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Biomedical subjects

H Anundi

Publications and source records attributed to H Anundi.

At least 19 recordsLinked to original sources
PubMed1993

High exposures to organic solvents among graffiti removers.

The exposure to organic solvents among 12 graffiti removers was studied. Health effects were also assessed by structured interview and a symptom questionnaire. Blood and urine samples were collected at the end of the day of air sampling. The concentrations of dichloromethane, glycol ethers, trimethylbenzenes and N-methyl-2-pyrrolidinone in the breathing zone of each worker were measured during one working day. The 8-h time-weighted average exposure to dichloromethane ranged from 18 to 1200 mg/m3. The Swedish Permissible Exposure Limit value for dichloromethane is 120 mg/m3. The air concentrations of glycol ethers, trimethylbenzenes and N-methyl-2-pyrrolidinone were low or not detectable. No exposure-related deviations in the serum concentrations of creatinine, aspartate transaminase, alanine transaminase, gamma-glutamyl transpeptidase or hyaluronan or the urine concentrations of alpha 1-microglobulin, beta 2-microglobulin or N-acetyl-beta-glucosaminidase were found. Irritative symptoms of the eyes and upper respiratory tract were more prevalent than in the general population. This study demonstrates that old knowledge about work hazards is not automatically transferred to new professions. Another aspect is that the public is also exposed as the job is performed during daytime in underground stations. At least for short periods, bystanders may be exposed to high concentrations of organic solvent vapours. People with predisposing conditions, e.g. asthmatics, may risk adverse reactions.

Adolescent↗
PubMed1993

Exposure dependent increase in DNA single strand breaks in leucocytes from workers exposed to low concentrations of styrene.

Single strand breaks in DNA were monitored in leucocytes from 17 men occupationally exposed to styrene. Personal air monitoring was carried out during one workday with two diffusion samplers and a portable photoionisation detector placed in the breathing zone. Exposure to styrene was also monitored by analysing styrene in blood and urine and mandelic acid in urine. Single strand breaks were measured in leucocytes by the alkaline elution technique. The biological samples were collected before a shift, at the end of a shift, and the next morning, before the next shift. An exposure dependent increase in single strand breaks was seen at the end of a shift but not before a shift or the next morning. Linear regression analysis indicated that the amount of DNA damage was roughly doubled after eight hours of exposure to 18 ppm styrene or at a urine concentration of 240 mg mandelic acid/g creatinine compared with the damage in non-exposed men. This study indicates that monitoring of single strand breaks with the alkaline elution technique may be a sensitive marker of genotoxic effects. To our knowledge, this is the first time that such a marker has been shown to correlate with exposure to less than 20 ppm styrene.

Adult↗
PubMed1993

Increase in neuropsychiatric symptoms after occupational exposure to low levels of styrene.

The results of this study suggest that exposure to styrene below the current Swedish permissible exposure limit of 20 ppm induces neurotoxic effects expressed as an increased number of neuropsychiatric symptoms. Twenty men exposed to styrene at a plastics factory participated. The reference group included 20 non-exposed men matched for age, working schedule, and physical work load. Exposure to styrene during one workday was assessed by personal air monitoring and biological monitoring. To evaluate the physical work load the pulse(heart) rate was measured. One week before the study each man completed a neuropsychiatric symptom questionnaire containing 16 items. Also 17 questions regarding acute symptoms of local irritation and symptoms of the central nervous system were presented after the psychometric tests were performed. The tests were simple reaction time, colour word vigilance, and symbol digit. A follow up with regard to the symptoms among the exposed men was done after their summer vacation, about two to five weeks after their last exposure. The mean eight hour time weighted average (TWA) concentration of styrene in air, measured by passive dosimetry was 8.6 ppm (range 0.04-50.4 ppm). The exposed men had significantly more symptoms than the referents although there were no significant differences for the psychometric tests. At the follow up the exposed men reported fewer symptoms. This study indicates that symptoms are earlier indicators of adverse effects than complex tests and underlines the importance of regular follow up of people exposed to styrene (and probably organic solvents in general).

Acute Disease↗
PubMed1991

Identification of human blood plasma and serum proteins in two-dimensional gels by use of protein A-Sepharose: application to alpha 1-microglobulin.

The relative position identification of some of the proteins in human blood plasma and serum after separation by two-dimensional electrophoresis (2-DE) in gel slabs have been studied. Antibodies specific to the protein to be identified were first immobilized on Protein A-Sepharose. Serum or plasma samples devoid of this protein were obtained following adsorption and subsequently the protein itself was eluted. The preparations were examined by 2-DE, silverstaining and blotting with parallel analysis of the purified proteins. Position identification in 2-DE gels of the spots of alpha 1-microglobulin (= protein HC) is shown as an example. The technique has general applicability not only for identification of the positions in 2-DE gels of serum and plasma proteins but also for proteins in other fluids, tissues and organs from humans and other species.

Alpha-Globulins↗
PubMed1987

The complete amino acid sequence of human serum retinol-binding protein.

The complete amino acid sequence of human serum Retinol-binding protein (RBP) including the distribution of its three disulfide bridges, has been determined. The protein consists of 182 amino acid residues, the order of which was determined following the isolation of five CNBr-fragments. Direct amino acid sequence analysis in an automatic liquid phase sequencer provided almost the entire sequences of the five CNBr-fragments. Several sets of enzymatically derived peptides of RBP were also used to elucidate the primary structure. RBP displays significant homology to bovine beta-lactoglobulin, human alpha 1-microglobulin and rat alpha 1-microglobulin. RBP contains an internal homology. Thus, residues 36 to 83 display statistically significant homology with residues 96 to 141.

Alpha-Globulins↗
PubMed1985

Amino acid sequence homologies between rabbit, rat, and human serum retinol-binding proteins.

The main transporting protein for vitamin A in rabbit serum, the retinol-binding protein (RBP), was isolated and its amino acid sequence determined. Rabbit RBP was found to be highly homologous to human RBP, whose amino acid sequence was elucidated earlier, and to rat RBP. The rat RBP sequence was obtained by combining information deduced from the nucleotide sequences of two overlapping cDNA clones with the NH2-terminal sequence of the isolated protein determined by automated Edman degradation. The identity between the three proteins is approximately 90%. The high degree of homology between RBP molecules from different species is probably explained by the fact that RBP participates in at least three types of molecular interactions: in the binding of prealbumin, in the interaction with retinol, and in the recognition of a specific cell surface receptor. All these interactions should lead to a conservation of RBP structure. The amino acid differences between rabbit, rat, and human RBP are discussed in light of the recent elucidation of the three-dimensional structure of human RBP. Hybridization of a probe isolated from a rat RBP cDNA clone to restriction enzyme-digested genomic DNA from rat and mouse suggests that RBP is encoded by a single gene.

Amino Acid Sequence↗
PubMed1985

The primary structure of rat liver cellular retinol-binding protein.

The complete amino acid sequence of a cellular retinol-binding protein (CRBP) has been determined for the first time. The primary structure of rat liver CRBP was elucidated by analyses of cyanogen bromide fragments and peptides obtained by tryptic and thermolytic digestions. The single polypeptide chain of rat CRBP consists of 134 amino acid residues. Under reducing conditions, CRBP exists as a monomer, but, in the absence of reducing agents, dimers and multimers of the protein emerge. This is explained by the observation that CRBP contains 3 cysteines, one of which seems to be highly reactive. Whether CRBP contains a disulfide bond is not yet established. The present data extend the previously described homology between CRBP and a family of low molecular weight proteins, all members of which may bind hydrophobic ligands. Since some of these proteins apparently display intracellular transport functions, a similar role for CRBP is envisaged.

Amino Acid Sequence↗
PubMed1984

7S Nerve growth factor alpha and gamma subunits are closely related proteins.

The polypeptide composition and partial amino acid sequence of the 7S nerve growth factor (NGF) alpha subunit have been determined. Residues in 76 unique positions corresponding to 35% of the molecule were identified. The sequence shows that the NGF alpha subunit is closely related to the NGF gamma subunit and thus a member of the same protein family as the serine proteases. This finding is unexpected since the NGF alpha subunit is devoid of detectable protease activity. However, the NGF alpha subunit differs in one important respect from the NGF gamma subunit and related serine proteases. The highly conserved amino-terminal activation cleavage structure, common to most serine proteases, has been deleted, and an uncleaved activation peptide remains attached to the amino terminus of the mature NGF alpha subunit. It is suggested that this feature is causally related to the apparent lack of proteolytic activity.

Amino Acid Sequence↗
PubMed1983

Subcellular localization in normal and vitamin A-deficient rat liver of vitamin A serum transport proteins, albumin, ceruloplasmin and class I major histocompatibility antigens.

The subcellular localization in rat liver cells of retinol-binding protein (RBP), prealbumin, ceruloplasmin, albumin, and class I transplantation antigen chains was investigated by radioimmunoassay determinations. The concentration of RBP was high in the rough and smooth endoplasmic reticulum (SER). The relative concentrations of prealbumin, ceruloplasmin and albumin were similar in the endoplasmic reticulum fractions and in the Golgi fraction. Neither of the proteins were found in significant amounts in the post-microsomal supernatant nor in the plasma membrane. The concentrations of the class I transplantation antigen chains were higher in the Golgi fraction than in the endoplasmic reticulum fractions. In the rough endoplasmic reticulum (RER) fraction ceruloplasmin and the class I antigens partially interact with high-molecular weight (MW) components, presumably membrane-bound glycosyltransferases. RBP, prealbumin and albumin seemed to be present in free form within the microsomal lumen. In vitamin A deficiency the RBP and to a lesser extent the prealbumin concentrations in the endoplasmic reticulum fractions were significantly increased, as compared to fractions from normal livers. This suggests that the presence of vitamin A is a prerequisite for the transport of RBP from the endoplasmic reticulum to the Golgi complex. The intracellular concentrations of albumin and ceruloplasmin were not significantly altered by vitamin A deficiency. In contrast, the amounts of the class I antigen heavy chains were found to be increased.

Animals↗
PubMed1982

Partial amino-acid sequence of the epidermal growth-factor-binding protein.

The partial amino acid sequence of the epidermal growth-factor-binding protein was determined. Residues in 108 unique positions, corresponding to 45% of the molecule, were identified. The protein is a serine protease, closely related to the nerve growth factor gamma subunit. It is suggested that the epidermal growth-factor-binding protein, like other serine protease, is synthesized as a single polypeptide chain which undergoes limited endoproteolysis. The isolated material also contained minor amounts of a second serine protease. This protease is closely related to the epidermal growth-factor-binding protein, differing from it in 7 out of the 45 amino acid positions available for comparison. The latter protease may be identical to the previously described protease A.

Amino Acid Sequence↗
PubMed1980

On the stoichiometry of the interaction between prealbumin and retinol-binding protein.

The stoichiometry of the interaction between prealbumin and retinol-binding protein was investigated. Gel chromatography analyses of prealbumin on columns equilibrated with retinol-binding protein (RBP)-containing buffers and fluorescence polarization analyses of RBP in the presence of various concentrations of prealbumin demonstrated that 3 molecules of RBP could simultaneously bind to prealbumin. Each RBP molecule seemed to interact with prealbumin with an apparent association constant of about 7.8 X 10(6) M-1. Fab fragments of anti-iudiotypic antibodies raised against anti-RBP antibodies reaced specifically with the RBP-binding sites on prealbumin. Two anti-idiotypic Fab fragments could simultaneously interact with prealbumin. These data strongly suggest that prealbumin exhibits at least two RBP-binding sites.

Binding Sites↗
PubMed1980

The retinol-binding protein.

Vitamin A is transported from its storage site in the liver to the epithelial tissues by a carrier protein, the Retinol-binding protein (RBP). In plasma RBP forms a complex with thyroxine-binding prealbumin. The present article reviews available data on the RBP system. The complete primary structure of RBP has been determined. The plasma concentration of RBP is regulated by the vitamin A status so that in vitamin A deficiency RBP molecules are not secreted from the liver. RBP molecules interact with a cell membrane receptor, probably a protein component present on epithelial cells. Vitamin A is thereby delivered to the cells. The uptake of vitamin A by the cells causes a reduction of the affinity of RBP for prealbumin. The RBP molecules which no longer are able to interact efficiently with prealbumin are excreted through the kidney glomerulus and degraded.

Amino Acid Sequence↗