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At least 451 records · Page 25Linked to original sources
PubMed1997

Immunoblot detection of decreased antibodies to haptoglobin-like protein in the serum of infertile women with or without endometriosis.

The purpose of this study was to find out differences in the levels of antibodies to distinct antigens in the serum of fertile versus infertile patients with and without endometriosis and to identify these antigens. Blood was collected from 61 patients undergoing laparoscopy for pelvic pain, infertility, or tubal ligation. Serum antibodies against serum antigens with apparent molecular masses of 22 kDa and 18 kDa were assessed by immunoblot analysis. Gel filtration, HPLC DEAE ion-exchange chromatography, NH2-terminal sequencing, and double immunodiffusion were used to characterize and identify these proteins. The relative amount of antibodies reacting with 22- and 18-kDa proteins detected in a standard preparation of antigens was significantly lower in the serum of infertile patients with endometriosis (0.20 +/- 0.05 and 0.57 +/- 0.10) and without endometriosis (0.21 +/- 0.06 and 0.53 +/- 0.08) compared to that of control fertile women without endometriosis (0.53 +/- 0.08 and 1.09 +/- 0.13). After purification by chromatography, the NH2-terminal amino acid sequence of the proteins in the 22- and 18-kDa range was identical through 20 amino acids with the alpha chain of the human haptoglobin. Double immunodiffusion implied immunochemical identity between commercial human haptoglobin and the purified proteins. We conclude that infertile patients with and without endometriosis show reduced serum levels of antibodies against a haptoglobin-like protein. These results would indicate an alteration of the immune system or changes in the levels of these antigens in infertility and/or endometriosis.

Adult↗
PubMed1976

Binding of human hemoglobin and its polypeptide chains with haptoglobin coupled to an agarose matrix.

The interactions of human haptoglobin covalently linked to agarose with human hemoglobin and with p-chloromercuribenzoic-acid-treated alpha and beta chains (alpha* and beta* chains) were studied by flow chromatography and equilibrium binding. The results indicate that in solid state, haptoglobin maintains the same binding characteristics as in solution, the order of binding affinities being: hemoglobin greater than alpha* chain greater than beta* chain. The study of the binding parameters of the alpha* chain shows an heterogeneity of binding sites on the haptoglobin and an average affinity constant Ka of 3.6 X 10(4)l/mol.

Binding Sites↗
PubMed1982

Haptoglobin: a natural bacteriostat.

The combination of bacteria and blood in a wound can have lethal consequences, probably because hemoglobin iron supports prolific bacterial growth. Rats inoculated intraperitoneally with pathogenic Escherichia coli and small amounts of hemoglobin die. Simultaneous administration of haptoglobin, a naturally occurring hemoglobin-binding protein, fully protects against lethality. Therefore, haptoglobin may not only accelerate the clearance of free hemoglobin, but also limit its utilization by adventitious bacteria. Haptoglobin may have therapeutic potential in the treatment of life-threatening, hemoglobin-driven bacterial infections.

Escherichia coli↗
PubMed1961

Serum haptoglobin in liver disease.

Serum haptoglobin levels have been measured in 115 cases of widely differing liver disease. Although low levels were found in some cases of cirrhosis and a number of patients with obstructive jaundice had increased levels, 70% of the values fell within the normal range. The estimation was of no help in distinguishing between intra- and extrahepatic obstructive jaundice. A characteristic pattern was observed in infective hepatitis, and a falling serum haptoglobin in the presence of increasing jaundice is diagnostic of the latter condition. The cause of these changes is uncertain. Low levels could not be accounted for by increased red cell breakdown and there was no correlation with the serum albumin level. Prednisolone therapy produced a rise in serum haptoglobin level in cirrhosis, which was accompanied by an improvement in liver function. Temporary rises in level were observed in intrahepatic obstructive jaundice and were probably due to a non-specific effect of prednisolone. In the latter condition norethandrolone therapy was often associated with high levels.

Female↗
PubMed1960

A simple method for the determination of serum haptoglobins.

Changes in the serum haptoglobin level have been reported in certain forms of anaemia (Allison and ap Rees, 1957; Allison, 1958; Nosslin and Nyman, 1958; Nyman, Gydell, and Nosslin, 1959), in hepatobiliary disease (Owen, Mackay, and Got, 1959) and in various inflammatory and chronic diseases (Jayle and Boussier, 1955; Allison and Blumberg, 1958). A simple colorimetric procedure for the determination of serum haptoglobins is presented. It is based on the peroxidase activity of haptoglobin-methaemoglobin complexes.

Haptoglobins↗
PubMed1966

Low plasma haptoglobin in march haemoglobinuria.

A student had haemoglobin in the urine after running but not after cycling. The haemoglobinuria was related to the hardness of the surface on which he ran and to his running style. The concentration of haptoglobin in his plasma was less than normal. This was most pronounced after he had been running, when haptoglobin had combined with free haemoglobin, but the concentration was also low when there had been no haemolysis for six weeks. Thus two factors combined to give him haemoglobinuria: lysis of red cells by mechanical damage and lack of haptoglobin to combine with liberated haemoglobin.

Adolescent↗
PubMed1991

Bovine haptoglobin response in clinically defined field conditions.

In order to assess the usefulness of haptoglobin as a measure of the acute phase response in cattle, the concentration of serum haptoglobin was estimated in the non-infectious conditions of milk fever and ketosis, and in the infectious conditions of severe mastitis, acute severe metritis, retained placenta and chronic endometritis. Mean haptoglobin concentrations were normal in cattle with non-infectious conditions and chronic endometritis but significantly increased in cattle with infectious conditions.

Acute Disease↗
PubMed1998

Serum haptoglobin concentrations in Holstein dairy cattle with toxic puerperal metritis.

The serum concentration of haptoglobin was measured in 51 cows with toxic puerperal metritis which were being treated with one of three different antimicrobial regimens. The mean concentration of haptoglobin was 19.0 mg/dl on the day that the treatments began and declined steadily during the five day treatment period to a mean concentration of 7.35 mg/dl. There was no correlation between the serum haptoglobin concentrations and the rectal temperatures of the cows during the five days.

Animals↗
PubMed2001

Abnormal microheterogeneity of haptoglobin in serum from dogs with various diseases.

Changes in the patterns of glycosylation of canine haptoglobin have recently been demonstrated by isoelectric focusing and immunoblotting. Fucosylated fractions of haptoglobin were identified by selective binding of a fucose-specific lectin. In this study, similar changes were found in the serum of 86 of 137 dogs with various inflammatory, autoimmune and neoplastic diseases. Major changes, including fucosylation, were observed in 40 of the dogs and were most frequent in association with autoimmune haemolytic anaemia. All 40 cases had markedly increased concentrations of haptoglobin and decreased concentrations of haemoglobin. Minor changes were found in the other 46 dogs, whereas no changes in glycosylation were detected in the serum of 40 healthy dogs.

Animals↗
PubMed1985

Haptoglobin and transferrin types in schizophrenia.

Haptoglobin and transferrin types were studied in schizophrenic patients and controls. In the haptoglobin system a significant departure from the Hardy-Weinberg equilibrium with an excess of heterozygotes was found among the patients (p less than 0.01). The distribution of haptoglobin types in the schizophrenic patients was significantly different from that in the controls. The distribution of transferrin types showed a good agreement with the Hardy-Weinberg equilibrium. There was no significant difference between patients and controls with respect to transferrin types.

Gene Frequency↗
PubMed1992

Haptoglobin subtypes in Norway and a review of HP subtypes in various populations.

Isofocusing and immunoblotting of reduced serum samples identify the common haptoglobin alpha-chain variants 1S, 1F, 2FS, 2SS, 2FF, 3, as well as several rare alpha- and beta-chain variants. The gene frequencies found in 6,668 unrelated persons involved in Norwegian paternity cases were: HP*1S: 0.22, HP*1F: 0.16, HP*2FS: 0.58, HP*2SS: 0.04, HP*2FF: 0.004, HP*3: 0.0004, other HP* alpha variants: 0.0004, HP* beta variants: 0.0008. The corresponding gene frequencies in 153 unrelated Norwegian Saamis (Lapps) were: HP*1S: 0.19, HP*1F: 0.07, HP*2FS: 0.70, HP*2SS: 0.04. Norwegians and Norwegian Saamis differed both in phenotype and allele distribution. An earlier Norwegian population study has shown a lower HP*1 frequency in the north than in the south. This regional difference in haptoglobin gene distribution was reflected in the present material as a lower 1F frequency, indicating a Saamish influence in northern Norway. Furthermore, the relatively low 2FF frequency in the north coincides with the lack of observed 2FF genes in the Saamish population. Non-Scandinavians involved in Norwegian paternity cases did not differ from the rest of the material. A review of published haptoglobin gene frequencies shows the 1F frequency to be a good indicator of ethnic origin, and that 2FF and 2SS frequency determinations may also be valuable in genetic population studies.

Alleles↗
PubMed1983

[Changes in blood levels of haptoglobin and ceruloplasmin in vitamin A deficiency in Sprague-Dawley rats].

The aim of the present study was to find out whether the elevation of the serum ceruloplasmin level, previously described in vitamin-A-deficient rats, is a specific phenomenon. Quantitative variations of serum ceruloplasmin, albumin and haptoglobin (whose concentration increased during inflammation) were determined in normal and vitamin-A-deficient rats. Concentrations of ceruloplasmin, haptoglobin, and the value of the haptoglobin to albumin ratio are increased in the serum of vitamin-A-deficient rats compared to normal rats. The results suggested that the increased serum level of ceruloplasmin in vitamin-A-deficient rats was due to the presence of inflammation.

Animals↗
PubMed1981

[13,14-Dihydro-15-keto prostaglandin F2 alpha and haptoglobin in the serum of patients with urogenital tumors].

Prostaglandin F2 alpha can be measured as a stable degradation product, 13,14-dihydro-15-keto-prostaglandin F2 alpha (DHK-PGF2 alpha). Pathological serum levels of this lipid compound have been observed in prostate hyperplasia and treated testicular cancer patients. In renal cancer patients elevated DHK-PGF2 alpha shows a trend to normalize 12 months following nephrectomy in stage T0N0M0. Bladder cancer patients have slightly increased DHK-PGF2 alpha that differ in relation to preinvasive bladder cancer. In contrast serum haptoglobin levels were significantly pathological in patients with kidney and bladder cancer, suggesting involved cancer metabolism. Patients with prostate and testis cancer are without distinct relation to the tumour stage. After specification of haptoglobin types no coincidence to urogenital tumours could be detected. Correlated aberration of PGF2 alpha and haptoglobin displayed different patterns depending on the type of urogenital tumour.

Adult↗
PubMed1980

Transferrin, C3 complement, haptoglobin, plasminogen and alpha 2-microglobulin in patients with urogenital tumors.

The serum levels of transferrin, haptoglobin, C3 proactivator, plasminogen and alpha 2-macroglobulin have been measured in patients suffering from urogenital cancer. In this randomized study, we found a frequent decrease of transferrin coinciding with the elevation of C3-proactivator and haptoglobin. The serum concentration of plasminogen and alpha 2-macroglobulin were rarely observed in the pathological range excluding cancer-associated changes. Tumor metabolites and/or the circulating immune complex may account for the alteration of transferrin, haptoglobin and C3-proactivator, more than primary cancer-related synthesis of these proteins.

Adenocarcinoma↗
PubMed1987

Association of haptoglobin with sodium sensitivity and resistance of blood pressure.

Sodium sensitivity and resistance of blood pressure were examined in 117 normotensive and 85 hypertensive subjects by means of a protocol using rapid extracellular fluid volume expansion with intravenously administered saline (2 L over 4 hours) followed by a day of low dietary sodium intake (10 mEq) and volume contraction induced by a diuretic (furosemide, 120 mg orally). Genetic markers were also examined. Both hypertensive and normotensive subjects with haptoglobin 1-1 phenotype were significantly more (p less than 0.05) likely to be sodium-sensitive than were those with 2-1 or 2-2 phenotypes, and subjects with 2-2 phenotypes were more apt to be sodium-resistant. A second population was examined in which both adults and children with haptoglobin 1-1 phenotype were found to have significantly (p less than 0.05) higher casual systolic and diastolic blood pressures. These two studies independently confirm a relationship between haptoglobin phenotypes and blood pressure and suggest an environmental factor (sodium) as well.

Adolescent↗
PubMed1969

Development of gamma G, gamma A, gamma M, beta IC-beta IA, C 1 esterase inhibitor, ceruloplasmin, transferrin, hemopexin, haptoglobin, fibrinogen, plasminogen, alpha 1-antitrypsin, orosomucoid, beta-lipoprotein, alpha 2-macroglobulin, and prealbumin in the human conceptus.

The synthesis of gammaG, gammaA, gammaM, beta(1C)/beta(1A), C'1 esterase inhibitor, ceruloplasmin, transferrin, hemopexin, haptoglobin, fibrinogen, alpha(1)-antitrypsin, orosomucoid, beta-lipoprotein, alpha(2)-macroglobulin, and prealbumin was studied in 15 normal human embryos and fetuses of 29 days to 18 wk gestation and in the yolk sacs of four embryos from 5.5 to 11.5 wk gestation using tissue culture in (14)C-labeled amino acids followed by radioimmunoelectrophoresis. The human embryo as early as 29 day gestation synthesized beta(1C)/beta(1A), C'1 esterase inhibitor, transferrin, hemopexin, alpha(1)-antitrypsin, beta-lipoprotein, alpha(2)-macroglobulin, and prealbumin in culture. At 32 days gestation ceruloplasmin and orosomucoid were also synthesized, but synthesis of fibrinogen was not observed before 5.5 wk. Synthesis of gammaM occurred as early as 10.5 wk gestation, and gammaG synthesis was found in cultures as early as 12 wk gestation; gammaA synthesis was not detected in any of the tissue cultures. With the exception of the gamma-globulins, each of the proteins studied was synthesized by the liver, but additional sites of synthesis for some of these proteins were also found. Synthesis of gammaG and gammaM occurred primarily in the spleen, but other sites of synthesis were noted as well. Changes in the concentrations of most of these proteins and plasminogen in embryonic and fetal serum from 5.5 to 41 wk gestation, in amniotic fluid from 6.5 to 38 wk gestation, and in the sera of neonates during the 1st 3 wk postpartum are described. Although gammaA, gammaM, ceruloplasmin, or haptoglobin were not detectable in some of the embryonic and fetal sera, gammaA and ceruloplasmin were both present as early as 6.5 wk gestation, haptoglobin by 9.5 wk gestation, and gammaM by 17 wk gestation. Each of the other proteins were present in all of the sera examined.

Abortion, Therapeutic↗
PubMed2006

Haptoglobin-related protein is a high-affinity hemoglobin-binding plasma protein.

Haptoglobin-related protein (Hpr) is a primate-specific plasma protein associated with apolipoprotein L-I (apoL-I)-containing high-density lipoprotein (HDL) particles shown to be a part of the innate immune defense. Despite the assumption hitherto that Hpr does not bind to hemoglobin, the present study revealed that recombinant Hpr binds hemoglobin as efficiently as haptoglobin (Hp). However, in contrast to Hp, Hpr did not promote any high-affinity binding to the scavenger receptor CD163. Binding of hemoglobin to circulating native Hpr incorporated into the HDL fraction was indicated by hemoglobin-affinity precipitation of plasma Hpr together with apoL-I. In conclusion, plasma has 2 high-affinity hemoglobin-binding haptoglobins instead of one, but only Hp-hemoglobin complexes are efficiently recognized by CD163. Circulating Hpr-bound hemoglobin should therefore be taken into consideration when measuring "free" plasma hemoglobin. Furthermore, Hpr-bound hemoglobin might contribute to the biologic activity of the circulating apoL-I/Hpr-containing HDL particles.

Amino Acid Sequence↗
PubMed1989

A simple method for measurement of the haemoglobin binding capacity of canine haptoglobin.

The potential of a series of related compounds to induce haemolytic anaemia in dogs highlighted the need for a reliable and sensitive technique to identify changes in plasma haptoglobin concentration. An indirect method established for human samples was adapted for use with canine plasma. This method measures the haemoglobin binding capacity of plasma, which is directly proportional to the functional haptoglobin concentration. The efficacy of this technique was investigated on samples taken from Beagle dogs which had previously received small quantities of water intravenously. A substantial reduction in haemoglobin binding capacity was recorded before other haematological parameters were significantly affected. It was concluded that measurement of haemoglobin binding capacity by this method provides a valid reflection of haptoglobin status in the dog.

Animals↗