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Biomedical subjects

L Tejler

Publications and source records attributed to L Tejler.

At least 19 recordsLinked to original sources
PubMed2001

[The Malmo model for private and public rheumatological outpatient care. Cooperation makes it possible to introduce disease modifying treatment quickly].

The Malmö model represents a close collaboration between private practitioners who receive public financing and hospital-based rheumatological clinics. A comparison of these two types of out-patient care was undertaken by questionnaire in 1997 (70% response rate). Of the total patient cohort in the study, 73% were seen by private rheumatologists. The evaluation showed very similar outcomes, regardless of drug treatment employed or professional personnel involved (i.e., a physician or other members of the rheumatological team). Minor differences concerned easier accessibility to physicians in private practice, and the large proportion of immigrants seen at the hospital clinic. The results of the study confirmed the similarity of care provided in both types of out-patient clinics. Improved pharmacological products for suppressing inflammation will lead to increasing demands on out-patient rheumatological care. The model described illustrates a method of meeting those demands.

Adult↗
PubMed1991

Social network, social support and acute chest complaints among young and middle-aged patients in an emergency department--a case-control study.

The risk of developing non-specific chest complaints was higher among young and middle-aged persons with a weak social network and low social support, when comparing cases with controls at a hospital emergency department (ED). The study was comprised of 62 cases; two different control groups were recruited from other patients at the medical ED (n = 67) and from patients at the surgical ED with urolithiasis or cholecystitis (n = 31). Relative risks for non-specific chest complaints were 2.3-3.4 for patients with a low score on two of the social network factors (an overall index and social anchorage) and two social support factors (emotional esteem support and support by a confidant). These results could be used for developing guidelines for a more adequate clinical management of these patients, as well as for the prevention of stress-related conditions in general. An analysis was made of the conceptual validity of the instrument used for assessing social network and social support. It was concluded that structural elements, such as social network factors, represented a more valid measurement that was less affected by subjectivity. Future research is of importance for finding overbridging concepts, rather than to further continue the dissection of presently used indices into even more 'specific' variables.

Adaptation, Psychological↗
PubMed1985

Growth stimulating activity from lysed cultured arterial smooth muscle cells and skin fibroblasts.

Rabbit and bovine arterial smooth muscle cells (SMC) and human skin fibroblasts were lysed by freezing and thawing in the presence of protease inhibitors (PI). The supernatant was assayed for growth stimulating activity (GSA), and it stimulated the growth of SMC and fibroblasts, but not human and bovine endothelial cells. GSA was sensitive to heat and trypsin treatment, stimulated DNA synthesis after a lag time of 12-15 hours, and exhibited marked size and charge heterogeneity when subjected to gel chromatographies. GSA differed from many other known growth factors, mainly platelet derived growth factor (PDGF), through the behavior on ion exchange chromatography, the heat sensitivity and the lack of decline in activity in the presence of anti PDGF antibodies. The data suggests that several growth stimulating proteins can be obtained through the lysis of SMC or fibroblasts with possible implications for atherosclerosis and wound healing.

Animals↗
PubMed1983

Isolation of human complex-forming glycoprotein, heterogeneous in charge (protein HC), and its IgA complex from plasma. Physiochemical and immunochemical properties, normal plasma concentration.

Human complex-forming glycoprotein, heterogeneous in charge (protein HC) has previously been isolated from urine and immunochemically shown to be present in low and high molecular weight forms in blood plasma (Tejler, L., and Grubb, A. O. (1976) Biochim. Biophys. Acta 439, 82-94). In the present work, the major low and high molecular weight forms of the protein were isolated from plasma by immunosorption followed by gel chromatography. The plasma low molecular weight protein HC and the urinary protein had similar, if not identical, molecular weight, amino acid composition, NH2-terminal and carboxyl-terminal amino acid sequences and electrophoretic mobility. The low molecular weight plasma protein HC carried a yellow chromophore like the urinary protein, but its molar extinction coefficient at 280 nm was lower and its charge heterogeneity less pronounced than that of urinary protein HC. The plasma high molecular weight protein HC had a hydrodynamic volume which was greater than that of monomeric IgA but smaller than that of dimeric IgA. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the isolated high molecular weight protein followed by electrophoretic blotting and immunochemical analysis demonstrated that the protein contained four polypeptide chains: two light immunoglobulin chains (Mr = 23,000), one IgA alpha-chain (Mr = 54,000), and one chain with Mr approximately 90,000 which carried both alpha-chain and protein HC antigenic determinants. Whether the protein HC X IgA complex is a functionally significant part of the humoral immune system cannot be decided without further experimentation, but the complex was found to be completely absent from the blood plasma of patients with a selective deficiency of IgA-secreting immunocytes. The isolated low and high molecular weight plasma protein HC components were used as standard proteins in the construction of a quantitative crossed immunoelectrophoretic assay for the simultaneous quantitation of the two major protein HC components in blood plasma. The plasma concentrations of the low and high molecular weight protein HC components were measured by this method in 13 healthy Caucasians. The results for the low molecular weight protein HC were: mean, 20.3 mg/liter, S.D., 3.2 mg/liter, range, 13.6-26.0 mg/liter; and for the protein HC X IgA complex: mean, 293 mg/liter, S.D., 176 mg/liter, range, 36-620 mg/liter.

Adult↗
PubMed1981

Proteinuria following nephroangiography. IX. Chemical and morphological analysis in dogs.

Following unilateral selective nephroangiography with diatrizoate, changes in urinary concentrations of prealbumin, albumin, IgG and alpha 2-macroglobulin were analysed in 8 dogs. All reacted with increased proteinuria. The median increase of urinary albumin concentration was 1,300 times (range 27-3 500). The proteinuria was caused mainly by increased glomerular permeability exhibiting some molecular size selectivity in filtration of the proteins measured. Light and electron microscopy did not reveal any glomerular on tubular abnormalities which could be attributed to effects of the angiography. It is suggested that the increased glomerular permeability to proteins might be an effect of disturbance of the electrical hindrance in the glomerular capillary wall.

Albuminuria↗
PubMed1980

Proteinuria following nephroangiography. V. Influence of calcium and magnesium ions in non-ionic contrast media.

The influence on albuminuria following nephroangiography was investigated after addition of Ca2+ to the non-ionic contrast medium metrizamide (Amipaque) in the rat and after addition of Ca2+ or Ca2+ and Mg2+ to the experimental non-ionic contrast medium C 29 in the dog. When Ca2+ or CA2+ and Mg2+ were added to metrizamide or C29 in concentrations two to three times th plasma level no influence occurred. Higher concentrations of Ca2+ (10-25 mmol/l) in the metrizamide or C29 solutions resulted in increased albuminuria.

Albuminuria↗
PubMed1978

Production of protein HC by human fetal liver explants.

Human fetal lever explants were found to secrete protein HC into the medium in molar amounts comparable to those of albumin, alpha 1-antitrypsin and orosomucoid. Incorporation of a radioactive amino acid from the medium into the secreted protein HC demonstrated de novo synthesis. The secreted protein HC had the same size and electrophoretic mobility as protein HC of plasma and urine and gave a reaction of immunochemical identity with the protein in these biological fluids.

Alpha-Globulins↗
PubMed1978

Proteinuria following nephroangiography. III. Role of osmolality and concentration of contrast medium in renal arteries in dogs.

Nephroangiography in dogs, with renal artery injections of Urografin 76%, resulted in massive albuminuria. Unilateral nephroangiography causes massive albuminuria only from the injected kidney. Significantly less albuminuria was caused by renal artery injections of a corresponding volume of a sodium chloride solution of equal osmolality or intravenous injections of twice that volume of Urografin 76%. Thus, the hypertonicity of the contrast medium is not the main cause of the albuminuria. The degree of albuminuria is related to the concentration of medium in the renal arteries and not to the amount excreted.

Albuminuria↗
PubMed1978

Proteinuria following nephroangiography. II. Influence of contrast medium and catheterization in dogs.

Major increases of urinary albumin were common following nephroangiography in dogs using Urografin (diatrizoate) or Isopaque Cerebral (metrizoate) as contrast medium. Neither the catheterization procedure nor the injection of a supposed inert solution resulted in significant albuminuria but following injection of contrast medium albuminuria commenced within a few minutes; normalization occurred within 2 days. Higher doses of contrast medium induced massive albuminuria than lower ones.

Albuminuria↗
PubMed1977

Proteinuria following nephroangiography. I. Clinical experiences.

Following nephroangiography with an ionic contrast medium (metrizoate) proteinuria occurred in 25 of 28 patients, reaching its maximum with 1/2 to 24 hours. It fell to preangiographic values within 6 days. The degree of proteinuria varied but was massive, i.e. more than 10 g albumin/g creatinine, in 9 patients. The underlying mechanism is a marked, reversible increase in glomerular permeability.

Adult↗
PubMed1977

Expression of protein HC on the plasma membrane of different human cell types.

The surface expression of a recently described plasma glycoprotein called human complex-forming glycoprotein, hetergeneous in charge (protein HC) on a number of different human cell types was investigated. By means of direct and indirect immunofluorescence, protein HC was shown to be associated with the surface of virtually all cells of the investigated normal cell types including erythrocytes, peripheral blood B and T lymphocytes, and the human fibroblast lines HE 81, HE 31, and WI 38. When transformed and malignant cell populations were studied, it was found that some populations (e.g., the T cell line Molt-4) carried protein HC on the surfaces of very few cells, whereas other cell populations (e.g., chronic lymphocytic leukemia lymphocytes) carried the protein on most cells. Malignant cell populations with intermediary percentages of protein HC-positive cells were also found. Protein HC on the cell surface of normal peripheral blood lymphocytes could be redistributed by incubation of the cells with anti-protein HC-antiserum at 37 degrees C, and this reaction could be inhibited by sodium azide.

Animals↗
PubMed1977

Proteinuria following renal arteriography. Report of two cases.

Two patients reacting with transitory, massive proteinuria after diagnostic renal arteriography with a commonly used non-ionic contrast medium, metrizoate, are described. One of them developed temporary renal failure; the concentration of urinary albumin reached 330 g/g creatinine. It is suggested that intratubular precipitation of proteins, obstructing urinary flow, might be one factor in the development of her renal failure.

Acute Kidney Injury↗
PubMed1976

A complex-forming glycoprotein heterogeneous in charge and present in human plasma, urine, and cerebrospinal fluid.

A glycoprotein from the urine of one healthy individual was purified by ultrafiltration, ion-exchange chromatography, gel chromatography and immunosorption. The protein contained only one polypeptide chain with an approximate molecular weight of 31 000 and was associated with a brown colour which did not disappear even after total reduction and alkylation of the protein followed by dialysis in 6 M guanidine hydrochloride. The protein appeared homogeneous on sodium dodecyl sulphate-polyacrylamide electrophoresis and gel chromatography. It had only one N-terminal amino acid sequence, Gly-Pro, and gave only one precipitate with a polyvalent antiserum but was found to be very heterorgeneous on agarose gel electrophoresis and on isoelectric focusing. Desialylation of the protein failed to alter this heterogeneity. An electroimmunoassay system was designed to measure the amount of the protein in normal human plasma, urine, and cerebrospinal fluid where the mean concentrations were found to be about 100, 10 and 0.3 mg/l, respectively. The protein was found to occur in normal plasma and urine as free monomers and dimers and as complexes with IgA and albumin.

Amino Acid Sequence↗
PubMed1976

Immunofluorescent demonstration of the presence of protein HC on the surface of human lymphocytes.

Indirect immunofluorescence was used to demonstrate the presence of protein HC on the surface of a large percentage of normal human peripheral blood lymphocytes. Protein HC is a recently described charge heterogeneous, complex-forming glycoprotein normally present in human plasma, urine and cerebrospinal fluid. The synthesis of protein HC by lymphocytes was indicated by the removal of the glycoprotein from the cell surfaces on trypsinization of the cells followed by the reappearance of the protein on continued cultivation of the cells.

Cell Membrane↗