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Biomedical subjects

P Vainio

Publications and source records attributed to P Vainio.

At least 91 records · Page 5Linked to original sources
PubMed1988

Impairment of diastolic function in middle-aged type 1 (insulin-dependent) and type 2 (non-insulin-dependent) diabetic patients free of cardiovascular disease.

Left ventricular systolic and diastolic function was studied using systolic time intervals and echocardiography in 19 male and 17 female patients with Type 1 (insulin-dependent) diabetes, 24 male and 15 female patients with Type 2 (non-insulin-dependent) diabetes and 24 male and 24 female control subjects. The subjects for the present study were selected from a population based study in which 117 Type 1 and 510 Type 2 diabetic patients and 649 non-diabetic subjects were originally examined. After exclusions, none of the subjects had any evidence of coronary heart disease, hypertension or other diseases known to affect left ventricular function. There were no consistent differences in systolic time intervals or echocardiographic variables of systolic function between patients with Type 1 diabetes and non-diabetic control subjects; but patients with Type 2 diabetes showed an increased fractional shortening. Female patients with Type 2 diabetes showed an increased left ventricular mass not explicable by hypertension. Isovolumic relaxation period was longer in male (86 +/- 3 ms; mean +/- SEM) and female patients (84 +/- 6 ms) with Type 2 diabetes than in male (76 +/- 3 ms; p less than 0.05) and female (71 +/- 3 ms; p less than 0.05) control subjects. Peak diastolic filling rate was lower in female patients with Type 1 diabetes (12.8 +/- 0.8 cm/s, p less than 0.05) and in male (11.5 +/- 0.8 cm/s; p less than 0.01) and female patients (11.5 +/- 0.6 cm/s; p less than 0.001) with Type 2 diabetes as compared to male (14.4 +/- 0.7 cm/s) and female (14.9 +/- 0.5 cm/s) control subjects.(ABSTRACT TRUNCATED AT 250 WORDS)

Diabetes Mellitus, Type 1↗
PubMed1987

Evaluation of the reconstruction of brachytherapy implants in three-dimensions from stereo radiographs.

The precision and the accuracy of the stereo-shift method for reconstruction of brachytherapy implants were evaluated. Analysis of shift films was performed by measuring the coordinates of the seeds in an experimental set-up in the laboratory, by manually calculating the coordinates of the seeds from the projection distances on the stereo-shift radiographs, and by using a computer-aided treatment planning system. The resultant reconstructed coordinates agreed well with each other. The uncertainties in precision for the coordinates were expressed as the standard deviation of the measurements. The standard deviation of the computer and manual measurements agreed well with predicted values by an analysis of the random uncertainties in the reconstruction parameters. The uncertainties were within 0.2 mm for the coordinates parallel to the plan of the film and were within 0.4 mm for the coordinate perpendicular to the plane of the shift film. The uncertainties in the accuracy of the reconstruction were compared with the values obtained in clinical practice as well as with the values reported in the literature. Suggestions are made to improve the accuracy.

Brachytherapy↗
PubMed1985

1-Palmitoyl-2-pyrenedecanoyl glycerophospholipids as membrane probes: evidence for regular distribution in liquid-crystalline phosphatidylcholine bilayers.

We have synthesized 1-palmitoyl-2-pyrenedecanoyl-sn-glycero derivatives of 3-phosphatidylcholine, 3-phosphatidylethanolamine, 3-phosphatidylserine, 3-phosphatidylglycerol, 3-phosphatidylinositol, and 3-phosphatidic acid and investigated their behavior in monolayers and in neat and mixed bilayers. Fluorescence spectroscopy of neat pyrene phospholipid dispersions revealed a well-defined thermotropic transition at 13.5-19 degrees C depending on the polar head group. An endotherm coinciding with this transition was observed with differential scanning calorimetry, indicating it to be due to the melting of the lipid acyl chains. For pyrenephosphatidylethanolamine, the endotherm was observed at a much higher temperature (70 degrees C). Compression isotherms obtained at an argon/water interface revealed that the pyrene moiety somewhat increases the mean molecular area of a phospholipid molecule but does not prevent the expression of head-group-dependent packing behavior. Partition of the pyrene lipids between coexisting fluid and solid phases was investigated with fluorometry and calorimetry. Both techniques indicate that these lipids prefer the fluid phase and that this preference is independent of the head group. The rates and apparent activation energies of lateral diffusion in fluid bilayers were found to be similar for most pyrene lipids, suggesting that the lateral movement of phospholipids is not critically dependent on interactions at the head-group level. Lateral distribution of the pyrene lipids in gel and fluid phosphatidylcholine bilayers was studied with the excimer technique and calorimetry. In gel-state dipalmitoylphosphatidylcholine bilayers, the pyrene lipids form clusters. These clusters, however, do not consist of pure pyrene lipid but of aggregates (compounds) of the labeled and unlabeled lipid.(ABSTRACT TRUNCATED AT 250 WORDS)

Calorimetry, Differential Scanning↗
PubMed1985

Hydrolysis of phospholipid monolayers by human spermatozoa. Inhibition by male contraceptive gossypol.

Monomolecular films of phospholipid were used to study the interaction of intact human spermatozoa with model membranes. Exclusively with negatively charged phosphatidylglycerol monolayers rapid penetration of spermatozoa into the monolayer with subsequent hydrolysis of the lipid was triggered by the addition of 5 mM calcium into the medium. The results suggest the localization of a calcium-dependent phospholipase A2 at the outer acrosomal or plasma membrane of human spermatozoa with its active site exposed to the external environment. Preincubation of the cells with 100 microM gossypol completely abolished the ability of human spermatozoa to hydrolyze or penetrate monolayers of phosphatidylglycerol. The inhibition of the phospholipase activity by gossypol may contribute to the unknown contraceptive mechanisms of this non-steroidal male antifertility agent.

Gossypol↗
PubMed1984

Mineral density of calcaneus in men at different ages: a population study with special reference to life-style factors.

The mineral density of the calcaneus was measured in representative samples of men, aged 31-35, 51-55, and 71-75 years, utilizing a 125I-gamma-ray attenuation method. There was a gradual decrease in bone mineral density from the youngest to the oldest age group. Those men who participated in regular physical activity or who were non-smokers showed higher values for bone mineral density when compared to sedentary men or smokers, respectively. Furthermore, bone mineral density correlated positively with physical performance capacity and negatively with the prevalence of chronic diseases.

Adult↗
PubMed1983

N-(5-dimethylaminonaphthalene-1-sulfonyl)-3-aminobenzene boronic acid as an active-site-directed fluorescent probe of lipoprotein lipase.

Resonance energy transfer was used to monitor the interaction of an active-site-directed fluorescent inhibitor, N-(5-dimethylaminonaphthalene-1-sulfonyl)-3-aminobenzene boronic acid, and lipoprotein lipase (EC 3.1.1.34). The binding of this probe to the active site of lipoprotein lipase had an association constant, Ka, of 1.1 X 10(6) M-1, indicating a strong interaction. The binding was displaced competitively by benzene boronic acid. The method described provides a sensitive procedure to probe the active site of lipoprotein lipase.

Animals↗
PubMed1983

Interaction of synthetic N-5-dimethylaminonaphthalene-1-sulfonyl-apolipoprotein C-II peptides with lipoprotein lipase.

Synthetic fragments of apo-C-II, specifically labeled on their NH2-terminals with the 5-dimethylaminonaphthalene-1-sulfonyl (dansyl or DNS) fluorophore, have been prepared by solid phase peptide synthesis. When a complex is formed between bovine milk lipoprotein lipase and N-dansyl-apo-C-II peptides, resonance energy transfer occurs from the tryptophan residues of the enzyme to the dansyl-labeled peptides upon excitation at 280 nm. In the absence of lipid, the association constant increases 10-fold when the length of the DNS peptide is increased from apo-C-II-DNS(64-78) (0.04 X 10(6) M-1) to apo-C-II-DNS(60-78) (0.3 X 10(6) M-1). In the presence of lipid, the association constants are dependent on peptide chain length, and increase from 0.4 X 10(6) M-1 for apo-C-II-DNS(64-78) to 2.2 X 10(7) M-1 for apo-C-II-DNS(43-78). The interactions are specific for lipoprotein lipase, are disrupted by guanidinium chloride, are not affected by 1.0 M NaCl, and are competitive with the corresponding nondansylated peptide. Apolipoproteins C-III and A-I, at 5 to 1 molar ratios, had no effect on the interaction. These findings demonstrate the importance of the COOH-terminal region in the lipoprotein lipase-apo-C-II interaction and show that activation of the enzyme involves a specific protein-protein interaction.

Amino Acids↗
PubMed1983

Esterase-type of activity possessed by human plasma apolipoprotein C-II and its synthetic fragments.

Human plasma apolipoproteins apo A-I, A-II, C-I, C-II and C-III (with the exception of apoE), porcine pancreatic colipase and procolipase hydrolyze 4-methylumbelliferyloleate. In all cases, liberation of 4-methylumbelliferone could be inhibited by phenylmethylsulfonyl-fluoride, thus suggesting the involvement of serine residues. To the best of our knowledge this is the first report on the esterase activities of these peptides. Synthetic fragments of the lipoprotein lipase activator, apoC-II, prepared according to the known sequence, also possessed this esterase-type of activity. Furthermore, the esterase-type of activities of the synthetic apoC-II fragments with different chain lengths bore a relatively good correlation to the reported abilities of these peptides to produce activation of lipoprotein lipase. We propose a model for the mechanism of activation of lipoprotein lipase by apolipoprotein C-II. ApoC-II would enhance the apparent catalytic rate constant of lipoprotein lipase by functioning as a specific acyl-enzyme hydrolase. A similar catalytic mechanism is suggested for other protein co-factors of hydrolytic enzymes.

Amino Acid Sequence↗
PubMed1983

Hydrolysis of 1-triacontanoyl-2-(pyren-1-yl)hexanoyl-sn-glycero-3-phosphocholine by human pancreatic phospholipase A2.

A novel fluorescent phospholipid analogue, 1-triacontanoyl-2-(pyren-1-yl)hexanoyl-sn-glycero-3-phosphocholine (C30PHPC) was employed as a substrate for human pancreatic phospholipase A2. C30PHPC has a main endothermic phase transition with Tm at 46 degrees C as determined by differential scanning calorimetry (DSC). For an aqueous dispersion of C30PHPC the ratio of the intensities of pyrene excimer and monomer fluorescence emission, (IE/IM) has a maximum between 32 and 36 degrees C. The excimer emission intensity (at 480 nm) exceeds the monomer emission intensity (at 400 nm) 6.5-fold thus indicating a close packing of the phospholipid pyrene moieties in the lipid phase. C30PHPC has a limiting mean molecular area of 37 A2 at surface pressure 35 dyn cm-1 as judged by the compression isotherm at an air-water interphase. The hydrolysis of C30PHPC by human pancreatic phospholipase A2 was followed by monitoring the increase in the pyrene monomer fluorescence emission intensity occurring as a consequence of transfer of the reaction product, pyren-1-yl hexanoic acid into the aqueous phase. The enzyme reaction exhibited an apparent Km of 2.0 microM substrate. Calcium at a concentration of 0.2 mM activated the enzyme 4-fold. Maximal hydrolytic rates were obtained at 45 degrees C and at pH between 5.5 and 6.5. The enzyme reaction could be inhibited by 5 mM EDTA, confirming the absolute requirement for Ca2+ of this enzyme. The present fluorimetric assay easily detects hydrolysis of C30PHPC in the pmol min-1 range. Accordingly, less than nanogram levels of human pancreatic phospholipase A2 can be detected.

Fluorescent Dyes↗
PubMed1982

Inhibition of lipoprotein lipase by benzene boronic acid. Effect of apolipoprotein C-II.

The catalytic mechanism of triacylglycerol hydrolysis by lipoprotein lipase was studied. We found lipoprotein lipase to be inhibited by benzene boronic acid, with an apparent Ki of 8.9 micro M at pH 7.4. This indicates the presence of serine and histidine in the active site of the enzyme. Inhibition of lipoprotein lipase by benzene boronic acid is likely to be due to the formation of an inhibitor-enzyme complex having analogous bonding to the active site histidine and serine as the transition-state complex which precedes the formation of an obligatory acyl-enzyme intermediate. The presence of apolipoprotein C-II, the apolipoprotein activator of lipoprotein lipase, partly reverses the inhibition of lipoprotein lipase by benzene boronic acid. This reversal by apolipoprotein C-II has a distinct pH optimum in the range of 8-9.

Animals↗
PubMed1981

The active site and the phospholipid activation of rat liver lysosomal lipase are not stereospecific.

The stereochemical specificity of lysosomal lipase of rat liver was investigated using enantiomeric triacylglycerol analogs, sn-1-alkyl-2,3-diacylglycerol and sn-3-alkyl-1,2-diacylglycerol as substrates. Lysosomal lipase utilized both substrates with equal rates. The dependence of the activity of lysosomal lipase on the stereoconfiguration of activating acidic phospholipid was also studied. Our results showed that both sn-3-phospholipids (diphosphatidylglycerol, phosphatidylserine) and sn-1-phospholipids (bis(monoacylglycero)phosphate (BMP)) were efficient activators of this enzyme and thus the stereochemical configuration of the activating phospholipid is not important. Accordingly, the rat liver lysosomal lipase lacks stereospecificity with respect to both the triacylglycerol substrate and the acidic phospholipid activator.

Animals↗
PubMedDate not supplied

Quantification of metabolites from single-voxel in vivo 1H NMR data of normal human brain by means of time-domain data analysis.

We present here a combination of time-domain signal analysis procedures for quantification of human brain in vivo 1H NMR spectroscopy (MRS) data. The method is based on a separate removal of a residual water resonance followed by a frequency-selective time-domain line-shape fitting analysis of metabolite signals. Calculation of absolute metabolite concentrations was based on the internal water concentration as a reference. The estimated average metabolite concentrations acquired from six regions of normal human brain with a single-voxel spin-echo technique for the N-acetylaspartate, creatine, and choline-containing compounds were 11.4 +/- 1.0, 6.5 +/- 0.5, and 1.7 +/- 0.2 mumol kg-1 wet weight, respectively. The time-domain analyses of in vivo 1H MRS data from different brain regions with their specific characteristics demonstrate a case in which the use of frequency-domain methods pose serious difficulties.

Aspartic Acid↗
PubMedDate not supplied

MR T2 relaxometry in Alzheimer's disease and age-associated memory impairment.

A prolonged MR T2 relaxation time was proposed to mark the presence and severity of Alzheimer's disease (AD). We studied the value of T2 relaxometry in diagnosing early AD. T2 was measured from 54 patients with AD, 25 subjects with age-associated memory impairment (AAMI), 18 elderly and 16 young controls. The AD patients had longer T2 in the right hippocampal head (104 +/- 11 ms) and tail (98 +/- 10 ms) than age-matched controls (95 +/- 5 and 92 +/- 9 ms, respectively). This prolongation was not related to age. In the AD group, the T2 of the left hippocampal head also correlated with the clinical severity. The T2 of the amygdala did not differ across the groups. Increased T2 in the temporal and parietal white matter and the thalamus related to increasing age rather than to the diagnostic category. The AAMI subjects had T2 comparable with those of age-matched controls. Despite the prolongation of T2 in the AD group the possible diagnostic value was compromized by a substantial overlap between the study groups. We, thus, conclude that the T2 relaxometry is not a reliable method for diagnosing early AD.

Adult↗