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PubMed2003

HbHope/HbS and HbS/beta-thal double compound heterozygosity in a Mauritanian family: clinical and biochemical studies.

The hemoglobin Hope was discovered in a Mauritanian family that comes from Gorgol in the southwest of the country. The family belongs to the Soninké ethnic group, which is one of the black population groups in Mauritania. Along with this abnormal hemoglobin, HbS and beta-thalassemia were also found. This family, which we refer to as D, was encountered during a survey we conducted to study hemoglobinopathies in Mauritania. First the father was identified to carry an association of HbS and HbHope, then the study was extended to the entire family members: the wife who was found to have a beta-thalassemia trait and their three children who were found to carry HbS/beta-thalassemia mutations each. All together this family carries three different mutations that resulted in a double compound heterozygosity HbHope/HbS and HbS/beta-thal.

DNA Mutational Analysis↗
PubMedDate not supplied

[Hemoglobin Stanleyville II and mucoviscidosis in an Alsatian family].

Hemoglobin Stanleyville II, resembling hemoglobin D, has been found several times in individuals from Central Africa. This paper now reports its discovery in Alsace, in an 8 year old girl with cystic fibrosis. The mother and 5 out of 7 siblings had the abnormal hemoglobin. Only 2 of these 5 children had all the symptoms of cystic fibrosis. The family has been living in Alsace for many generations. Cystic fibrosis, a congenital disease, has a high incidence (1/1,800) among white children but is rare in black people.

Adult↗
PubMed1977

Increased oxygen affinity for hemoglobin Sawara: alphaA4(6) aspartic acid replaced by alanine.

The oxygen binding property of Hb Sawara (alphaA4 Asp replaced by Ala) was studied at different pH values with and without addition of 2,3-diphosphoglycerate. The oxygen affinity of Hb Sawara was shown to be increased, the difference of the log P50 value between normal and abnormal hemoglobins being 0.37 at pH 7.0. Both the magnitude of the alkaline Bohr effect and the effect of 2,3-diphosphoglycerate upon oxygen affinity of Hb Sawara were comparable to those of Hb A. The amino acid substitution of alanine for alphaA4 aspartic acid might result in the loss of a stabilizing force for ionic interaction between the alpha-amino group of NA (1)alpha1 valine and the alpha-carboxyl of HC3(141)alpha2 arginine in the deoxy-form.

Alanine↗
PubMed1976

Characterization of hemoglobin Burke [beta 107 (G9) Gly replaced by Arg].

Hb Burke [beta 107 (G9) Gly replaced by Arg] was discovered in a young woman with hemolytic anemia. A substitution in this position has not been previously reported either in the human beta-chain or in any of the animal beta-chains so far sequenced. The abnormal hemoglobin shows heat instability and a lowered oxygen affinity. The substitution of a large charged arginine residue for the small glycine residue in the G helix next to a heme contact (Leu-106) may be responsible for these effects. Hb Burke is compared with five other hemoglobins having Gly-Arg substitutions in other parts of the molecule.

Adult↗
PubMed1984

Identification of beta variant hemoglobins by DNA restriction endonuclease mapping.

An alternative method for identifying beta variant hemoglobins is described. Computer analysis of restriction sites was used to predict which beta variants could be detected by DNA mapping. 61 of 217 variants were shown to have changes in restriction fragment patterns which were useful markers for the abnormal hemoglobin. A further 25 could be identified by polyacrylamide electrophoresis. Implications of DNA analysis in diagnosis of variant hemoglobins are discussed.

Base Sequence↗
PubMed1981

Chart reminders in the diagnosis of anemia.

We hypothesized that chart reminders would decrease the number of cases in which a low admission hemoglobin level was missed or ignored. Additionally, we compared the cost of generating the chart reminders by hand with the estimated cost of modifying the university hospital information system for this function. For three months, two medical students reviewed all abnormal hemoglobin results and assigned those more than 1 g below normal limits to a control or study group. A questionnaire, placed in all study group charts, requested an explanation for the low hemoglobin level. Eleven of 141 study cases and 16 of 150 control cases failed the audit criteria (differences not significant). The cost was $308 compared with $3,000 for altering the hospital information system. We conclude that chart reminders did not improve the detection of anemia and that it cost less to test this intervention by manually simulating the computer function.

Adult↗
PubMed1996

Hemolytic anemias due to hemoglobinopathies.

Hemoglobinopathies responsible for hemolytic anemias may be divided into two groups. The first one corresponds to thalassemias and the second to the presence of a structurally abnormal hemoglobin (Hb). In thalassemia, the primary biochemical abnormality is a quantitative defect in the biosynthesis of one type of Hb chain. This defect leads to an overall deficit of Hb accumulation in the erythrocyte (hypochromia) together with the presence of an excess of the normally synthesized chains. The unpaired subunits which are less soluble than HbA precipitate, bind to the membrane and ultimately lead to hemolysis. In the second group, the hemolytic anemia is a direct consequence of the physicochemical properties of the structurally abnormal Hb. This molecule may polymerize, precipitate or crystallize within the red blood cell (RBC) leading to membrane alterations and to the destruction of the cell. This chapter will emphasize several examples of structurally abnormal Hbs, such as sickle cell disease and congenital Heinz body hemolytic anemia (CHBHA).

Anemia, Hemolytic↗
PubMed2005

A family with hemoglobin Hirosaki.

A 48-year-old man had a 30-year history of hemolytic anemia of undetermined cause. Spherocytes were not observed, osmotic fragility was normal, and red cell enzyme activities were normal. His brother and daughter also had hemolytic anemia. The brother had previously undergone splenectomy, and the anemia had been ameliorated. In the proband and daughter, no abnormal hemoglobin was apparent in the results of isoelectric focusing and DEAE anion-exchange high-performance liquid chromatography analyses. On evaluation with the isopropanol test, unstable hemoglobin was not observed in the proband but was detected in the daughter. There was also a decreased ratio of 3 globin/3 globin chain production. Analysis of the 32 gene demonstrated the presence of a mutation (alpha43 [CE1] Phe --> Leu), hemoglobin Hirosaki.

Amino Acid Substitution↗
PubMed1979

Hemoglobin Dunn: alpha 6 (A4) aspartic acid replaced by asparagine.

Hemoglobin Dunn, alpha 6 (A4) Asp leads to Asn was found in a 39-year-old black woman and her daughter. The hematological data on the propositus were normal and there were no apparent clinical or pathological findings associated with this abnormal hemoglobin. The structural characterization of this variant is described.

Adult↗
PubMed1997

Hb Auckland [alpha 87(F8) His-->Asn]: a new mutation of the proximal histidine identified by electrospray mass spectrometry.

Hb Auckland is a newly described unstable hemoglobin with a mutation of alpha 97(F8)His-->Asn. This substitution, involving the proximal histidine, does not lead to methemoglobinemia, but to instability and accelerated heme loss. The clinical picture is of a mild compensated hemolytic anemia. The presence of an abnormal hemoglobin was first demonstrated by the isopropanol stability test and confirmed by electrospray ionization mass spectrometry of total lysate. This showed that 14% of the alpha chains had a mass of 15,103.4 Da, i.e. 23 Da less than normal. Examination of tryptic digests showed an identical decrease in mass for peptide alpha T-9 (from 2,997.4 to 2,974.5 Da). Subdigestion with endoproteinase Asp-N located the 23 Da loss to residues alpha 85-90, and further digestion with thermolysin identified the mutation as His-->Asn at position 87 of the alpha chain. This was confirmed by sequence analysis of the peptide alpha 85-90.

Adult↗
PubMed1980

[Hemoglobin N Baltimore: 28 cases in one Guadeloupe family (author's transl)].

The detection of hemoglobin AN Baltimore in a young man, 28 years old in June 1978, led us make a family study. This family study was very interesting because our proband had 16 brothers and sisters, many of whom also had many children. Research on abnormal hemoglobins was done on 46 family members: 28 were carriers of hemoglobin AN Baltimore and three children, carriers of heterozygote SN Baltimore.

Adolescent↗
PubMed2005

Modeling for tertiary structure of globin chain in Hemoglobin Suan-Dok disorder.

Hemoglobinopathies are an important inherited disorder with a high prevalence in Southeast Asia. Hemoglobin Suan-Dok is an example of a hemoglobinopathy that was first identified and described in Thailand. It has been identified as an unstable hemoglobin variant associated with alpha-thalassemia. The role of the hemoglobin instability in Hb Suan-Dok in the altered red cell morphology in comparison to the thalassemia-like deficit of alpha globin mRNA has not been entirely resolved and needs additional structural study for clarification. In this study the amino acid sequence of human alpha globin was extracted using ExPASY and compared with that obtained from the Hb Suan-Dok disorder. The derived sequences, alpha globin chains in both the normal and Hb Suan-Dok disorder, were used for further investigation of the tertiary structures. Modeling these proteins for the tertiary structure was performed using the CPHmodels 2.0 Server. For comparison the tertiary structure of human alpha globin chains in normal and hemoglobin Suan-Dok are calculated and presented. Based on this information, there was no significant difference between the predicted alpha globin tertiary structures of normal hemoglobin and Hb Suan-Dok. Therefore, from this study we can state that the tertiary structure of alpha globin is not significantly affected by the mutation in the Hb Suan-Dok disorder and that the effect of this hemoglobin abnormality may be silent. The data suggests that the thalassemic defect associated with the Suan-Dok mutation results from another unidentified process rather than the structural aberration and that the finding of a thalassemic picture might be due to another undetectable inherited hemoglobin disorder.

Hemoglobins, Abnormal↗
PubMed1973

Hemoglobin Okaloosa (beta 48 (CD7) leucine leads to arginine). An unstable variant with low oxygen affinity.

A slow-moving hemoglobin with electrophoretic mobility similar to that of hemoglobin S was discovered in a white laboratory technologist. She had an elevated reticulocyte count, as did several members of her family. Her red cell survival was shortened. Amino acid analysis indicated that leucine at position beta48 (CD7) had been replaced by arginine. The abnormal hemoglobin, called Okaloosa, was heat-precipitable and had decreased oxygen affinity. It exhibited a greater change in oxygen affinity than hemoglobin A when 2,3 DPG was added to "stripped" hemolysates. These findings cannot be readily explained by current views of structure-function relationships in the hemoglobin molecule. However, it is of interest that the amino acid in position CD7 is normally leucine in the alpha, beta, delta, and gamma-hemoglobin chains and in the myoglobin chain of man and a wide variety of other vertebrates.

Amino Acids↗
PubMed1987

Structure and function of a new hemoglobin variant, Hb meilahti (alpha 2 beta 2 36(C2)Pro----Thr), characterized by mass spectrometry.

An abnormal hemoglobin was found by isoelectric focusing in the blood of a Finnish woman with erythrocytosis. Oxygen equilibrium curves of the patient's hemolysate indicated the presence of a variant with a very high oxygen affinity. Structural analysis was carried out by mass spectrometry. In the spectrum of the tryptic digest, an abnormal peptide was found at m/z1278 which corresponded to the mass number of the protonated molecular ion of beta T4 with 36Pro----Thr substitution. The structure was confirmed by the mass spectrum of the chymotryptic digest.

Genetic Variation↗
PubMed1998

[Diagnosis of hemoglobinopathies].

The chemical identification of variant hemoglobins was largely overtaken by DNA analysis during the last decade, despite remarkable improvement and automation of individual procedures in conventional chemistry. DNA diagnosis has proved more versatile, covering both variant hemoglobin and thalassemia mutations, less labor-demanding, and easier to learn. Protein chemistry is now reserved for some special problems such as post-translational modification (this problem would be covered much better by mass spectrometry), biosynthesis and stability, and pathologic physiology of selected abnormal hemoglobins. After introduction of DNA analysis during mid 1980's, the number of blood samples referred to our laboratory rapidly increased, mainly because of thalassemia traits in the differential diagnosis of microcytic anemia. Our experience during the past forty years and the present strategy for the rapid presumptive diagnosis of hemoglobinopathies and precise identification of mutations are briefly summarized.

DNA↗
PubMed1983

Hemoglobin Okayama [beta 2 (NA 2) His replaced by Gln]: a new 'silent' hemoglobin variant with substituted amino acid residue at the 2,3-diphosphoglycerate binding site.

A new 'silent' abnormal hemoglobin, Hb Okayama [beta 2 (NA 2) His replaced by Gln], happened to be discovered in a diabetic Japanese female living in Okayama Prefecture, Japan, in the course of glyco-Hb measurement of the blood samples of diabetic patients. This variant did not differ from Hb A by conventional electrophoretic tests. Only the isoelectric focusing on PAG plate for the determination of glyco-Hb and the cation exchanger chromatography were successful in the separation of this abnormal variant from Hb A and glyco-Hb. Functional study of the whole blood demonstrated a slight increase of oxygen affinity.

2,3-Diphosphoglycerate↗
PubMed1994

Hb Washtenaw [ beta 11(A8)Val-->Phe]: an electrophorectically silent, unstable, low oxygen affinity variant associated with anemia and chronic cyanosis.

Hb Washtenaw [beta 11(A8)Val-->Phe] is a new, low oxygen affinity variant with a previously undescribed substitution, identified in seven members over three generations of a Hungarian-American family. The hemoglobin is mildly unstable and the family members studied are clinically asymptomatic but mildly cyanotic, and some exhibit mild anemia. The index case had severe pulmonary hypertension and some of the family members had increased pulmonary vascular resistance on echocardiography. An association between the inheritance of this abnormal hemoglobin and the pathogenesis of primary pulmonary hypertension is suggested but the mechanism is unclear.

Adolescent↗