Biomedical subjects

V Hukkanen

Publications and source records attributed to V Hukkanen.

42 records · Page 3Linked to original sources

PubMed1985

Detection of Chlamydia trachomatis in clinical specimens by nucleic acid spot hybridization.

A nucleic acid spot hybridization assay was used to detect Chlamydia trachomatis DNA. The hybridization probes included DNA isolated from elementary bodies of lymphogranuloma venereum (LGV) strains and cloned fragments of both chromosomal and plasmid DNA. The sensitivity of the test was in the range 10 to 100 pg homologous DNA and 10 in vitro infected cells. Cross-reactivity with bacterial DNA was avoided when purified chlamydia-specific DNA fragments were used as probes. C. trachomatis was detectable in most of the clinical specimens with large amounts of infectious particles. Also some isolation-negative specimens gave a positive signal in the test.

Chlamydia trachomatis↗

PubMed1983

Antibodies in cerebrospinal fluid to white matter glycoproteins in multiple sclerosis patients.

Cerebrospinal fluid (CSF) specimens from 45 patients with multiple sclerosis (MS) and 45 age- and sex-matched controls with other neurological diseases (OND) were tested for antibodies to white matter (WM) membrane glycoprotein (GP) fractions prepared from MS and control WM membranes by lentil lectin chromatography. The binding of the CSF IgG to the 125I-labeled GP fractions was determined by immunoprecipitation using Protein A-Sepharose. CSF from patients with MS bound highly significantly more strongly to the GP fraction prepared from MS WM than did the OND CSF specimens (P less than 0.001). There was no such difference when control GP fraction was used as an antigen. No highly significant differences were observed when 20 paired serum specimens were tested. Electrophoresis of the immunoprecipitates showed that components with molecular weights (MWs) of 157,300, 135,600, 111,100, 93,000, 75,700, 63,300, 50,100, 24,300, 20,300 and 17,000 daltons were precipitated from the MS GP fraction by CSF specimens of both MS and OND groups, whereas components with MWs of 50,100, 24,300, 20,300 and 17,000 daltons were precipitated from the control GP fraction.

Adult↗

PubMed1983

Characterization of immune complexes in multiple sclerosis by an antigen-specific immune complex radioimmunoassay.

Serum and cerebrospinal fluid samples from multiple sclerosis (MS) patients containing various levels of Clq-reactive immune complexes (IC) and samples from age- and sex-matched controls were tested by an antigen-specific IC radioimmunoassay which detects IC containing myelin membrane-related antigens. Positive reactivity in the assay was significantly associated with IC-containing MS sera (P less than 0.005) but such an association was not observed with MS cerebrospinal fluid. Analysis of longitudinal specimens revealed that the levels of the antigen-specific serum IC fluctuated with time. Significant correlation between serum levels of Clq-reactive IC and serum levels of IC containing myelin membrane-related antigens was observed (r = 0.62; P less than 0.001). Sucrose gradient centrifugation of sera from 1 patient showed that the IC had a peak density of 1.075 g/ml, indicating the presence of lipid material. The results suggest that serum IC of MS patients frequently contain myelin membrane-related antigens and that these antigens may be lipids or lipid-associated.

Antigen-Antibody Complex↗

PubMed1982

Membrane protein antigens in multiple sclerosis.

Rabbits were immunized with white matter (WM) membrane fractions isolated from autopsy brain specimens of three patients with multiple sclerosis (MS), and three controls. All the rabbits developed high serum antibody titers to the MS and control WM fractions, as tested by enzyme immunoassay. Antibodies against WM membrane components were analyzed further by immunoprecipitation of radio-labeled WM proteins and subsequent polyacrylamide gradient gel electrophoresis. Antigenic membrane components with molecular weights of 138 000, 111 000, 86 500, 79 600, 69 000, 63 000, 58 000, 53 400, 45 700, 24 500 and 22 300 were found in both MS and control WM. Although there may have been some quantitative differences in these immunogenic proteins of MS and normal WM, no multiple sclerosis-specific membrane antigen could be demonstrated. The hyperimmune anti-WM sera did not precipitate 35S-labeled polypeptides from cells infected with herpes simplex type 1, adeno type 5, measles, mumps, rubella, respiratory syncytial, parainfluenza type 2 or cytomegaloviruses, which suggests that the MS brain WM membrane proteins do not share common antigenic determinants with the viral polypeptides.

Antigens↗

PubMed1982

Lectin-reactive components in white matter membranes from normal and multiple sclerosis brains.

Polypeptides derived from human white matter membranes reacted with the radioiodinated lectins concanavalin A, Lens culinaris phytohemagglutinin, Ricinus communis agglutinin and wheat germ agglutinin after electrophoresis in polyacrylamide pore gradient gels. The molecular weights of these lectin-reactive bands were estimated by comparison with radioiodinated protein standards by using the linear relationship between log of the molecular weight and log of the gel concentration reached by the protein after electrophoresis in a polyacrylamide gradient gel. The molecular weight estimates for components reactive with concanavalin A were 176,800, 141,200, 72,800, 52,800, 44,700, 40,000, 24,800 and 23,900. The molecular weights of the bands reactive with both wheat germ agglutinin and Lens culinaris phytohemagglutinin were 138,000, 113,500, 92,100, 52,800, 44,700, 24,800 and 23,900. Wheat germ agglutinin was bound also to a band with a molecular weight of 72,800. Ricinus communis agglutinin bound to bands with estimated molecular weights of 138,000, 72,800, 52,800, 44,700, 24,800 and 23,900. The electrophoretic pattern of lectin-reactive polypeptides derived from normal-appearing white matter of multiple sclerosis brains was not qualitatively different from the lectin-binding pattern of control brain membrane polypeptides.

Brain↗

PubMed1981

Galactose oxidase labeling of membrane proteins from human brain white matter.

The use of galactose oxidase (EC 1.1.3.9) and tritiated sodium borohydride for labeling of membrane glycoproteins, described by Gahmberg and Hakomori, has previously been applied to the study of myelin glycoproteins of experimental animals. Rat brain myelin glycoproteins have been studied by sequential lectin affinity of chromatography and recently the lectin-binding capacity of rat central nervous system myelin glycoproteins has been characterized. Complex heterogeneity of the glycoprotein pattern of rat central nervous system myelin has been reported, and so a variety of glycoproteins can be expected to exist in human white matter membranes. Application of the galactose oxidase procedure to the study of human brain membranes could be useful in research concerning certain neurological diseases if the properties of autopsy brain material are taken into account. In this study, membrane proteins of human autopsy brain white matter were subjected to the galactose oxidase/NaB3H4 labeling procedure and the membrane labeled by this method or by the [3H]acetic anhydride techniques were studied by lectin affinity chromatography using Lens culinaris phytohemagglutinin (lentil lectin) attached to Sepharose 4B beads.

Cerebral Cortex↗