PubMed · 5163863
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1971-11-26. Vitamin E.. https://pubmed.ncbi.nlm.nih.gov/5163863/
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BACKGROUND: A minority of blood donors are Rh(D)-negative, and Rh(D)-negative red blood cell (RBC) products are often overutilized. As such, Rh(D)-negative RBCs may be difficult to maintain in blood bank inventory. STUDY DESIGN AND METHODS: We changed our blood bank laboratory policy to approve non-alloimmunized Rh(D)-negative patients to receive Rh(D)-positive RBCs for routine transfusion under defined criteria. Those criteria included Rh(D)-negative males (all ages) and females (aged >50 years) who were designated as do not resuscitate (DNR), either with or without intubation, in the electronic medical record. RESULTS: From August 15, 2024 through August 15, 2025, a total of 204 Rh(D)-negative patients met the above criteria and were approved to receive routine Rh(D)-positive RBC transfusions. Within that group, 23 patients received Rh(D)-positive RBCs. The remaining patients either did not require transfusion or were issued Rh(D)-negative RBC units. Since implementing this practice, a total of 68 Rh(D)-negative units were conserved during this time frame. Notably, 28 of the 68 units (41%) were type O, Rh(D)-negative. DISCUSSION: Rh(D)-positive RBCs can be routinely given to non-alloimmunized Rh(D)-negative patients who are not at risk for developing hemolytic disease of the fetus and newborn (HDFN). By creating clear guidelines for the routine administration of Rh(D)-positive RBCs to patients who are not at risk for HDFN, the inventory of Rh(D)-negative RBC units can be directed to those patients who would most benefit from this limited resource.
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Fructosamine 3-kinase, which phosphorylates low-molecular-mass and protein-bound fructosamines on the third carbon of their deoxyfructose moiety, is quite active in erythrocytes, and was proposed to initiate a process removing fructosamine residues from proteins. In the present study, we show that incubation of human erythrocytes with 200 mM glucose not only caused the progressive formation of glycated haemoglobin, but also increased the level of an anionic form of haemoglobin containing alkali-labile phosphate, to approx. 5% of total haemoglobin. 1-Deoxy-1-morpholinofructose (DMF), a substrate and competitive inhibitor of fructosamine 3-kinase, doubled the rate of accumulation of glycated haemoglobin, but markedly decreased the amount of haemoglobin containing alkali-labile phosphate. The latter corresponds therefore to haemoglobin bound to a fructosamine 3-phosphate group (FN3P-Hb). Returning erythrocytes incubated with 200 mM glucose and DMF to a low-glucose medium devoid of DMF caused a decrease in the amount of glycated haemoglobin, a transient increase in FN3P-Hb and a net decrease in the sum (glycated haemoglobin+FN3P-Hb). These effects were prevented by DMF, indicating that fructosamine 3-kinase is involved in the removal of fructosamine residues. The second step of this 'deglycation' process is most likely a spontaneous decomposition of the fructosamine 3-phosphate residues to a free amine, 3-deoxyglucosone and P(i). This is consistent with the findings that 2-oxo-3-deoxygluconate, the product of 3-deoxyglucosone oxidation, is formed in erythrocytes incubated for 2 days with 200 mM glucose in a sufficient amount to account for the removal of fructosamine residues from proteins, and that DMF appears to inhibit the formation of 2-oxo-3-deoxygluconate from elevated glucose concentrations.