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PubMed2004

[The phenotypes of haptoglobin and the level of acute-phasic proteins in the sera of children with local form of intrathoracic tuberculosis].

Seventy-seven children aged 4-12 years who had local forms of primary intrathoracic tuberculosis were examined. On admission to and discharge from hospital, haptoglobin (Hp) was phenotyped and the content of Hp was measured, and the activity of alpha1-antitrypsin (alpha1-AT) was determined. In all ill children, the distribution of Hp phenotypes did not differ from the normal level, but all patients with tuberculous pleurisy were found to be carriers of Hp1 gene (among them the phenotype Hp 2-2 was absent and the minor variant of Hp 1-1 was detectable in half the cases). In patients of this group, alpha1-AT acted as a typical acute phase reagent and remained moderately increased by the termination of treatment in the vast majority of the examinees. On the contrary, on admission the content of Hp was to be decreased. Its increase was natural only in patients with tuberculous pleurisy. The level of Hp was associated with its phenotype. Carriers of Hp1-1 had elevated levels of Hp in the overwhelming majority of cases whereas those of Hp 2-2 had its decreased levels. It is concluded that in children with primary tuberculosis, the serum level of Hp may not be used as an indicator of the activity of the process. Possible causes and the values of decreased levels of circulating Hp in children with primary tuberculosis are discussed in the paper.

Acute-Phase Proteins↗
PubMed2004

The effect of O-glcnac glycosylation of rat liver nucleoproteins on their acute phase-dependent binding ability to the hormone responsive element of the haptoglobin gene.

We examined whether the transcriptional activation of the rat haptoglobin (Hp) gene during the acute phase (AP) response reflects the O-linked N-acetylglucosamine (O-GlcNAc) status of liver nucleoproteins (NPs) and their binding for the hormone responsive element (HRE). After deglycosylation with N-acetylglucosaminidase of the O-GlcNAc glycoproteins obtained by WGA, affinity chromatography and South-Western analysis, it was observed that only increased HRE binding ability of p64/p70 in control and p51 obtained from turpentine-treated rats can be directly attributed to the presence of O-GlcNAc residues. Therefore, expression of the rat Hp gene could be controlled by this modification of certain trans-acting NPs.

Acetylglucosamine↗
PubMed1992

Hemoglobin-binding site on human haptoglobin. Identification of lysyl residues participating in the binding.

The locus of human haptoglobin (Hp) molecules that interacts with human hemoglobin (Hb) was examined by the differential labeling technique. First, amino groups of Hp were extensively labeled with ethyl acetimidate (EAI) either in the free state (experiment A) or in the equimolar complex with Hb (experiment B). Each of the labeled Hp samples was reduced and S-carboxymethylated, and the remaining amino groups were then allowed to react with trinitrobenzenesulfonic acid (TNBS) under denatured conditions. Only 0.6 mol/mol of the trinitrophenyl (TNP) group was introduced into the heavy chain of Hp in experiment A, whereas 2.5 mol/mol of TNP groups were into the same chain in experiment B. The extent of TNP modification for the light chain was very low in either of the experiments. The amino acid residues carrying TNP groups in the heavy chain were identified by the peptide mapping procedure. They were Ile1, Lys136, and Lys218 in experiment B, and only Ile1 in experiment A. These findings suggest that epsilon-amino groups of Lys136 and Lys218 in the heavy chain are both situated within the Hb-binding locus of Hp, and that the alpha-amino group of Ile1 is buried inside the molecule either in the presence or absence of Hb.

Amino Acid Sequence↗
PubMed2006

Haptoglobin phenotypes, which one is better and when?

Haptoglobin (Hp) phenotype 2-2 presents characteristics of being an independent risk factor for cardiovascular disease (CVD) and more significant in diabetic CVD. In chronic kidney disease (CKD), due to various processes that take place simultaneously, the combined effect is different in the elderly and the young. In older patients (> 60 years), Hp 2-2 is associated with a greater risk for cardiovascular and renal morbidity and mortality. In younger (< 60 years) hemodialysis patients, infections and high hemoglobin turnover are predominant, and patients with Hp 2-2 have a longer survivorship than those with Hp 1-1. The functional differences between the Hp phenotypes are most probably due to their antioxidative property and to macrophage activation with differential release of cytokines.

Age Factors↗
PubMed1991

[Haptoglobin phenotypes and serum enzyme activity].

Haptoglobin (Hp) phenotypes were determined by thin-layer polyacrylamide gel electrophoresis in 2071 normal Russians, Tatars, and Bashkirs. Hp phenotype distribution was found similar in these populations, making up 13.4% for Hp 1-1, 48% for Hp 1-2, 38.6% for Hp 2-2. Hp1 gene incidence (0.37) was characteristic of the European populations. Serum alkaline phosphatase and gamma-glutamyl transpeptidase activities were similar in all the three Hp phenotypes. Alanine and aspartate aminotransferases and acid phosphatase activities were higher in Hp 1-1 phenotype by 25, 15, and 15 percent, respectively.

Enzymes↗
PubMed1991

[Status of the bronchi in patients with pulmonary tuberculosis and different haptoglobin phenotype].

External respiration function test and bronchologic examination were conducted in 206 pulmonary tuberculosis patients with different haptoglobin (Hp) phenotypes. It was found that obstructive changes in peripheral portions of the bronchial tree were most common and marked among the revealed disorders of pulmonary ventilation function. These changes promote a decrease in the ventilation reserve to a great extent. As compared to Hp 2-1 carriers, specific endobronchitis and bronchial obstruction symptoms were significantly more frequent in patients with Hp 2-2. Bronchial obstruction symptoms alone were twice as frequent as in patients with Hp 1-1 than in Hp 2-1 carriers. The findings indicate that there is a close relationship between the status of the bronchi in pulmonary tuberculosis patients and the genetically determined Hp phenotype.

Adult↗
PubMed1991

Haptoglobin levels among alcoholics in Alaska.

The levels of haptoglobin, plasma proteins and amino acids were studied in a non-fasting population of alcoholics. In 25 subjects, only small differences were seen between the means when Native subjects were compared to non-Native. There did not appear to be any acute phase response differences between these two groups. This study did not substantiate other reports on the correlation of the severity of alcoholism with glycoprotein synthesis.

Alaska↗
PubMed1991

Isolation and characterization of bovine haptoglobin from acute phase sera.

A macromolecular hemoglobin-binding protein, which was not detectable in normal bovine sera but appeared during acute phase inflammation, was purified, characterized, and designated as bovine haptoglobin (Hp). The purified protein had a molecular mass of 1,000-2,000 kDa, and was composed of two kinds of peptides, a 20-kDa peptide (alpha chain) and a 35-kDa glycopeptide (beta chain) linked by disulfide bonds. Amino acid composition and N-terminal sequence analyses revealed that both peptides were homologous to each counterpart of human Hp. Studies using some reducing reagents proved that highly polymerized Hp in serum was composed of 2-20 polymerized forms of alpha 2 beta 2 tetramer. Hp could bind one molecule of hemoglobin/alpha 2 beta 2 unit. Hp with smaller sizes obtained from native Hp by partial reduction with cysteine showed almost the same Hb-binding capacity.

Acute-Phase Reaction↗
PubMed1991

Detection of haptoglobin from concentrated urine samples by enzyme immunoassay.

The detection of haptoglobin (Hp) from serum and bloodstains is utilized extensively in forensic science laboratories in order to include or exclude possible donors. There is an increasing need to make the same discriminations utilizing genetic markers from urine samples. This paper describes the use of enzyme immunoassay and Western blotting (electrophoretic) techniques to determine Hp phenotypes from concentrated urine samples. Serum and urine specimens were collected from volunteer donors. The serum sample from each donor was typed for Hp. The urine specimens were concentrated 3000-fold from the starting volume of 15 mL to a final volume of 5 microL and applied to the gradient polyacrylamide gels. This procedure allows the separation of Hp samples into the three common phenotypes as well as the other rare variants found in humans. The Western blotting electrophoretic technique was used to achieve the transfer of Hp bands from the gels to the nitrocellulose membranes. Enzyme immunoassay with goat anti-Hp antiserum and rabbit anti-goat immunoglobulin alkaline phosphatase conjugate were used to identify the Hp bands from the concentrated samples. Specimens stored for six months at -22 degrees C were also concentrated and typed successfully. Recent implementation of drug-screening policies has resulted in an increase in the submission of substituted urine specimens. The above procedure can be used to detect an additional genetic marker from urine samples and thus facilitate the identity of the donor.

Blotting, Western↗
PubMed1990

Identification of the crossing-over point of a hybrid gene encoding human glycophorin variant Sta. Similarity to the crossing-over point in haptoglobin-related genes.

One of the human glycophorin variants, Stones (Sta), has been shown to be the product of a hybrid gene of which the 5'-half derived from the glycophorin B (GPB) gene whereas the 3'-half derived from the glycophorin A (GPA) gene. The present study reveals the crossing-over point of this hybrid gene from the analysis of polymerase chain reaction products. The genomic sequences encompassing the region corresponding to exon 3 to exon 4 of GPA were amplified by polymerase chain reaction with oligonucleotide primers synthesized according to GPA and GPB genomic sequences (Kudo, S., and Fukuda, M. (1989) Proc. Natl. Acad. Sci. U.S.A. 86, 4619-4623). After subcloning the products, the nucleotide sequences derived from GPA, GPB, and putative Sta genes were determined. Comparison of the nucleotide sequences of GPA, GPB, and Sta genes indicate that the crossing-over took place 200 base pairs upstream from the first nucleotide of exon 4. Intriguingly, the nucleotide sequence surrounding the putative crossing-over point is homologous to the crossing-over point proposed for haptoglobin genes (Maeda, N., McEvoy, S.M., Harris, H.F., Huisman, T.H.J., and Smithies, O. (1986) Proc. Natl. Acad. Sci. U.S.A. 83, 7395-7399). These results suggest strongly that homologous recombination through unequal crossing-over can be facilitated by specific genomic elements, such as those in common in these two crossing-over events. The present study also revealed that this Sta individual has a variant GPA gene; substitution of adenine for guanine at the nucleotide for codon 39 results in substitution of lysine for arginine at amino acid 39, and loss of an SstI restriction site.

Amino Acid Sequence↗
PubMed1990

Cerebral blood flow and serum haptoglobin in the diagnosis of death by rapid drowning.

Diagnosis of death and the feasibility of resuscitation in cases of acute drowning in fresh water (FW) or sea water (SW) inhalation in rabbits were evaluated using cardiopulmonary function monitoring, measurement of cerebral blood flow (CBF) and determination of haptoglobin (HP). Death took place more quickly in FW drowning, two to five minutes, as compared with four to seven minutes required in SW drowning. In view of the CBF patterns in the brain circulation, many problems exist regarding the judgement of the point of death and the applicability of resuscitation. However, it is considered that brain damage in SW drowning occurs more rapidly than in FW drowning.

Animals↗
PubMed1990

Identification of haptoglobin alpha-2FF variants in mid-trimester maternal serum as potential markers for Down syndrome.

Exploratory protein analysis in mid-trimester maternal sera by 2-dimensional electrophoresis and image analysis was performed to determine the differences between mothers carrying fetuses with Down syndrome (DS) and control mothers. Nine haptoglobin alpha-1 and alpha-2 (Hp1 and Hp2) variants were detected. Three apparent isoforms of the Hp2FF protein having the same relative charge but different Mr's were detected, with the two smaller variants--Hp2FF (-0.7k) and Hp2FF (-1.3k)--believed to be first reported here. Ninety-two percent of the cases (n = 83) had the Hp2FF (-0.7k) protein, and 61% had Hp2FF (-1.3k). The geometric mean concentration of Hp2FF (Mr = 18.0 kd) was found to be significantly increased (P less than 0.01) in mid-trimester sera from cases (n = 27) compared to controls (n = 56). When the concentrations of the three Hp2FF isoforms were added, the cases had larger sums on average than controls (P less than 0.01).

Age Factors↗
PubMed1990

[Study on the usefulness of haptoglobin used on endoscopic injection sclerotherapy].

The effect of haptoglobin (Hp) used on endoscopic injection sclerotherapy (EIS) was evaluated by examining the increase of serum free hemoglobin (FHb) and the changes of renal function. In control group, the increase of serum FHb (delta FHb) was paralleled with the volume of 5% ethanolamine Oleate (EO) injected intravariceally, and free Hp (FHp) was disappered in this group soon after EIS. On the contrary, in the group treated with Hp, neither the increase of FHb nor decrease of FHp were recognized. The significant increase of urine beta 2 microglobulin and NAG was recognized in control group. Therefore, if Hp is used at initial EIS, it would be prevented that serum FHb due to intravascular hemolysis increases, consequently the possibility of renal dysfunction.

Adult↗
PubMedDate not supplied

[Analysis of sheep blood serum haptoglobin].

Three types of haptoglobin (Hp), differing in the number of bands of Hp--Hb complex on polyacrylamide gel electrophoregramm are found in sheep blood serum. HpA, HpB and HpC fractions included one, two-three and six-eight bands respectively. A modified procedure for the HpC isolation is described. Effects of urea, sodium dodecylsulpate, beta-mercaptoethanol, pH and maleinization on the behaviour of HpC under polyacrylamide gel electrophoresis is studied. The data obtained suggest that the HpC molecule consists of two subunits (of alpha and beta types), bound with S--S bounds in an alphabeta-dimer, which form a whole HpC molecule for the expense of non-covalent bonds.

Animals↗
PubMed1985

Behavior of haptoglobin in experimental allergic encephalomyelitis in chickens.

Concentration of haptoglobin (Hpc) in serum of chickens with inflammation and allergic encephalomyelitis (EAE) was determined. Chickens with aseptic inflammatory state revealed 2.5 times higher concentration of Hpc while in the course of EAE only small increase was observed. Administration of immunomodulator--isoprinosine, resulted in elevation of Hpc level as compared to nontreated chickens.

Animals↗
PubMed1988

[Comparative studies of bronchial secretions in children with chronic, nontuberculous lung diseases. 3. The detection of lysozyme, transferrin, alpha 1-antitrypsin, alpha 2-macroglobulin, haptoglobin and alpha 1-acid glycoprotein].

In 166 bronchial secretions from 63 children with chronic nontuberculous lung diseases lysozyme, transferrin, alpha 1-antitrypsin, alpha 2-macroglobulin, haptoglobin and alpha 1-acid glycoprotein were estimated. In patients with hard bronchoscopic or bronchographic alterations a reduction of lysozyme, alpha 1-antitrypsin and alpha 2-macroglobulin could be found. These proteins were measured more frequently in cases with dark altered mucosa. Moreover no relation could be found between transferrin, alpha 1-antitrypsin and alpha 2-macroglobulin and the outbreak of the diseases. -In bacterial contaminated secretions transferrin could be demonstrated more frequently in comparison with sterile bronchial secretions.

Adolescent↗
PubMed1989

[Determination of haptoglobin phenotypes using electrophoresis in viral hepatitis B, HBsAg carriers and normal subjects].

Haptoglobin (Hp) phenotype distribution has been examined in 193 patients with an acute icteric form of hepatitis B (HBsAg+), in 36 chronic HBsAg carriers, and in 317 normal controls. The incidence rates of three Hp types have been virtually the same in the acute patients and in the controls. In chronic HBsAg carriers the Hp 1-1 type has been detected 3 times more frequently than in acute hepatitis B patients and 4 times more frequently than in normal subjects. The authors suppose that the presence of Hp 1-1 type is one of the genetic factors that determine (in case of a hepatitis B infection) the liability to the development of a chronic subclinical infectious process and not of an acute form of this infection.

Blood Protein Electrophoresis↗