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Biomedical subjects

A Linde

Publications and source records attributed to A Linde.

At least 253 records · Page 14Linked to original sources
PubMed1984

"On-off" phenomenon in Parkinson's disease: correlation to the concentration of dopa in plasma.

To investigate the relation between "on-off" fluctuations in symptomatology and bioavailability of dopa in patients with Parkinson's disease, five Parkinsonian patients with pronounced "on-off" symptoms were studied. Continuously during the study the degree of disability in the patients was registered. Every one hour, and in addition, whenever there was a change from "on" to "off" or vice versa, a blood sample was collected for dopa determination. Since dopa is transported from plasma into the brain by a saturable carrier for which it has to compete with endogenous large neutral amino acids (LNAA), the concentrations of these competitors were measured too. In four of the patients there were considerable oscillations in the plasma dopa concentration during the day; in one of these patients the highest value was as much as 12 times higher than the lowest value. These dramatic fluctuations in the absolute concentration of dopa in plasma had a major influence on the relative dopa concentrations (calculated as the ratio dopa/sum of LNAA) as the fluctuations in the concentrations of LNAA in plasma were much less pronounced. Consequently, the absolute and the relative concentrations of dopa in plasma were highly parallelled. In four of the five patients "on"-periods began within one hour after a peak in the concentration of dopa in plasma and in the fifth patient five out of seven "on"-periods were preceded by a rise in plasma dopa concentration within the same time interval. From the present data it could be concluded that the "on-off" phenomenon in Parkinson's disease, at least partly, is due to oscillations in the concentration of dopa in plasma. A reduction in the variations of the concentration of dopa in plasma seems to be necessary to overcome the "on-off" problem. The introduction of a slow release preparation of dopa is therefore urgently warranted. The concentration of LNAA in plasma must, however, also be considered in this context.

Aged↗
PubMed1984

Ultrastructural localization of fibronectin in duct cells of human minor salivary glands and its immunochemical detection in minor salivary gland secretion.

Fibronectin (Fn) was localized in duct cells by means of a light and electron microscopic immunohistochemical technique. The subcellular localization demonstrated that Fn is synthesized in these cells and thus not exclusively produced by cells with a mesodermal background. Fn concentration, as measured by radioimmunoassay, was higher in saliva from the minor salivary glands than in unstimulated whole saliva, whereas Fn was undetectable in stimulated parotid saliva. Fn is thus a conspicuous component in unstimulated resting saliva. Fn may be an important factor, negative or positive, for the integrity of the oral hard and soft tissues because it has the capability to bind and agglutinate microorganisms.

Fibronectins↗
PubMed1984

Transfer and persistence of viral antibody-producing cells in bone marrow transplantation.

Antiviral humoral reactivity was studied after bone marrow transplantation. Antiviral IgG--reflecting the presence of functional B cells--was found for a substantial period after transplantation. However, most patients unexpectedly stopped producing antibody after an extended period of observation (i.e., for more than three months and up to as long as 12 months). This cessation was noted whether the viral reactivity involved was of donor or recipient origin. The transferred viral antibody-producing cells thus usually persisted for only a moderate length of time and seemed to have a finite life span. The findings indicate that donor and recipient memory cells are susceptible to the conditioning regimen or to the treatment that follows transplantation. In a few cases transferred immunity of long duration was seen; this finding indicated the occasional engraftment of memory cells.

Antibodies, Viral↗
PubMed1984

IgG-subclass-specific CMV reactivity in bone marrow transplant recipients.

IgG subclasses of cytomegalovirus (CMV) antiviral antibodies were determined in 37 donor-recipient pairs of bone marrow transplants (BMT). Bone marrow transplant recipients, like healthy persons, have a restricted immune reactivity, producing mainly two types of anti-CMV IgG: IgG1 and IgG3. Passively transfused specific antibody subclasses were readily measurable. Take of the transplant could be detected from the production of subclass IgG antiviral antibody 1-3 months after BMT of seronegative recipients with marrow from seropositive donors. Patients with protracted CMV infections or other severe diseases initially also produced CMV IgG1 and IgG3, but anti-CMV subclass titers then decreased. In severe disease, CMV was isolated from blood cells as well as from urine. In moderate infections, in which the patients recovered, CMV was isolated from urine but usually not from blood, and a strong and durable antiviral subclass response was measured.

Anemia, Aplastic↗
PubMed1984

Virus-specific immunoglobulin G subclasses in herpes simplex and varicella-zoster virus infections.

The subclass specificities of antiviral immunoglobulin G (IgG) produced in response to herpes simplex and varicella-zoster virus infections were investigated. IgG1 and IgG3 with anti-herpes simplex virus activity were seen in patients with primary and reactivated disease, as well as in healthy seropositive subjects and in immunoglobulin preparations. IgG4 was occasionally seen alone or together with IgG1 and IgG3 in patients. In varicella, IgG3-specific antiviral antibodies were predominant, whereas in zoster, IgG1 was the dominant subclass.

Antibodies, Monoclonal↗
PubMed1984

Dental fear and avoidance: a comparison of two modes of treatment.

Ninety-nine individuals, all of whom had long avoided dental treatment due to severe dental fear, received therapy according to one of two treatment modalities--behavioral therapy from a psychologist (BT) and treatment under general anesthesia (GA)--both of which were followed by clinical training and dental test treatments. These treatment programs were followed by referring the individuals to community dental clinics for complete oral rehabilitation. Among BT patients, significantly more (92%) completed the treatment program, compared with the GA patients (69%). Complete oral rehabilitation in community dental clinics was achieved by 78 and 53%, respectively. BT patients also had a significantly lower frequency of cancellations. The reduction in dental anxiety according to the Corah Dental Anxiety Scale was substantial in both groups, but the anxiety was significantly more reduced for BT patients, who reached a level equivalent to that of average dental patients. Patients' self-reported tension and the dentists' ratings of patient behavior during treatment were also significantly more positive for the BT groups.

Adult↗
PubMed1983

Non-collagenous proteins of predentine from dentinogenically active bovine teeth.

Predentin(e) was dissected out from unerupted permanent bovine teeth. The non-collagenous proteins were extracted at -13 degrees C by 4 M-guanidinium chloride containing proteinase inhibitors and separated by DEAE-Sepharose and Sephadex G-100 chromatography. In addition to a few minor constituents, the only major non-collagenous components that could be demonstrated were albumin and proteoglycan. The localization of the former, demonstrated by optical-microscopical immunochemistry, was such that it was concluded that albumin is not a constituent of predentin matrix. Very low amounts of phosphoprotein were found in predentin matrix. This was of two types, high- and low-phosphorylated. Larger amounts of phosphoprotein were not present until the dissection was carried deeper into newly formed dentin(e). On the basis of the present results and previously obtained morphological data the conclusion was drawn that predentin matrix, containing virtually only collagen type I and proteoglycan, is similar in composition to that of loose connective tissue and primarily aimed at the production and maturation of collagen fibres. Only immediately before the mineralization front are the non-collagenous protein components secreted that initiate and govern calcium-phosphate mineral formation.

Amino Acids↗
PubMed1983

Noncollagenous proteins of rat compact bone.

In order to obtain a comprehensive overview of the noncollagenous proteins (NCPs) of bone matrix, the NCPs were extracted from rat compact bone and fractionated using methods aiming to prevent artifactual degradation and losses of protein. The NCP content of rat bone was found to be similar to that of rat dentin in several respects but different in others. The soluble NCPs of bone fell into four categories: acidic glycoproteins, gamma-carboxyglutamate-containing proteins, phosphoproteins, and proteoglycans. With the exception of the gamma-carboxyglutamate-containing proteins, the majority of NCPs had apparent molecular weights exceeding 50,000. As in rat dentin, several gamma-carboxyglutamate-containing proteins could be demonstrated in rat bone. Earlier studies have only taken one molecular species into consideration. No highly phosphorylated phosphoprotein could be demonstrated in bone. However, at least two phosphoproteins with a low degree of phosphorylation were found to be present. No plasma proteins could be demonstrated in any of the chromatographic fractions from the EDTA extracted NCPs by means of double diffusion. The NCPs, remaining firmly associated with the collagenous matrix after thorough demineralization and extraction, were analyzed after CNBr and collagenase degradation of the matrix. Much smaller amounts of phosphoprotein were recovered after CNBr digestion than reported earlier. Collagenase digestion released small amounts of acidic glycoprotein, phosphoprotein, and proteoglycan. The results give additional evidence that this small remainder might be explained, not by any covalent linkage to collagen, but by an inefficient extraction.

Amino Acids↗
PubMed1983

Multiple forms of rat dentin phosphoproteins.

Previous studies have shown that the phosphoprotein from rat dentin is heterogenous and can be partially separated into two fractions by ion-exchange chromatography. These proteins were further characterized by polyacrylamide gel electrophoresis, gel chromatography, and amino acid and phosphate analysis, after chromatographic separations on ion-exchange columns. On 5-15% gradient gels, the phosphoproteins extracted from rat dentin and precipitated by CaCl2 gave three Alcian blue-staining bands with apparent molecular weights in the 90-95,000 range. The two slower-moving bands corresponded to highly phosphorylated proteins (HP) that had phosphoserine contents of greater than 400 residues per thousand and contained little or no valine, leucine, phenylalanine, or arginine. The faster-moving band corresponded to a moderately phosphorylated protein that contained about 250 residues per thousand of phosphoserine and greater quantities of glutamic acid, proline, and several other amino acids than HP. The nature of the phosphoproteins in HP was further studied after total removal of the phosphate with an insoluble form of bovine intestinal alkaline phosphatase. The dephosphorylated product (dP-HP) gave a single major band on gel electrophoresis but showed evidence for two closely related NH2-terminal sequences, Asp-Asp-Asp-Asn and Asp-Asp-Pro-Asn. The dephosphorylated material was separated into two components (dP-HP1 and dP-HP2) by chromatography on QAE-Sephadex A-25. The amino acid compositions of the two components showed that they differed in their primary structures. This conclusion was verified by the finding of the proline-containing sequence in dP-HP2. In addition to these two groups of phosphoproteins, a third class, LP, contains low levels of phosphoserine and high amounts of glutamic acid (W.T. Butler, M. Bhown, M.T. DiMuzio, and A. Linde, (1981) Coll. Res. 1, 187-199).

Amino Acids↗
PubMed1983

Fibrinogenolytic and fibrinolytic activity in oral microorganisms.

Samples were taken from blood accumulated in dental alveoli after surgical removal of mandibular third molars, from subgingival plaque of teeth with advanced periodontal destructions, from teeth with infected necrotic pulps, and from subjects suffering from angular cheilitis. Of the microorganisms subcultured from these samples, 116 strains were assayed for enzymes degrading fibrinogen and fibrin. Enzymes degrading fibrinogen were assayed with the thin-layer enzyme assay cultivation technique. This assay involves the cultivation of microorganisms on culture agars applied over fibrinogen-coated polystyrene surfaces. Enzymes degrading fibrin were assayed with both a plate assay and a tube assay, in which fibrin was mixed with a microbial culture medium. Microorganisms degrading fibrinogen or fibrin or both were isolated from all sampling sites. Activity was mainly detected in strains of Actinomyces, Bacteroides, Fusobacterium, Peptococcus, Propionibacterium, and Staphylococcus aureus. Most Fusobacterium strains degraded fibrinogen only. Enzymes degrading fibrinogen as well as enzymes degrading fibrin via activation of plasminogen were revealed in strains of Clostridium, S. aureus, and Streptococcus pyogenes. It was generally found that fibrinogen was degraded by more strains than was fibrin, which indicates that different proteases may be involved.

Bacteria↗
PubMed1983

An epidemiological survey of nephropathia epidemica in Sweden.

The indirect immunofluorescence test (IFT) using the Hantaan virus (agent of Korean hemorrhagic fever, KHF) was applied for detection of antibodies to nephropathia epidemica (NE). From 103 patients with symptoms suggesting NE, 61% revealed KHF/NE antibodies in the convalescent sera. All seropositive patients seemed to have acquired their disease in NE endemic areas (north of the 60th parallel). Only patients found to have a typical clinical NE (fever, abdominal pain and renal engagement) were seropositive. Antibodies to KHF/NE were found in 4.2% of sera from 647 healthy persons living in NE endemic areas. Signs of local clusters were found. Subclinical or mild disease seems common. Proof of man to man spread of the disease was not found. Sera from 355 persons living outside NE endemic areas were also tested and 2.4% contained KHF/NE antibodies.

Adolescent↗
PubMed1982

Disagreement in molecular weight determinations of dentin phosphoprotein.

The molecular weight of highly phosphorylated phosphoprotein from rat incisor dentin was estimated by three different methods: sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis, gel chromatography in 6 M guanidinium chloride (GdnHCl) and analytical ultracentrifugation at high salt concentration. SDS-polyacrylamide gel electrophoresis revealed an abnormal migration of the phosphoprotein and its enzymatically dephosphorylated derivative in comparison to standard proteins. Depending on the acrylamide concentration in the gel (7.5-20%), the apparent molecular weight of the phosphoprotein varied from 90,000 to 27,000. Similar results were obtained for the dephosphorylated protein. In gel chromatography using 6 M GdnHCl as eluent the phosphoprotein had an elution volume corresponding to that of a standard protein with a molecular weight of 67,000, while the enzymatically dephosphorylated phosphoprotein showed an apparent molecular weight of 30,000. The phosphoprotein behaved non-ideally in equilibrium sedimentation runs. The apparent molecular weight was strongly concentration-dependent and the extrapolation to zero concentration was uncertain. However, after enzymatic dephosphorylation the concentration dependence disappeared and a molecular weight of 28,000 could be calculated. Since the phosphate groups represent 26% of the phosphoprotein by weight, the true molecular weight of the highly phosphorylated phosphoprotein components from rat incisor dentin should be 38,000. The study shows that it is not possible directly to estimate the molecular weight of this type of protein by standard methods elaborated for normal globular proteins.

Animals↗
PubMed1982

Evidence for several gamma-carboxyglutamic acid-containing proteins in dentin.

With anion-exchange chromatography, the gamma-carboxyglutamic acid (Gla)-containing proteins of rat dentin were separated into four closely related fractions (gamma 1-gamma 4). Edman degradation of gamma 2 gave two NH2-terminal sequences with a minor sequence beginning five residues shorter than the major one. Gel electrophoresis of gamma 2 yielded one major and one minor protein band. Fraction gamma 3 gave one band on gel electrophoresis and a single NH2-terminal sequence. The composition of gamma 4 suggested that, compared to gamma 2 and gamma 3, a portion of the COOH-terminal was missing. Thus some of the heterogeneity of rat dentin Gla-containing proteins can be explained by shortened ends.

1-Carboxyglutamic Acid↗
PubMed1982

Immunofluorescent localization of fibronectin in human oral mucosa.

Fibronectin (FN) with an immunohistochemical fluorescence technique using anti-human FN and anti-rat FN sera was localized in the basement membrane of lip, buccal mucosa, palate, tongue, around ectopic sebaceous glands and around acini and ducts of labial salivary glands though in different amounts. In the mucosal lamina propria, FN was present in a net-like pattern. The highest concentrations of FN were in the palatal and tongue connective tissues. Much FN was present in the walls of small blood vessels and in perineural sheaths of peripheral nerves. No fluorescence was seen in the acini of labial salivary glands. In their striated ducts however, some cells were intensely fluorescent; the significance of this is unknown.

Basement Membrane↗
PubMed1982

Localization of fibronectin during dentinogenesis in rat incisor.

Fibronectin (FN) was localized in the dental pulp and predentine at different stages of dentinogenesis by indirect immunofluorescence. Fibronectin was present in the basement membrane between the inner enamel epithelium and the underlying dental mesenchyme and also in mantle predentine. Fibronectin was absent from predentine during further (circumpulpal) dentine formation, indicating that the FN molecule is not directly involved in mineralization. The findings emphasize the difference between the mantle and circumpulpal dentine formation. Fibronectin was localized in the odontoblast layer at the level where the cell processes leave the cell bodies and where the odontoblasts adhere to each other by junctional complexes.

Animals↗