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Biomedical subjects

M K Fagerhol

Publications and source records attributed to M K Fagerhol.

At least 73 records · Page 4Linked to original sources
PubMed1987

Distribution of a formalin-resistant myelomonocytic antigen (L1) in human tissues. II. Normal and aberrant occurrence in various epithelia.

L1 is an approximately 36-kd protein present in virtually all resting peripheral blood neutrophils and monocytes. It is particularly well preserved in formalin-fixed and paraffin-embedded routine material. In a recent immunohistochemical study, the authors showed that L1 has a restricted distribution within the monocyte-derived cell lineage, being mainly confined to reactive histiocytes (infiltrating macrophages). A protein sharing physicochemical and antigenic properties with L1 was identified in extracts of epidermal scales obtained from patients with psoriasis. This epithelial L1 was generally not expressed by normal epidermis, but its production was abundant in several skin diseases. Moreover, mucosal squamous epithelium normally expressed L1. No other epithelia showed signs of L1 production, although occasional patchy uptake was indicated, particularly in kidney tubular epithelium.

Antigens, Surface↗
PubMed1986

Contaminating fibrin in CPD-blood: solubility in plasma and distribution in blood components following separation.

In order to estimate the solubility of contaminating fibrin in CPD-blood, thrombin induced fibrin polymerzation in CPD-plasma was examined by light scattering and fibrinopeptide A (FPA) determinations. In addition, I125 fibrin monomer enriched CPD-blood was used to investigate fibrin monomer retention in blood bags and transfusion filters (170 microns) and fibrin distribution in blood components derived from CPD-blood. Initial fibrin polymerization in CPD-blood occurred after conversion of 15 per cent of the fibrinogen to fibrin, implying that substantial amounts of fibrin may be kept solubilized in CPD-blood bags. Only minor amounts of I125 fibrin monomers were retained in blood bags (2.4 per cent) and in transfusion filters (2.9 per cent) after sham transfusions. After separating I125-fibrin monomer enriched CPD-blood into its constituent components, the major part of fibrin (75.0 per cent) could be traced in the cryoprecipitate.

Adenine↗
PubMed1986

Epidermal and dermal distribution of a myelomonocytic antigen (L1) shared by epithelial cells in various inflammatory skin diseases.

The L1 antigen is a major cytosol component of human granulocytes that may also be expressed by macrophages and epithelial cells. Its epidermal and dermal occurrence was investigated in formalin-fixed routine biopsy material from eleven different inflammatory skin disorders. Localization was performed with a rabbit antiserum to L1 applied in an unlabeled antibody peroxidase-antiperoxidase method. L1 antigen was not found in normal skin except in epithelial cells of pilosebaceous units. However, epidermal L1 antigen was demonstrated in every biopsy specimen from lupus erythematosus, lichen planus, dermatitis herpetiformis, and atopic dermatitis, whereas granuloma annulare test results were usually negative. The occurrence of dermal L1 antigen depended on the composition of the inflammatory infiltrate; specimens rich in neutrophilic granulocytes (e.g., dermatitis herpetiformis) were particularly strongly stained. Extracellular dermal staining was also seen, especially in areas adjacent to accumulation of positive leukocytes. The varying epidermal occurrence of L1 antigen in skin diseases probably signified different degrees of proliferative activity of the epithelial cells and could apparently not be ascribed to uptake from the dermis.

Adolescent↗
PubMed1986

Thrombin generation during collection and storage of blood.

Thrombin generation, as evidenced by radioimmunologic fibrinopeptide A (FPA) determination, was studied upon drawing and storage of blood. Blood from 5 healthy subjects was drawn into Fenwal bags (PL 146, 16-gauge needle, 92-cm collecting tube), and blood samples for FPA analysis were taken from the proximal and distal part of the collecting tubes. The FPA concentrations were considerably higher in the distal part of the tubes both at zero time and after 5 and 10 min, implying substantial thrombin generation to have occurred upon blood passing through the tubes. In 20 healthy blood donors (age 19-52 years) subjected to a standard collection procedure (Fenwal bags PL 146, CPDA formula-1 anticoagulant solution, 450 ml blood), higher FPA values were observed in the bags immediately upon collection, as compared to control venipuncture values (p less than 0.02). Furthermore, in 6 women using oral contraceptives, even larger increases were observed, indicating thrombin generation to be more pronounced in such donors (p less than 0.01). No statistically significant increase in FPA concentrations was found upon storage of CPDA-blood at 4 degrees C for 24 h. There was no correlation between FPA and beta-thromboglobulin (BTG) concentrations after blood collection, indicating alpha-granule release from platelets to be non-thrombin-mediated.

Blood Donors↗
PubMed1986

Tracing the leukocyte marker protein in lung fluids and lung-draining lymph nodes during endotoxemia in sheep.

Infusion of Escherichia coli endotoxin into sheep produces a form of acute lung injury that resembles the adult respiratory distress syndrome (ARDS). A large portion of the physiologic derangements produced by E. coli endotoxin in this model is thought to be granulocyte-dependent. We measured the level of L1, a granulocyte and monocyte marker protein, in various tissues and fluids after infusion of E. coli endotoxin into sheep. In an acute study, sheep received saline or 1.25 microgram/kg E. coli endotoxin dissolved in saline, or endotoxin after hydroxyurea-induced granulocytopenia. L1 was measured by radioimmunoassay in efferent lymph from the caudal mediastinal lymph node collected between 5 and 6 h after infusion. In addition, L1 was visualized in both lung-draining and extrapulmonary lymph nodes by indirect immunofluorescence. In a chronic study, sheep were prepared with lung lymph fistulas, and L1 was measured in draining pulmonary lymph, plasma, and bronchoalveolar lavage (BAL) fluid, serially, over a 24-h period after infusion. Mean L1 level in pulmonary lymph in the acute study was 6 times higher by absolute concentration, and 19 times higher when lymph flow rates were taken into account, in the sheep that received endotoxin than in saline-infused sheep or endotoxin-infused, granulocytopenic sheep. Fluorescence was greater in the outer cortical region adjacent to subcapsular, afferent sinuses of lung draining-lymph nodes of endotoxin-treated sheep than in the comparable nodes of saline-infused sheep and endotoxin-infused granulocytopenic sheep. In endotoxin-treated sheep, extrapulmonary lymph nodes were less reactive than lung-draining nodes.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1985

Distribution of a new myelomonocytic antigen (L1) in human peripheral blood leukocytes. Immunofluorescence and immunoperoxidase staining features in comparison with lysozyme and lactoferrin.

The L1 antigen is a highly immunogenic protein of about 36,500 daltons that can be purified from granulocytes with good yield. Immunocytochemistry with a rabbit anti-serum raised against L1 showed it to be present in the cytoplasm of virtually all resting peripheral neutrophils and monocytes. Moreover, immunofluorescence staining demonstrated variable expression of L1 on the plasma membrane of both these cell types, usually along with lysozyme. This indicated that L1 represents a secretory product like lysozyme as their coexpression on the surface of vital cells was contrasted by the absence of lactoferrin. Cytoplasmic L1 was well preserved by both precipitating and cross-linking fixatives, the latter being preferable to avoid leaching out of antigenic material and to obtain good cellular morphology. Thus, fixation for 3 minutes at room temperature in glutaraldehyde (1%)-formaldehyde (3%) afforded excellent immunoperoxidase staining, particularly when a calcium-containing buffer was used. L1 was not found in eosinophilic granulocytes or in resting B- and T-lymphocytes. Neither did blast transformation of lymphocytes seem to induce L1 expression.

Antigens, Surface↗
PubMed1984

Plasma levels of the leucocyte L1 protein in febrile conditions: relation to aetiology, number of leucocytes in blood, blood sedimentation reaction and C-reactive protein.

Plasma levels of a novel leucocyte protein (L1) were determined in a series of 176 febrile patients and compared with CRP, BLC, and BSR. Among 82 patients with bacterial infection, 81 had L1 levels above the 0.95 interval. Levels of 40 to 130 times the normal mean were seen frequently during life-threatening infections like septicaemia, meningitis, or pneumonia. In contrast, 23 of 27 patients with viral infections had normal L1 levels. A poor correlation was found between L1 levels, CRP, BLC, and BSR, suggesting that these parameters reflect different aspects of the response to tissue damage and inflammation. L1 and CRP seem equal in distinguishing between bacterial and viral infections. Low or normal L1 levels argue strongly against a bacterial infection, while elevated L1 levels discriminate poorly between bacterial and non-infectious inflammatory or malignant diseases.

Adolescent↗
PubMed1984

Relationship of neutrophil cytoplasmic protein (L1) to acute and chronic lung disease.

L1 protein is a neutrophil cytoplasmic protein and its measurement in body fluids probably reflects neutrophil turnover. The serum range in normal subjects is wide (60-5700 microgram/l) with a median value of 547 microgram/l but lower (2P less than 0.01) than in patients with chronic obstructive bronchitis (median, 750; range, 99-500 microgram/l). Patients with "emphysema" do not have increased serum L1 protein concentrations. On the other hand patients with a variety of active lung diseases have raised concentrations compared to normal subjects suggesting that L1 protein is a marker of inflammation within the lung. The secretion concentration of L1 protein reflects its purulent nature and rapid falls in both serum and secretion L1 concentration occur with treatment. The results suggest that sequential L1 measurements may provide a measure of the inflammatory state of the lung and a rapid indication of the response to treatment.

Adult↗
PubMed1983

Quantitation of a highly immunogenic leukocyte antigen (L1) by radioimmunoassay: methodological evaluation.

This paper describes a radioimmunoassay (RIA) for the quantitation of a major protein antigen (L1) released from human granulocytes. A protein A-carrying strain of Staphylococcus aureus was used as a solid phase IgG-binding reagent for the separation of antigen-antibody complexes from free antigen in the assay. A two-step version of the RIA may be completed in 2.5 h and has a detection limit of about 5 ng/ml. The sensitivity may be increased by minor modifications. A single step version takes 1.5 h and has adequate sensitivity to cover clinically important plasma levels. Selection and optimal use of reagents for the two-step procedure is described and their storage discussed. The simplicity of the procedure combined with high sensitivity and satisfactory accuracy, precision and reproducibility makes this assay suitable for quantitation of L1 in various body fluids.

Animals↗
PubMed1983

Purification and partial characterization of a highly immunogenic human leukocyte protein, the L1 antigen.

L1 is a major and highly immunogenic protein component of human granulocytes. It was purified from random samples of blood-donor leukocytes. An antiserum to L1 was initially raised in rabbits by immunization with protein fractions from preparative agarose gel electrophoresis. The main problem in purifying L1 was its poor stability when carried through multiple steps. Preparative isoelectric focussing was therefore adopted as an efficient one-step method. The isoelectric focussing pattern of L1 was greatly influence by the presence of EDTA or calcium ions in the sample buffer. With low EDTA concentrations or calcium excess, L1 focussed as seven protein bands in two regions, pH 6.1-6.5 and pH 7.6-8.4. Conversely, L1 was found only in the pH-6.1-6.5 region when excess EDTA was added to the sample. Irrespective of conditions, the bulk of L1 focussed at pH 6.3 and pH 6.5. Also the electrophoretic mobility of L1 was strongly influenced by calcium ions, suggesting uptake of calcium by the protein. In the presence of calcium, L1 adhered to glass surfaces and filters used for concentration of protein solutions. The latter problem could be prevented by addition of EDTA. The molecular mass of L1 was determined to be about 36.5 kDa. The molecule was shown to consist of three non-covalently linked 12.5-kDa subunits.

Animals↗
PubMed1983

Severe toxic reaction to tinidazole.

A physician aged 44 years participated as a volunteer in pharmacokinetic studies with tinidazole (FASIGYN, Pfizer). He received 1600 mg of the drug as an intravenous infusion over 80 min. Shortly afterwards, he fainted and was unconscious for about 10 s. The attack was followed by low blood pressure, nausea and tiredness for several h. The serum concentration of tinidazole was 35.4 mg/l when the attack started. Blood tests showed a normal immunoglobulin E level, and a transient fall in the concentration of complement factor C3 after the infusion. It is concluded that tinidazole caused an acute toxic reaction with subsequent activation of complement factors.

Adult↗
PubMed1980

PiZpratt: a new alpha 1-antitrypsin allele in an American Negro family.

A rare alpha 1-antitrypsin phenotype was detected in serum of individuals belonging to three generations of an American Negro family. Following the recommended guidelines of nomenclature, we labeled the new Pi type Zpratt; the corresponding allele is PiZpratt. Alpha 1-antitrypsin concentration and trypsin inhibitory capacity are normal in MZpratt serum.

Adult↗