Scientific Research on Priority Areas Cancer; a Grant-in-Aid for Scientific Research (B); a Grant-in-Aid for Young Scie...

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Section: Discussionmentioning

confidence: 99%

Section: Shortened Lifespan Of Circulating Rbcs In Shps-1 Mutant Micementioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

SHPS-1 promotes the survival of circulating erythrocytes through inhibition of phagocytosis by splenic macrophages

Ishikawa-Sekigami

Kaneko

Okazawa

et al. 2006

Blood

111

112

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“…If this were the case, then the predilection of different Plasmodium species to red blood cells of different ages (from reticulocytes to mature and possibly ageing normocytes) might well be accounted for by variations in the density of some receptors at the surface of the red blood cell. The fact that red blood cells are devoid of DNA does not preclude the appearance and increase of surface receptor as the red cell ages, as it is known that age-related alteration of the membrane leads to the exposure of some proteins that were inaccessible in the young red blood cell (Killmann, 1964;Berlin and Berk, 1975;Ballas et al, 1986;Clark, 1988;Woolley et al, 2000). However, experimental approaches that aim to elucidate the nature of the parasite's red blood cell tropism are actually quite restricted.…”

Section: Invasion Of Host Cells By Malaria Parasites 239mentioning

confidence: 99%

Invasion of host cells by malaria parasites: a tale of two protein families

Iyer

Grüner

Rénia

et al. 2007

Molecular Microbiology

130

124

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SummaryMalaria parasites are obligate intracellular parasites whose invasive stages select and invade the unique host cell in which they can develop with exquisite specificity and efficacy. Most studies aimed at elucidating the molecules and the mechanisms implicated in the selection and invasion processes have been conducted on the merozoite, the stage that invades erythrocytes to perpetuate the pathological cycles of parasite multiplication in the blood. Bioinformatic analysis has helped identify the members of two parasite protein families, the reticulocyte-binding protein homologues (RBL) and erythrocyte binding like (EBL), in recently sequenced genomes of different Plasmodium species. In this article we review data from classical studies and gene disruption experiments that are helping to illuminate the role of these proteins in the selection-invasion processes. The manner in which subsets of proteins from each of the families act in concert suggests a model to explain the ability of the parasites to use alternate pathways of invasion. Future perspectives and implications are discussed.

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Use of ⁷⁵se‐labeled methionine to study the sequestration of senescent red blood cells

Smedsrød

Aminoff

1985

American J Hematol

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Labeling red blood cells with Na251CrO4 enabled us to study certain aspects of red cell survival and sequestration from the circulation. As a random labeling procedure, however, the 51Cr method has certain limitations. Therefore, we developed a cohort labeling method using 75Se-methionine as a two-rat procedure. This gives us a clear pulse-labeled population of rat red cells to study the dynamics of sequestration. With this labeling procedure, it was possible to demonstrate that 1) there is an increase in the density of red cells with age, 2) a significant sequestration of red cells from the circulation is apparent at the end of 48 days and essentially is complete at the end of 60 days, 3) there is a corresponding uptake of senescent red cells in the spleen, which peaks at 55 days, and 4) the 60-day end point is sharper and is more definitive when the "specific activity" (cpm per red blood cell) of the labeled red cells in the spleen is compared to that of the red cells still in the circulation. Asialo red cells, obtained by removal of sialic acid with sialidase, frequently have been used as a model for the study of sequestration of senescent red cells. With the technique herein described, it was possible to show that while asialo red cells will inhibit the uptake of labeled asialo red cells, they have no effect on the sequestration of senescent red cells. Presumably, different sites and mechanisms of sequestration are involved.

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The Biological Life of the Red Cell

Cited by 49 publications

References 247 publications

SHPS-1 promotes the survival of circulating erythrocytes through inhibition of phagocytosis by splenic macrophages

SHPS-1 promotes the survival of circulating erythrocytes through inhibition of phagocytosis by splenic macrophages

Invasion of host cells by malaria parasites: a tale of two protein families

Use of ⁷⁵se‐labeled methionine to study the sequestration of senescent red blood cells

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The Biological Life of the Red Cell

Cited by 49 publications

References 247 publications

SHPS-1 promotes the survival of circulating erythrocytes through inhibition of phagocytosis by splenic macrophages

SHPS-1 promotes the survival of circulating erythrocytes through inhibition of phagocytosis by splenic macrophages

Invasion of host cells by malaria parasites: a tale of two protein families

Use of 75se‐labeled methionine to study the sequestration of senescent red blood cells

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Product

Resources

About

Use of ⁷⁵se‐labeled methionine to study the sequestration of senescent red blood cells