Hematological aspect of Rh deficiency syndrome: A case report and a review of the literature

Nash, Richard A.; Shojania, A. Majid

doi:10.1002/ajh.2830240306

Cited by 58 publications

(27 citation statements)

References 37 publications

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“…Its deletion decreases erythrocyte plasma membrane ammonia transport (27,55). Rhag deletion also results in chronic hemolytic anemia characterized by stomatocytosis, reduced osmotic fragility, and abnormal autohemolysis (51). Mutations in conserved amino acids in the pore region of RhAG have recently been associated with development of overhydrated hereditary stomatocytosis, a rare autosomal dominant hemolytic anemia characterized by a profuse monovalent cation membrane leak (7).…”

Section: Discussionmentioning

confidence: 99%

Collecting duct-specific Rh C glycoprotein deletion alters basal and acidosis-stimulated renal ammonia excretion

Lee¹,

Verlander²,

Bishop³

et al. 2009

American Journal of Physiology-Renal Physiology

137

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NH3 movement across plasma membranes has traditionally been ascribed to passive, lipid-phase diffusion. However, ammonia-specific transporters, Mep/Amt proteins, are present in primitive organisms and mammals express orthologs of Mep/Amt proteins, the Rh glycoproteins. These findings suggest that the mechanisms of NH3 movement in mammalian tissues should be reexamined. Rh C glycoprotein (Rhcg) is expressed in the collecting duct, where NH3 secretion is necessary for both basal and acidosis-stimulated ammonia transport. To determine whether the collecting duct secretes NH3 via Rhcg or via lipid-phase diffusion, we generated mice with collecting duct-specific Rhcg deletion (CD-KO). CD-KO mice had loxP sites flanking exons 5 and 9 of the Rhcg gene (Rhcg(fl/fl)) and expressed Cre-recombinase under control of the Ksp-cadherin promoter (Ksp-Cre). Control (C) mice were Rhcg(fl/fl) but Ksp-Cre negative. We confirmed kidney-specific genomic recombination using PCR analysis and collecting duct-specific Rhcg deletion using immunohistochemistry. Under basal conditions, urinary ammonia excretion was less in KO vs. C mice; urine pH was unchanged. After acid-loading for 7 days, CD-KO mice developed more severe metabolic acidosis than did C mice. Urinary ammonia excretion did not increase significantly on the first day of acidosis in CD-KO mice, despite an intact ability to increase urine acidification, whereas it increased significantly in C mice. On subsequent days, urinary ammonia excretion slowly increased in CD-KO mice, but was always significantly less than in C mice. We conclude that collecting duct Rhcg expression contributes to both basal and acidosis-stimulated renal ammonia excretion, indicating that collecting duct ammonia secretion is, at least in part, mediated by Rhcg and not solely by lipid diffusion.

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Section: Discussionmentioning

confidence: 99%

Collecting duct-specific Rh C glycoprotein deletion alters basal and acidosis-stimulated renal ammonia excretion

Lee¹,

Verlander²,

Bishop³

et al. 2009

American Journal of Physiology-Renal Physiology

137

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“…[1][2][3]. Moreover, although the physiological role of these antigens is still unclear, they are probably important structures for erythrocyte membrane integrity, as evidenced by the mild hemolytic anemia (4,5), abnormalities in cation permeability (6,7), and membrane lipid asymmetry (8) (1,2,9), but whether these antigens are the products of one gene or several closely linked genes has not been clarified (review in ref. 1).…”

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confidence: 99%

Molecular cloning and protein structure of a human blood group Rh polypeptide.

Chérif-Zahar

Bloy

Kim

et al. 1990

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

285

167

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cDNA clones encoding a human blood group Rh polypeptide were isolated from a human bone marrow cDNA library by using a polymerase chain reaction-amplified DNA fragment encoding the known common N-terminal region of the Rh proteins. The entire primary structure of the Rh polypeptide has been deduced from the nucleotide sequence of a 1384-base-pair-long cDNA clone. Translation of the open reading frame indicates that the Rh protein is composed of 417 amino acids, including the initiator methionine, which is removed in the mature protein, lacks a cleavable N-terminal sequence, and has no consensus site for potential Nglycosylation. The predicted molecular mass of the protein is 45,500, while that estimated for the Rh protein analyzed in NaDodSO4/polyacrylamide gels is in the range of 30,000-32,000. These findings suggest either that the hydrophobic Rh protein behaves abnormally on NaDodSO4 gels or that the Rh mRNA may encode a precursor protein, which is further matured by a proteolytic cleavage of the C-terminal region of the polypeptide. Hydropathy analysis and secondary structure predictions suggest the presence of 13 membrane-spanning domains, indicating that the Rh polypeptide is highly hydrophobic and deeply buried within the phospholipid bilayer. In RNA blot-hybridization (Northern) analysis, the Rh cDNA probe detects a major 1.7-kilobase and a minor 3.5-kilobase mRNA species in adult erythroblasts, fetal liver, and erythroid (K562, HEL) and megakaryocytic (MEG01) leukemic cell lines, but not in adult liver and kidney tissues or lymphoid (Jurkat) and promyelocytic (HL60) cell lines. These results suggest that the expression of the Rh gene(s) might be restricted to tissues or cell lines expressing erythroid characters.

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“…Although the remarkable polymorphism of the RhD and RhCcEe proteins [216] limits their utility as target antigens for drug delivery, some Rh family member epitopes, such as Rh17 (also known as Hr 0 ) and Rh29 [217], are present on nearly all human RBCs with the notable exception of the rare Rh-null phenotype that occurs in approximately 1 in 6 million individuals [218]. High-frequency epitopes have also been identified in the RhAG protein, for example, the Duclos antigen [219].…”

Section: Choosing Target Binding Sites On Carrier Rbcsmentioning

confidence: 99%

Delivery of Drugs Bound to erythrocytes: New Avenues for an Old Intravascular Carrier

et al. 2015

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For several decades, researchers have used erythrocytes for drug delivery of a wide variety of therapeutics in order to improve their pharmacokinetics, biodistribution, controlled release and pharmacodynamics. Approaches include encapsulation of drugs within erythrocytes, as well as coupling of drugs onto the red cell surface. This review focuses on the latter approach, and examines the delivery of red blood cell (RBC)-surface-bound anti-inflammatory, anti-thrombotic and anti-microbial agents, as well as RBC carriage of nanoparticles. Herein, we discuss the progress that has been made in surface loading approaches, and address in depth the issues relevant to surface loading of RBC, including intrinsic features of erythrocyte membranes, immune considerations, potential surface targets and techniques for the production of affinity ligands.

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Hematological aspect of Rh deficiency syndrome: A case report and a review of the literature

Cited by 58 publications

References 37 publications

Collecting duct-specific Rh C glycoprotein deletion alters basal and acidosis-stimulated renal ammonia excretion

Collecting duct-specific Rh C glycoprotein deletion alters basal and acidosis-stimulated renal ammonia excretion

Molecular cloning and protein structure of a human blood group Rh polypeptide.

Delivery of Drugs Bound to erythrocytes: New Avenues for an Old Intravascular Carrier

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