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Hb Oegstgeest [alpha104(G11)Cys-->Ser (alpha1)]. A new hemoglobin variant associated with a mild alpha-thalassemia phenotype.

A microcytic hypochromic anemic state was observed in an 8-year old Black female of Surinam origin during pre-operative Hb S [beta6(A3)Glu-->Val] screening. Her high zinc protoporphyrin (ZPP) level suggested a chronic iron depletion but, in contrast, the high red blood cell (RBC) count (5.85 x 10(12)/L) was indicative of a possible coexisting thalassemia. No abnormal hemoglobin (Hb) bands were present on high performance liquid chromatography (HPLC) or alkaline electrophoresis and the Hb A2 level was normal. Break point polymerase chain reaction (PCR) failed to reveal any of the common alpha-thalassemia (thal) mutations but selective DNA sequencing of both alpha-globin genes disclosed a TGC-->AGC transversion at codon 104 of the alpha1 gene. Cystine at codon 104 is involved in alpha/beta globin contact and has been described to be a critical amino acid of the alpha2 chain when substituted by a tyrosine (Hb Sallanches), inducing Hb H (beta4) disease in the homozygous state. Our heterozygous patient had a moderate anemia of 12.2 g/dL and a borderline haptoglobin suggesting some degree of hemolysis.

Amino Acid Substitution↗

An automatic method for determination of glycosylated hemoglobins using low-pressure liquid chromatography.

Several studies have revealed a correlation between blood levels of glucose and hemoglobin A1c (HbA1c), a minor form of hemoglobin (Hb) present at elevated concentrations in patients with diabetes mellitus. To facilitate a clinical study of the level of circulating HbA1c we have developed an automatic chromatographic system. An efficient separation of HbA1c from HbA0 and other rapid hemoglobins (HbA1a, HbA1b) was achieved on Bio-Rex-70 columns using three buffers. This system allows the daily analysis of 40 samples. The mean level of HbA1c in normal subjects was 5.4 +/- 0.4%. The method also detects the presence of elevated levels of HbF and the most frequent forms of abnormal hemoglobin (HbS, HbC).

Adult↗

Mechanism of autoxidation of hemoglobin Kempsey (beta 99 Asp----Asn).

The mechanism of autoxidation of oxyhemoglobin Kempsey (beta 99 asp----asn) was studied at pH 7.0, 37 degrees C, using isoelectric focusing electrophoresis. During autoxidation, two intermediate hemoglobins, (alpha 2+ beta 3+)2 and (alpha 3+ beta 2+)2 were observed, and these were consecutively changed to methemoglobin. The autoxidation rates of oxyhemoglobin Kempsey were reduced about 43% by the addition of catalase and superoxide dismutase, but were not significantly changed by the addition of inositol hexaphosphate. This abnormal hemoglobin autoxidized more slowly than normal hemoglobin A. The differences in the autoxidation rates between these hemoglobins were explained by the changes in quaternary structure of these proteins. The reaction rate constant, k+1, k+2, k+3 and k+4 of each step including the reactions: (formula; see text) were determined by the analysis of fractional changes in these hemoglobin derivatives during the autoxidation. The difference in the reaction rate constants between k+1 and k+3 was explained by the nonequivalence of alpha and beta chains in tetrameric oxyhemoglobin Kempsey. The reaction mechanism of autoxidation of hemoglobin Kempsey was discussed on the basis of these kinetic results.

Asparagine↗

Hemoglobin saitama or beta 117 (G19) His leads to Pro, a new variant causing hemolytic disease.

An electrophoretically silent unstable hemoglobin was found in a 23-year-old Japanese woman suffering from hemolytic anemia and jaundice. The unstable beta subunit was precipitated with p-chloromercuribenzoic acid and the globin was further purified by urea CM-52 column chromatography. Results of amino acid analysis, tryptic fingerprinting and manual Edman degradation of the abnormal beta T12B established a substitution of proline for histidine beta 117 (G19). This new abnormal hemoglobin was absent in other members of the family.

Adult↗

Hemoglobin Queens: alpha 34 (B15) Leu-Arg structural and functional properties and its association with Hb E.

Hemoglobin Queens: alpha 34 (B15) Leu-Arg was found in association with Hb E in a Vietnamese boy. The observed microcytosis and hypochromia were due to Hb E, which also occurred in other members of this family. The functional properties of Hb Queens in the absence and presence of allosteric effectors were normal. The abnormal hemoglobins appear to be unrelated to the hyperbilirubinemia that was observed at birth.

Amino Acids↗

Contributions of asparagine at alpha 97 to the cooperative oxygenation process of hemoglobin.

According to the X-ray crystallographic results from human deoxyhemoglobin, beta 99Asp at the alpha 1 Beta 2 interface forms hydrogen bonds with alpha 42Tyr and alpha 97Asn. To clarify the structural and functional roles of the hydrogen bond between alpha 97Asn and beta 99Asp, we have engineered a recombinant hemoglobin in which alpha 97Asn is replaced by Ala, and have investigated its oxygen-binding properties, and have used proton nuclear magnetic resonance spectroscopy to determine the structural consequences of the mutation. Recombinant Hb (alpha 97Asn-->Ala) shows a milder alteration of functional properties compared to the severely impaired beta 99 mutants of the human abnormal hemoglobins. The addition of inositol hexaphosphate, an allosteric effector, causes recovery of the functional properties of recombinant Hb (alpha 97 Asn-->Ala) almost to the level of human normal adult hemoglobin without this allosteric effector. r Hb (alpha 97 Asn-->Ala) shows very similar tertiary structure around the heme pockets and quaternary structure in the alpha 1 beta 2 interface compared to those of human normal adult hemoglobin. The proton nuclear magnetic resonance spectrum of the deoxy form of this recombinant hemoglobin shows the existence of an altered hydrogen bond which is believed to be between alpha 42Tyr and beta 99Asp at the alpha 1 beta 2 interface. Thus, the present results suggest that the intersubunit hydrogen bond between alpha 97 Asn and beta 99Asp at the alpha 1 beta 2 interface is not as crucial as the one between alpha 42Tyr and beta 99Asp in the deoxy quaternary structure. Preliminary molecular dynamics simulations have been used to calculate the contributions of specific interactions of several amino acid residues in r Hb (alpha 97Asn-->Ala) to the free energy of cooperativity of this recombinant hemoglobin. The results of these calculations are consistent with the experimental results.

Adult↗

Electrophoretic HbA2 assessment in ischemic heart disease.

A series of fifty patients presenting ischemic heart disease are studied. As shown by the electropherogram, apart from the basic band of hemoglobin A2, an additional weaker band appears with a diffuse zone between them. The quantity of the entire HbA2-diffuse zone exceeds by 3.8 per cent the total hemoglobin. Its appearance is not attributed to abnormal hemoglobin or beta-thalassemia. With the passing of time its quantity shows a decrease, and within 3-6 days it disappears. Parallel to normalization of the hemoglobin profile the pain syndrome among patients with unstable stenocardia subsides, and stabilization of the patients with a history of myocardial infarction takes place.

Adult↗

Antimalarial red cells.

It is difficult to overestimate the evolutionary pressures exerted over the past few thousand years by endemic malaria. For most of hominid evolution, these parasites probably caused little morbidity and mortality. However, as Livingstone (1964, 1967, 1971) has pointed out, the advent of slash and burn horticulture and associated sedentary living patterns dramatically changed this situation. For many human populations, endemic malaria became an evolutionary emergency. In such pressing circumstances, genetic traits which ordinarily would carry with them an intolerable genetic load actually increase in frequency. Thus, although a few antimalarial red cell characteristics such as Duffy negativity are evidently innocuous, the majority of malaria-selected traits are not. Ovalocytosis, the abnormal hemoglobins and G-6-PD deficiencies are all quite deleterious in the homo- or hemizygote. This, more than anything else, bespeaks the extraordinary evolutionary pressures exerted by malaria. Needless to say, the mechanisms by which these various red cell traits protect are incompletely known. Although our discussion of such mechanisms has revolved about parasite/host cell relationships, the actual antimalarial effect may involve more distal interactions, especially of infected erythrocytes with the immune and reticuloendothelial systems. Protection exerted by modifications of such interactions would not be revealed by in vitro culture experiments upon which we rely for much of our information. For example, as normal red cells age and senesce, they express novel surface antigens which are recognized by specific immunoglobulins (Kay, 1983). Cells which have bound such antibodies are likely recognized and destroyed rapidly by the reticuloendothelial system. The expression of such senescence antigens may be hastened in already abnormal cells subject to the additional burden of an internal parasite. Therefore, it is quite possible that congenital defects of the red cell membrane, hemoglobin and metabolism may afford protection against malaria via immunologic mechanisms rather than by blocking penetration or predisposing the cell to spontaneous intravascular lysis. To be successful in the mammalian host, erythrocytic phase of malaria must recognize and attach to the host red cell, successfully penetrate, and replicate within. Remarkably, there are antimalarial red cells which impair each one of these individual steps. In this case, the ingenuity of natural selection has been almost--but not quite--a match for that of the malaria parasite.

Adenosine Triphosphate↗

Hereditary persistence of fetal hemoglobin, beta thalassemia, and the hemoglobin delta-beta locus: further family data and genetic interpretations.

Three Negro kindreds with hereditary persistence of fetal hemoglobin (HPFH) alone and in combination with various other hemoglobin abnormalities including beta thalassemia are presented. Among 11 offspring of two women heterozygous for both HPFH and the delta chain mutation Hb B2, five inherited the HPFH gene and six inherited the Hb B2 gene. In another kindred, a man inferred to be heterozygous for both HPFH and Hb C had six children; three offsprivg obtained the Hb C gene and three the HPFH gene. Similarly, a woman heterozygous for both Hb S and HPFH transmitted the Hb S gene to one of her two children and the HPFH gene to the other. Thus among 19 offspring, no crossovers between the HPFH locus or the Hb delta-beta locus were observed. These and earlier data are compatible with deletion of the Hb beta and delta loci as the primary event to explain the genetic origin of HPFH. Genetic considerations indicate that the finding of a single person with a hematologically normal phenotype among offspring of heterozygotes for both the African type of HPFH and a Hb beta or Hb delta structural abnormality would invalidate the deletion model.

Adolescent↗

Hemoglobin Beograd (alpha2beta2 121 Glu leads to Val) interacting with beta-thalassemia.

Hematological and biochemical findings in a family with hemoglobin (Hb) Beograd interacting with beta-thalassemia are presented. Hb Beograd (alpha2beta2 121 Gul leads to Val) was found in 3 members. In two members it interacted with beta-thalassemia. These two double heterozygotes had anemia of intermediate severity and splenomegaly. Studies with 51Cr and 59Fe showed a shortened life span of red cells and ineffective erythropoiesis. The abnormal Hb amounted to 86-87%, and Hb F to 5-7%. No Hb A was present. One subject of the family was heterozygous for Hb Beograd. He showed normal clinical and hematological findings. The abnormal hemoglobin was 38%. Four members of the family were heterozygotes for beta-thalassemia. The interaction between beta-thalassemia and beta-chain variants is discussed.

Adult↗

Homozygous cases for hemoglobin J Mexico (alpha54 (E3)Gln replaced by Glu) evidence for a duplicated alpha gene with unequal expression.

Hemoglobin J Mexico has been found in five generations of a large Algerian family. Nine subjects have 55% Hb J although their parents, siblings and offspring may have 31%, the usual quantity found in heterozygotes. Those with 55% Hb J are considered to be homozygous for a chromosome carrying both a normal alpha chain locus and a locus for alphaJ. The proportion of the abnormal hemoglobin in all the subjects is in favor of an unequal expression of both loci, the amount of protein synthesis directed by the alpha J gene being greater than that directed by the alpha A. In two heterozygotes a slightly higher proportion of the Hb J (38%) suggests the presence of a single normal alpha chain locus in trans. An associated alpha-thalassemia was excluded by biosynthetic studies in this family.

Genes↗

Hb Godavari [alpha 95(G2)Pro-->Thr]: a neutral amino acid substitution in the alpha 1 beta 2 interface that modifies the electrophoretic mobility of hemoglobin.

Hb Godavari [alpha 95(G2)Pro-->Thr] was characterized independently in two families of different ethnic origin. The first case, found in the Netherlands, involved an Indian patient. The second one was identified a few months later in an African family from Mali, living in France. Hb Godavari is the fourth example of a substitution involving neutral residues at position alpha 95(G2). In all these variants the electrophoretic pattern suggested that the structural modification unmasks a charged residue buried in the alpha 1 beta 2 contact area. The oxygen affinity of this abnormal hemoglobin was approximately 10% higher than that of Hb A; in the absence of 2,3-diphosphoglycerate, its cooperativity was moderately decreased, suggesting a slightly unstable T state.

Adult↗

Hemoglobin Hasharon (alpha-2-47 his(CD5)beta-2): a hemoglobin found in low concentration.

Hemoglobin Hasharon (alpha(2) (47 his)(CD5)beta(2)) was found to comprise only 16-19% of hemolysates of carriers. These heterozygotes appeared to have mild, compensated, hemolytic anemia. Hb Hasharon was more heat-labile than hemoglobins A, S, or C. Its specific activity was higher than that of Hb A after administration of (59)Fe to two carriers. When hemoglobin synthesis by bone marrow cells was studied in vitro, about 18% of incorporated leucine appeared in the Hb Hasharon fraction. It is suggested that Hb Hasharon is unstable in vivo, and that mild hemolytic anemia and a relatively small decrease in its concentration in hemolysates result from its denaturation within red cells. Decreased synthesis, which appears to be the major cause of the small amount of abnormal hemoglobin, may protect heterozygotes from clinically significant hemolytic anemia.

Aged↗

Identification of Hb Lepore-Washington-Boston in association with Hb E [beta 26(B8)Glu----Lys] in a Thai female.

The proposita was a Thai female showing signs of a mild anemia (Hb: 11.4 g/dl; RBC: 4.91 X 10(6)/mm3; reticulocytes: 2.4%; MCV: 70 fl; MCHC: 23.3 g/dl). Hemoglobins were isolated by DEAE-cellulose chromatography in the following relative amounts: Hb E + Hb A2 = 53%; Hb F0 = 30.0%; Hb delta beta-Lepore = 12.7%; Hb F1 = 4.3%. The beta E and delta beta-Lepore chains were isolated by CM-cellulose chromatography and were subjected to tryptic peptide mapping on paper in comparison to normal beta A chains. Amino acid analysis of selected peptides permitted unambiguous identification of the abnormal hemoglobins as Hb E [beta 26(B8)Glu----Lys] and Hb Lepore-Washington-Boston, which has a delta chain sequence for residues 1-87, and a beta chain sequence for residues 116-146. The presence of a Lepore hemoglobin was further confirmed by Pst I digestion of the proposita's DNA. The association of the two hemoglobin variants gave rise to elevated levels of Hb F.

Adult↗

[Rare variants of Hb D Punjab, Hb O Arab and polymorphism of human hemoglobins].

This report describes the occurrence, study and molecular diagnostics of 40 Hb O Arab beta 121 Glu Lys cases and 4 Hb D punjab beta 121 Glu Gln cases in Bulgaria. Hematological, morphological and clinical data for 12 patients with Hb O arab are listed. Among them we observed 7 simple heterozygotes for Hb O Arab/Hb A, two double heterozygotes-compounds for Hb O/beta+-thalassemia and three compounds for Hb O/beta 0-thalassemia (the latter assumed). Also, general hematological, morphological and clinical data are presented for 4 Hb D Punjab carriers, from which two are simple heterozygotes and two are assumed, as compounds for Hb D/beta 0-thalassemia. The consideration of heterozygosity, homozygosity for both abnormal hemoglobins and of the compound state of Hb O or Hb D/beta-thalassemia or HbS types let us suggest the relative neutrality of the variants and the limitation in their distribution, depending on genetic structure of populations, where they spread. It may be concluded that human hemoglobin is characterized by marked monomorphism. At the same time, the high frequency of HbS, HbE and HbC in some populations can be well explained by contemporary selectionism; the distribution of relatively neutral Hb D Punjab and Hb O Arab with some limitations can follow Kimura's neutralism concept.

Amino Acids↗

Hb Amsterdam [alpha32(B13)Met--Ile (alpha2)]: a new unstable variant associated with an alpha-thalassemia phenotype and a new African polymorphism.

We have characterized a new abnormal hemoglobin (Hb) at position 32 of the alpha-globin chain. The proband, a 38-year-old woman of Surinamese Black ancestry, was referred to the Academic Hospital in Amsterdam, The Netherlands, after 3 years of Prednisone treatment in Surinam. Kidney failure was diagnosed at the Nephrology Department, Free University Medical Center, Amsterdam, The Netherlands; the cortisone treatment was interrupted and dialysis was started. At this stage, a microcytic hypochromic anemia was observed with high reticulocyte (40%) and ferritin (500 microg/L) levels, and hemoglobinopathy was suspected. No abnormal bands were visible on alkaline electrophoresis and high performance liquid chromatography (HPLC). The Hb A2 level was normal (2.7%) and the erythrocyte count was low (3.59 x 10(12)/L) with a normal haptoglobin level (68 mg/100 mL). None of the common alpha-thalassemia (thal) deletion defects were present. The beta-globin gene sequence was normal but the alpha2-globin gene sequence revealed an ATG-->ATA transition at codon 32, changing the methionine into an isoleucine residue. The mutation, called Hb Amsterdam, was observed in the mother of the proband, who was also heterozygous for the--alpha3.7-thal deletion and affected by a moderate microcytic hypochromic anemia. Both Hb Amsterdam and the--alpha(-3.7) allele were found in association with a new polymorphism, IVS-I-39 (C-->T), previously observed in our laboratory in seven patients of African origin, on both the alpha1 and alpha2 genes. In addition, Hb Amsterdam was also associated with the common African alpha2 polymorphism (G-->CTCGGCCC at position 7238 and T-->G at position 7174). Hb Amsterdam is the first mutation ever described at codon alpha32, a position involved in alpha1/beta1 interaction. The possibility of a contribution of this mutation to the nephropatic state of the proband is discussed.

Adult↗