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PubMed1980

[Haptoglobin types and chronic glomerulonephritis].

In 88 patients a chronic glomerulonephritis was diagnosed by histology and immunohistology. The haptoglobin type was also analyzed. The distribution of the haptoglobin types in the sample did not differ from the haptoglobin distribution in the population of Berlin. The distributions of histologic and immunohistologic forms of glomerulonephritis were related to the haptoglobin distribution in our patients. The distribution of histological subgroups does not depend on the distribution of the haptoglobins. In evaluation of the immunohistological subgroups we found that immunocomplexnephritis is less frequent in the group Hp 1--1 than in the groups 2--1 and 2--2. We suppose that persons with Hp 2--1 and Hp 2--2 are prone to increased antibody formation. Hp 1--1 is presumably a blocking antibody.

Antibody Formation↗

PubMed1995

Changes of haptoglobin and free hemoglobin due to blood transfusion.

Serum total haptoglobin and free hemoglobin levels during blood transfusion were investigated in 17 elective surgeries. Total haptoglobin and free hemoglobin levels in 73 stored whole blood were also investigated for different storage periods. Free hemoglobin was detected in serum when total haptoglobin level became 130 mg/dl or less and a mean storage period of transfused bloods were 11 days or longer. Total haptoglobin level became 130 mg/dl or less at a transfusion volume of 600 ml or more. No constant relationship was recognized between transfusion speed and total haptoglobin or free hemoglobin levels. In the stored whole blood, free hemoglobin level increased in accordance with an increase of storage period and it reached significant increase on 7-9 storage period against 1-3 storage period. The detection rate of free hemoglobin increased significantly when it was stored for 7 days or longer. It was concluded that 7 days or more stored whole bloods had free hemoglobin, but serum free hemoglobin was detected when 600ml or more of 11 days or longer whole bloods were transfused.

Adolescent↗

PubMed1975

The modification of hemoglobin-antihemoglobin reaction by haptoglobin.

In radioimmunoassay and double diffusion experiments, the reaction between hemoglobin (Hb) and antihemoglobin antibody is markedly affected by the presence of haptoglobin (Hp). Binding with haptoglobin exposes "neoantigenic" determinants in hemoglobin, probably as a result of conformational changes exposing previously inaccessible structures. Some of these are shared by both Hb A and Hb F an may be located on alpha-chains. The exposure of these determinants requires the binding of hemoglobin by haptoglobins of the phenotype Hp 2-2 or Hp 2-1. The phenotype Hp 1-1 and guinea pig haptoglobin have no discernible effect in this context. It thus appears that the conformational change induced in hemoglobin by the "polymeric" forms of haptoglobin differ from those, if any, caused by the "monomeric" forms such as Hp 1-1. Most antisera raised against free hemoglobin contain some antibodies specific for these hidden determinants which may have become exposed during the processing of the immunizing antigen. These findings have significant implication in the interpretation of radioimmunoassay data.

Animals↗

PubMed1997

[Dependence of the concentration of maternal serum markers on the haptoglobin gene].

This paper is the first in a series devoted to the investigation of the possible effect of maternal genotype on the levels of fetal alpha-fetoprotein (AFP) and human chorionic gonadotrophin (HCG) entering maternal blood. We studied the possible association between the maternal haptoglobin system and levels of maternal AFP and HCG, which are markers of fetal pathology. Haptoglobin types were determined in groups of pregnant women with different levels of serum markers. Distribution of haptoglobin types differed from the theoretically expected in one out of five groups tested. In the group with low AFP level, a significant decrease in frequency of the Hp*2 allele was found. A statistically significant decrease of the mean haptoglobin concentration in the group with low levels of AFP and elevated levels of HCG was observed. A reduction in serum haptoglobin concentration was shown to be accompanied by a decrease of serum iron concentration. The possible mechanism underlying the influence of maternal genotype on the levels of AFP and HCG in maternal blood are discussed.

Biomarkers↗

PubMed1989

[Effects of exocorpol and haptoglobin on hemolysis during ECC].

This study was performed to evaluate the effects of Exocorpol and Haptoglobin on hemolysis during ECC. We measured free hemoglobin (F-Hb) and free haptoglobin (F-Hp) at pre- and post-ECC. Patients were divided four groups: Group C, 5 patients undergoing no treatment; Group Ex, 5 patients undergoing treatment of Exocorpol; Group Hp, 5 patients undergoing treatment of Haptoglobin; Group Ex + Hp, 5 patients undergoing treatment of Exocorpol and Haptoglobin. F-Hb of pre- and post-ECC in four groups were 0 mg/dl: 85 mg/dl (Group C, p < 0.01), 0 mg/dl: 2 mg/dl (Group Ex, NS), 0 mg/dl: 1 mg/dl (Group Hp, NS), 0 mg/dl: 0 mg/dl (group Ex + Hp, NS). F-Hp of pre- and post-ECC in four groups were 143 mg/dl: 9 mg/dl (Group C, p < 0.02), 133 mg/dl: 25 mg/dl (Group Ex, p < 0.05), 186 mg/dl: 195 mg/dl (Group Hp, NS), 66 mg/dl: 163 mg/dl (Group EX + Hp, p < 0.05). There was no significant difference in F-Hb and F-Hp of pre-ECC among four groups. F-Hb of post-ECC in Group C was significantly higher than that of Group Ex, Hp and Ex + Hp (p < 0.01), and F-Hp of post-ECC in Group Hp and Ex + Hp was significantly higher than that of Group C and Ex.(p < 0.01, p < 0.02). We concluded that Exocorpol and Haptoglobin were effective on hemolysis during ECC, and combination of these was more effective.

Extracorporeal Circulation↗

PubMed1996

The biological role of haptoglobin and behaviour of this protein in different diseases, with special attention paid to brain stroke.

Haptoglobin (Hp) is an alpha 2 glycoprotein, the presence of which was determined in blood serum in 1940 by Polonovski and Jayle. Smithies showed genetically conditioned polymorphism of haptoglobin (4, 16). Molecular heterogeneity of haptoglobin is demonstrated by three main phenotypes: Hp 1-1, Hp 2-2, Hp 2-1. Haptoglobin is a glycoprotein with tetrametric structure. Haptoglobin 1-1 is composed of two alpha (light) chains with 9,000 molecular mass including 83 amino acids and two beta (heavy) chains with 40,000 molecular mass including 245 amino acids. Alpha chains are connected with each other by two sulfurous bonds which also connect alpha chains with beta chains (3, 4).

Acute-Phase Proteins↗

PubMed1998

Haptoglobin polymorphism, iron metabolism and mortality in HIV infection.

BACKGROUND: Three phenotypes of the antioxidant protein haptoglobin are known: Hp 1-1, Hp 2-1 and Hp 2-2. OBJECTIVES: To investigate the outcome of HIV infection according to haptoglobin type. DESIGN AND METHODS: Haptoglobin phenotypes were determined using starch gel electrophoresis in serum obtained from 653 HIV-infected Caucasians in the AIDS reference centers of Gent (n = 184), Antwerp (n = 309), and Luxembourg (n = 160). Survival was compared between haptoglobin types using Kaplan-Meier curves. Plasma HIV-1 RNA was quantified by reverse transcriptase PCR. Serum iron, transferrin saturation, ferritin, and vitamin C were assayed to evaluate iron-driven oxidative stress in 184 HIV-infected patients and 204 controls. RESULTS: The haptoglobin type distribution amongst the patients (17.6% Hp 1-1, 49.9% Hp 2-1, 32.5% Hp 2-2) corresponded to that of the controls. Kaplan-Meier curves showed a higher mortality for the Hp 2-2 group (P = 0.0001; adjusted mortality risk ratio, 1.78; 95% confidence interval, 1.25-2.54). Median survival time was 11.0 years (Hp 1-1 and Hp 2-1) versus 7.33 years (Hp 2-2). Plasma HIV-1 RNA levels prior to antiviral therapy and their increase over 1 year were highest in Hp 2-2 patients (P = 0.03 and 0.003, respectively). The Hp 2-2 type was associated with higher serum iron, transferrin saturation, and ferritin levels and with low vitamin C concentrations. Furthermore, ferritin concentrations were higher in HIV-infected patients than in controls (P < 0.0001). CONCLUSION: HIV-infected patients carrying the Hp 2-2 phenotype show a worse prognosis, which is reflected by a more rapid rate of viral replication (in the absence of antiviral treatment). They also accumulate more iron and oxidize more vitamin C, suggesting that less efficient protection against haemoglobin/iron-driven oxidative stress may be a direct mechanism for stimulating viral replication.

Adult↗

PubMed1997

Effect of dystocia on serum haptoglobin in Awassi ewes.

Serum haptoglobin concentration was determined in 102 Iraqi Awassi ewes. Blood samples were collected from 82 ewes before the correction of dystocia, 10 ewes with eutocia 2 to 4 h after parturition and 10 nonpregnant ewes during the seasonal anestrus phase. The mean serum haptoglobin concentration was significantly higher (P < 0.01) in ewes with dystocia than in ewes with normal births and in the nonpregnant ewes. No significant difference was found between serum haptoglobin concentrations of ewes with ringwomb and ewes with dystocia due to other causes. There was a significant elevation (P < 0.01) of serum haptoglobin in cases treated 24 h after labor compared with those treated during the first 24 h. Significant (P < 0.05) differences were found between serum haptoglobin concentrations in ewes treated surgically and those treated manually.

Journal Article↗

PubMed1960

SERUM HAPTOGLOBINS IN HAEMOLYTIC STATES.

Serum haptoglobin levels have been studied in patients with a number of haemolytic disorders. In general, serum haptoglobins were low in patients with increased haemolysis. Values were reduced irrespective of whether haemolysis occurred intravascularly or extravascularly. The reduction was related to the amount of haemoglobin destroyed per day. Serum haptoglobins may be raised in certain neoplasms and infections and during adrenocortical steroid hormone therapy. A rise in haptoglobins due to one of these factors may mask a fall due to haemolysis. Thus a normal or raised serum haptoglobin does not necessarily exclude a haemolytic process.

Journal Article↗

PubMed1990

Close linkage between panic disorder and alpha-haptoglobin excluded in 10 families.

We previously reported a lod score of 2.3 suggesting linkage between panic disorder and the alpha-haptoglobin locus on chromosome 16q22 in 26 pedigrees. In the present study we tested for linkage between alpha-haptoglobin and panic disorder in 10 new pedigrees and excluded a gene for panic disorder from 6 centimorgans (recombination fraction, 0.06) surrounding the alpha-haptoglobin locus. The data were analyzed under a variety of assumptions about the transmission of panic disorder, and linkage was excluded by all genetic models but one. When lod scores from the present set of 10 pedigrees were pooled with those from the first 26, no evidence of genetic heterogeneity was found, and the maximum lod score was 0.67 at a recombination fraction of 0.17. Taken as a whole, the present findings do not support the presence of a disease gene for panic disorder closely linked to the alpha-haptoglobin locus on chromosome 16q22.

Adult↗

PubMed2003

Matrix-assisted laser desorption/ionization- quadrupole ion trap-time of flight mass spectrometry sequencing resolves structures of unidentified peptides obtained by in-gel tryptic digestion of haptoglobin derivatives from human plasma proteomes.

Two-dimensional gel electrophoresis-separated and excised haptoglobin alpha2-chain protein spots were subjected to in-gel digestion with trypsin. Previously unassigned peptide ion signals observed in mass spectrometric fingerprinting experiments were sequenced using the matrix-assisted laser desorption/ionization-quadrupole ion trap-time of flight (MALDI-QIT-TOF) mass spectrometer and showed that the haptoglobin alpha-chain derivative under study was cleaved by trypsin unspecifically. Abundant cleavages occurred C-terminal to histidine residues at H23, H28, and H87. In addition, mild acidic hydrolysis leading to cleavage after aspartic acid residues at D13 was observed. The uninterpreted tandem mass spectrometry (MS/MS) spectrum of the peptide with ion signal at 2620.19 was submitted to database search and yielded the identification of the corresponding peptide sequence comprising amino acids (aa) aa65-87 from the haptoglobin alpha-chain protein. Also, the presence of a mixture of two tryptic peptides (mass to charge ratio m/z 1708.8; aa40-54, and aa99-113, respectively), that is caused by a tiny sequence variation between the two repeats in the haptoglobin alpha2-chain protein was resolved by MS/MS fragmentation using the MALDI-QIT-TOF mass spectrometer instrument. Advantageous features such as (i) easy parent ion creation, (ii) minimal sample consumption, and (iii) real collision induced dissociation conditions, were combined successfully to determine the amino acid sequences of the previously unassigned peptides. Hence, the novel mass spectrometric sequencing method applied here has proven effective for identification of distinct molecular protein structures.

Alleles↗

PubMed2000

Inhibition by deacetylase inhibitors of IL-1-dependent induction of haptoglobin involves CCAAT/Enhancer-binding protein isoforms in intestinal epithelial cells.

Intestinal epithelial cells participate in an acute phase response (APR) by responding to cytokines and by expressing acute phase protein genes. We hypothesized that butyrate, a fermentation product of the bacterial intestinal flora with deacetylase activity, affects the APR in intestinal epithelial cells. Sodium butyrate (NaBu) and Trichostatin A (TSA) induced alkaline phosphatase activity and histone H4 acetylation in IEC-6 rat intestinal epithelial cells treated with or without interleukin-1beta (IL-1). In contrast, both NaBu and TSA attenuated the IL-1-dependent induction of the acute phase protein gene haptoglobin, as well as C/EBPbeta and C/EBPdelta transcription factors mRNAs. Gel shift and supershift assays showed a strong decrease in the IL-1-induced C/EBPbeta and C/EBPdelta containing complexes binding to the HaptoA C/EBP DNA-binding site of the haptoglobin promoter, by NaBu and TSA. Furthermore, site-specific mutation of the HaptoA site abolished the NaBu- and TSA-dependent inhibition of haptoglobin, as determined by transient transfection assays. These results suggest that deacetylase inhibitors may regulate the IL-1 dependent induction of haptoglobin by down-regulating C/EBP isoforms, and that C/EBPs represent a target for the action of butyrate in the control of the APR of intestinal epithelial cells.

Animals↗

PubMed1998

Expression of the protective proteins hemopexin and haptoglobin by cells of the neural retina.

The blood-retinal barrier, consisting of retinal pigment epithelial cells and retinal endothelial cells, prevents hemopexin and haptoglobin, anti-oxidant protective plasma proteins normally synthesized by the liver, from entering the neural retina. If present, these proteins must, therefore, be made locally. The cell types within the retina in which hemopexin and haptoglobin mRNAs are made have been investigated. RNA was extracted from both the neural retina and pigment epithelium obtained by dissection of human donor eyes as well as from cultured pigment epithelial and photoreceptor cells. The mRNAs for both haptoglobin and hemopexin were detected, using reverse-transcriptase polymerase chain reaction, in the neural retina and cultured photoreceptors but not in pigment epithelial cells. The cellular location of these mRNAs was determined using in situ hybridization of sections of human retina which revealed that haptoglobin mRNA was located principally in the photoreceptor cells, cells of the inner nuclear layer and some cells of the ganglion cell layer. Hemopexin mRNA, previously shown to be made in the human neural retina (Hunt et al., 1996. Journal of Cellular Physiology 168: 71-80), is expressed by most of the cells of neural retina including the photoreceptors and, notably, the ganglion cells.

Antioxidants↗

PubMed1994

Parallel evolutionary events in the haptoglobin gene clusters of rhesus monkey and human.

Parallel occurrences of evolutionary events in the haptoglobin gene clusters of rhesus monkeys and humans were studied. We found six different haplotypes among 11 individuals from two rhesus monkey families. The six haplotypes include two types of haptoglobin gene clusters: one type with a single gene and the other with two genes. DNA sequence analysis indicates that the one-gene and the two-gene clusters were both formed by unequal homologous crossovers between two genes of an ancestral three-gene cluster, near exon 5, the longest exon of the gene. This exon is also the location where a separate unequal homologous crossover occurred in the human lineage, forming the human two-gene haptoglobin gene cluster from an ancestral three-gene cluster. The occurrence of independent homologous unequal crossovers in rhesus monkey and in human within the same region of DNA suggests that the evolutionary history of the haptoglobin gene cluster in primates is the consequence of frequent homologous pairings facilitated by the longest and most conserved exon of the gene.

Animals↗

PubMed2004

Convulsive disorder and genetic polymorphism. Association of idiopathic generalized epilepsy with haptoglobin polymorphism.

Haptoglobin is a polymorphic protein that is well known for its hemoglobin (Hb)-binding property. The protein shows gross differences in molecular size among genotypes, resulting in different degrees of diffusion in central nervous system tissue. Since the breakdown of erythrocytes in the intracerebral fluid results in Hb-mediated free OH radical formation, lipid peroxidation, and increased neuronal excitability, a differential diffusion of haptoglobin phenotypes in the intracerebral fluid might result in a different degree of protection from oxidative damage. We have studied two samples of children with idiopathic generalized epilepsy from two different Italian populations. In both samples the haptoglobin *1/*1 genotype is much less represented in epileptic children than in controls. These observations suggest that subjects carrying the Hp*1/*1 genotype, that has the lowest molecular size and diffuses more readily in the interstitial cerebral fluid, are more protected against idiopathic generalized epilepsy than those with other haptoglobin genotypes.

Adult↗

PubMed1984

Typing and subtyping of haptoglobin from native serum using disc gel electrophoresis in alkaline buffer: application to routine screening.

A method with which the six common phenotypes of human haptoglobin can be identified using unseparated serum is described. In contrast to other reported methods, both typing and subtyping of haptoglobin can be performed by polyacrylamide gel electrophoresis in alkaline buffer using 0.1-4.0 microliter of native serum with hemoglobin added. Haptoglobin-hemoglobin complexes are visualized by their peroxidase activity using benzidine and barium peroxide. This relatively inexpensive and fast method seems particularly well suited for the typing and subtyping of haptoglobin from minute amounts in large series of sera and other body fluids and thus may be useful in medical genetics and forensic medicine.

Adult↗

PubMed1983

Biosynthesis, intracellular processing and secretion of haptoglobin in cultured rat hepatocytes.

Biosynthesis, intracellular processing and secretion of the hetero-tetrameric (alpha 2 beta 2) glycoprotein, haptoglobin, were studied in primary cultured rat hepatocytes. The results obtained from pulse-chase experiments demonstrated that haptoglobin was initially synthesized as a larger precursor (pro-form), a single polypeptide chain comprising both the alpha- and beta-subunits, and immediately cleaved into subunits during intracellular transport, although about 8% of the newly synthesized haptoglobin was secreted as a pro-form. Monensin which impedes the secretory process at the Golgi complex blocked the complete glycosylation of beta-subunit but rather accelerated the conversion of the pro-form to subunits. These results indicate that the proteolytic processing of the haptoglobin precursor takes place at an early stage before the Golgi complex of the intracellular transport.

Animals↗

PubMedDate not supplied

A preliminary study of serum haptoglobin concentration as a prognostic indicator of ovine dystocia cases.

Serum samples were collected prior to the correction of dystocia in 45 sheep and from nine sheep following a normal parturition. Serum samples collected from a group of 16 non-pregnant ewes acted as non-pregnant controls. The mean serum haptoglobin concentration was significantly elevated (P less than 0.01) in those dystocia cases where dead lambs were present in utero compared to those ewes which had live lambs delivered. While the number of cases presented in this study is small, there is an indication that sheep with a serum haptoglobin concentration above 1.0 g/l represent a poor surgical risk. The three ewes which died following a caesarean operation had markedly elevated serum haptoglobin concentrations prior to surgery indicating an inflammatory reaction. Five ewes with a haptoglobin concentration of 0.4 g/l made an uneventful recovery following a caesarean operation.

Animals↗