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Biomedical subjects

H Lilja

Publications and source records attributed to H Lilja.

At least 145 records · Page 8Linked to original sources
PubMed1989

Microprocessor based waveform analysis of the fetal electrocardiogram during labor.

An increase in T wave amplitude of the fetal ECG (FECG) has experimentally been correlated to elevated catecholamine levels and myocardial glycogenolysis. The FECG changes have also been described during human delivery. The present aim was to investigate whether these ECG changes could be reproduced in an easily handled real time microprocessor system, and to correlate them to biochemical and clinical data. During 40 deliveries the FECG signal was transferred to a microcomputer system for real time averaging of the FECG. There was a high capacity of the system to reproduce the ST waveform changes though the averaging procedure reduced the QRS magnitude by 10%. With a normal umbilical artery pH (greater than or equal to 7.25) the highest T/QRS ratios recorded during each delivery was 0.26 +/- 0.19 (mean +/- S.D.). With lowered pH (less than 7.25) the T/QRS increased to 0.33 +/- 0.10 (P less than 0.02). A similar difference between the two groups was seen when the T/QRS ratios from the last hour before birth were compared; 0.13 +/- 0.08 and 0.18 +/- 0.05, respectively (P less than 0.01). Changes in the ST waveform with T/QRS greater than or equal to 0.30, ST segment alterations, or negative T waves appeared during 40% of the deliveries, however, 30% were short standing changes (less than 30 min). Intermediate CTG changes during at least 30 min occurred in 41% and the pattern was classified as abnormal in 18%. Using the scalp electrode as signal source, the ECG analysis could add further information to the routine CTG recording on the fetal condition during delivery.

Electrocardiography↗
PubMed1989

Radioimmunoassay of beta-microseminoprotein, a prostatic-secreted protein present in sera of both men and women.

We describe a simple radioimmunoassay of beta-microseminoprotein, one of the three most abundant secretory proteins of the prostate gland. The detection limit of the assay is 1 microgram/L, and its precision, expressed as the total coefficient of variation, is less than 10% for values between 10 and 150 micrograms/L. Using this assay, we found that beta-microseminoprotein immunoreactivity was present in sera from both sexes at about the same concentration. The protein detected had the same molecular size on gel chromatography as the protein isolated from seminal plasma, and dilution curves for the sera paralleled that for the pure protein. The findings suggest that beta-microseminoprotein is present in serum of healthy subjects of both sexes and that it originates in tissue other than the prostate gland. The range of the serum concentration was 0-10.6 micrograms/L (median 4.1) for 51 healthy adult women and 1.1-14.7 micrograms/L (median 6.2) for 35 healthy adult men not older than 40 years. In males with prostatic cancer the concentration in serum was highly variable and often greatly increased. The concentration of beta-microseminoprotein was correlated with that of creatinine in serum, suggesting that the protein is eliminated--at least partly--from the circulation by glomerular filtration. Little of the protein was present in the urine of women. In urine from men the concentration was high and variable, probably because of local contribution from the prostate gland to the urethral urine.

Age Factors↗
PubMed1988

Site-site interactions in EF-hand calcium-binding proteins. Laser-excited europium luminescence studies of 9-kDa calbindin, the pig intestinal calcium-binding protein.

Europium(III) binding to 9-kDa calbindin from pig intestines was studied by direct excitation of the 7Fo----5Do transition of the ion and by near-ultraviolet circular dichroic spectroscopy. Europium(III) binding is clearly biphasic. As with other lanthanides the C-terminal metal-binding site (site II) is filled first. The europium ion in this site gives an excitation spectrum with a single peak at 579.1 nm (peak 2). The occupation of the N-terminal site (site I) by europium gives excitation spectra that are pH-dependent and show a peak at 579.4 nm (peak 1a) at pH 5 which shifts to 578.7 nm (peak 1b) over the pH range 5-7. At pH 8.07 the fluorescence from europium in site I largely disappears because of weak binding, whereas that from site II is quenched by about 75% in spite of full occupancy of the site as shown by circular dichroic titration. There is a strong interaction between the two sites in spite of the very different affinities. The fluorescence from site II increases stoichiometrically with the addition not only of the first equivalent of europium, but also concomitantly with the fluorescence from site I upon addition of the second equivalent. Furthermore, when Eu1-calbindin is titrated with calcium the fluorescence at 579.1 nm is quenched by about 30% during the addition of one equivalent of calcium which fills site I. Subsequent titration with large excesses of calcium displaces europium from site II. The affinity of site II for europium is about 100 times that of calcium under these conditions.

Animals↗
PubMed1988

Three predominant proteins secreted by the human prostate gland.

Analyses of the proteins of azoospermic ejaculates from subjects with defective seminal vesicles demonstrated that three prostatic-secreted proteins were predominant. Prostatic acid phosphatase (PAP), prostate-specific antigen (PSA; or gamma-seminoprotein), and beta-microseminoprotein (beta-MSP; or beta-inhibin), were identified as the three predominant proteins secreted by the normal human prostate gland. Immunohistochemical localization of these proteins, in the epithelium of normal prostatic acini and ducts, with the avidin-biotin complex procedure demonstrated that each PAP-immunoreactive cell was invariably immunoreactive both with PSA-and beta-MSP-monospecific antisera as well.

Acid Phosphatase↗
PubMed1988

Immunohistochemical distribution of the three predominant secretory proteins in the parenchyma of hyperplastic and neoplastic prostate glands.

Prostatic acid phosphate (PAP), prostate-specific antigen (PSA), and beta-microseminoprotein (beta-MSP) were regularly localized immunohistochemically to the epithelium of the acini and that of the ducts in the nodules of 24 cases of benign prostatic hyperplasia. The immunohistochemical distribution of these three prostatic-secreted proteins was also examined, with monoclonal antisera against PAP and PSA and with polyclonal antisera against PAP, PSA, and beta-MSP, in a series of 40 cases of prostatic adenocarcinomas graded according to the WHO classification. Highly differentiated (grade I) carcinomas showed a high incidence of PAP-, PSA-, and beta-MSP-immunoreactive cells. As in the normal and hyperplastic prostate parenchyma, highly differentiated (grade I) carcinomas were found to contain an almost equal number of PAP-, PSA-, and beta-MSP-immunoreactive cells. When semiquantitatively assessed, the incidence of PAP-, PSA-, and beta-MSP-immunoreactive cells was found to be lower in the moderately and poorly differentiated (grades II and III) tumors than in the highly differentiated ones; they also showed greater staining variability. Tumor cells immunoreactive with a monoclonal antiserum raised against PAP in carcinomas of grades II and III were less frequent than tumor cells immunoreactive with antisera against PSA, beta-MSP, and a polyclonal antiserum against PAP. The almost identical distribution of PSA and beta-MSP in carcinomas of grades II and III suggests that PSA and beta-MSP are not less sensitive tumor markers than PAP for the monitoring of the course and the treatment of prostatic carcinomas.

Acid Phosphatase↗
PubMed1988

New software QRS detector algorithm suitable for real time applications with low signal-to-noise ratios.

A new algorithm for QRS-detection is presented; it is based on template-comparison, but unlike the cross-correlation algorithm, it involves no multiplications, and is less time-consuming and therefore suitable for real-time applications. It is demonstrated that the new algorithm performs practically as well as cross correlation, and is useful in situations where low signal to noise ratios are common.

Algorithms↗
PubMed1988

Fetal ECG during labour: a presentation of a microprocessor system.

Changes in the ST waveform of the fetal ECG have been detected in 47 term deliveries with vertex presentations using a specially developed microprocessor-based system for on-line recording of T wave amplitude. The T wave was quantified by the T/QRS ratio. The recording included one scalp electrode for exploration and a maternal skin electrode as reference. Signal quality allowed optimal ST waveform assessment in 89% of the cases. The degree of perinatal asphyxia was judged from cord artery acid-base status and the neonatal outcome. In completely normal fetuses at term the mean T/QRS ratio was 0.148 with a standard deviation of 0.048. With this basic information we can proceed in the investigation of the T/QRS ratio as a means for fetal surveillance.

Electrocardiography↗
PubMed1988

Fetal ECG during labour: a suggested standard.

Recording the fetal ECG as a means of fetal monitoring during labour has been investigated by many researchers. Different signal processing methods have been used, making comparisons difficult so that agreement on several topics has not been reached. We suggest the basis of a standard method of recording and processing the signal which we believe will be acceptable to the research and clinical communities.

Animals↗
PubMed1988

Structure and function of prostatic- and seminal vesicle-secreted proteins involved in the gelation and liquefaction of human semen.

At ejaculation, the epididymal spermatozoa mix with the secretions produced by the seminal vesicles and the prostate. The glandular secretions immediately turns into a gel-like structure which entraps the spermatozoa. The ejaculated spermatozoa become progressively motile as the gel dissolves. The discovery, structure, and interactions of proteins involved in these post-ejaculatory phase reactions of semen are here reported.

Amino Acid Sequence↗
PubMed1987

Molecular cloning of human prostate specific antigen cDNA.

A lambda gt11 clone encoding prostate specific antigen has been isolated from a human prostate cDNA library. The cDNA insert of 1415 nucleotides hybridizes specifically to a prostate mRNA species of 1.5 kb. The nucleotide sequence codes for part of a signal peptide, a short propiece and the mature protein of 237 amino acid residues. The Mr for the non-glycosylated protein was 26,089. One potential site for N-linked carbohydrate attachment was identified. The primary structure shows extensive homology with proteases of the kallikrein family.

Amino Acid Sequence↗
PubMed1987

Seminal vesicle-secreted proteins and their reactions during gelation and liquefaction of human semen.

The comparison of measurements of fibronectin and lactoferrin in ejaculates from vasectomized men, subjects with functional deficiency or aplasia of the seminal vesicles, and reference subjects provided evidence that both the fibronectin and the lactoferrin in human seminal fluid originate from the seminal vesicles and the ampullae. The fibronectin is incorporated in the framework of the seminal gel formed during the immediate postejaculatory phase, whereas the lactoferrin remains in solution. In the seminal gel fibronectin is linked to its predominant structural protein, a high molecular weight seminal vesicle protein (semenogelin). Both the gel-bound fibronectin and semenogelin are progressively fragmented and solubilized by the abundant prostatic kallikrein-like protease (prostate-specific antigen) during and after seminal gel liquefaction. Lactoferrin remains essentially unaffected by the seminal proteases.

Fibronectins↗
PubMed1986

Carcinogenesis studies of 4,4'-methylenedianiline dihydrochloride given in drinking water to F344/N rats and B6C3F1 mice.

Carcinogenesis studies of 4,4'-methylenedianiline dihydrochloride (98.6% pure) were conducted by administering this chemical in the drinking water of F344/N rats and B6C3F1 mice. Groups of 50 rats and 50 mice of each sex received drinking water containing 150 or 300 ppm 4,4'-methylenedianiline dihydrochloride (dosage expressed as the free base) for 103 wk. Groups of 50 rats and 50 mice of each sex, given drinking water adjusted with 0.1 N HCl to the pH (3.7) of the 300-ppm formulation, served as controls. Survival was comparable among groups except for male mice receiving the 300-ppm dose of 4,4'-methylenedianiline dihydrochloride; survival in that group was lower than that in controls. Mean body weight was reduced in 300-ppm-dose female rats and 300-ppm-dose male and female mice compared to controls. Water consumption was reduced in a dose-related manner in both sexes of rats. No compound-related clinical effects were observed. Under the conditions of these studies, there was clear evidence of carcinogenicity for F344/N rats and for B6C3F1 mice in that 4,4'-methylenedianiline dihydrochloride caused increased incidences of (1) follicular-cell carcinomas of the thyroid gland (controls, 0/49; low dose, 0/47; high dose, 7/48, 15%; p less than or equal to 0.012) and neoplastic nodules of the liver (controls, 1/50, 2%; low dose, 12/50, 24%; high dose, 25/50, 50%; p less than or equal to 0.001) in male rats, (2) follicular-cell adenomas (controls, 0/47; low dose, 2/47, 4%; high dose, 17/48, 35%; p less than or equal to 0.001) and C-cell adenomas (controls, 0/47; low dose, 3/47, 6%; high dose, 6/48, 13% p less than or equal to 0.029) of the thyroid gland in female rats, (3) follicular-cell adenomas of the thyroid gland (controls, 0/47; low dose, 3/49, 6%; high dose, 16/49, 33%; p less than or equal to 0.001), carcinomas of the liver (controls, 10/49, 20%; low dose, 33/50, 66%; high dose, 29/50, 58%; p less than or equal to 0.001), and pheochromocytomas of the adrenal gland in male mice (controls, 2/48, 4%; low dose, 12/49, 24%; high dose, 14/49, 29%; p less than or equal to 0.001), and (4) follicular-cell adenomas of the thyroid gland (controls, 0/50; low dose, 1/47, 2%; high dose, 13/50, 26%; p less than or equal to 0.001), carcinomas (controls, 1/50, 2%; low dose, 6/50, 12%; high dose, 11/50, 22%; p less than or equal to 0.002) and adenomas (controls, 3/50, 6%; low dose, 9/50, 18%; high dose, 12/50, 24%.(ABSTRACT TRUNCATED AT 400 WORDS)

Aniline Compounds↗
PubMed1986

Familial alpha 1-antichymotrypsin deficiency.

We studied patients and their relatives with partial deficiency, approximately 50% of normal plasma levels, of alpha 1-antichymotrypsin (ACT), an acute phase reactant with anti-cathepsin G activity. Six of eight ACT deficient individuals, over 25 years of age, had liver and three of eight lung manifestations, varying from severe disease to subtle laboratory abnormalities. The ACT of deficient individuals (who are heterozygotes for a rare gene, q = 0.003) had normal crossed immunoelectrophoretic properties. The abnormal gene is inherited in an autosomal, dominant way. The results suggest that deficiency of this antiprotease, which also has immune response modulating properties, may predispose to liver and lung disease.

Adolescent↗
PubMed1985

Isolation and characterization of two minor fractions of alpha 1-antitrypsin by high-performance liquid chromatographic chromatofocusing.

alpha 1-Antitrypsin is a glycoprotein that separates into five electrophoretic fractions, viz. M2, M4, M6, M7 and M8. Con A-Sepharose separates the protein into three fractions according to the branching degree of the three oligosaccharide chains. The Con A affinity is identical for M4 and M7 and for M6 and M8. Within each pair the proteins were isolated by rapid chromatofocusing. The M7 and M8 have the same carbohydrate structure as the major M4 and M6 respectively, but have lost the first five N-terminal amino acids (Glu-Asp-Pro-Glu-Gly) as compared to the majority of the protein.

Amino Acid Sequence↗
PubMed1985

Amino acid sequence of the predominant basic protein in human seminal plasma.

The predominant basic protein in liquefied human seminal plasma is the major degradation product of the gel-forming protein secreted by the seminal vesicles. The amino acid sequence of this basic protein is presented. The basic protein contains 52 amino acid residues. It is devoid of cysteine, methionine, tryptophan, and leucine, but contains seven histidine residues located in the NH2-terminal half of the molecule. The calculated Mr of 5753 is in close agreement with that obtained from gel filtration in guanidine-HCl on Sephacryl S-200 (Mr = 6000).

Amino Acid Sequence↗
PubMed1985

ST waveform changes of the fetal electrocardiogram during labour--a clinical study.

Waveform changes in the fetal electrocardiogram (ECG) are under reassessment as a means of fetal surveillance. The purpose of the study was to identify ST waveform changes from the fetal scalp lead during labour and to compare any change with conventional signs of fetal distress. Two scalp electrodes provided a sufficiently stable signal from which ST waveform changes could be identified and measured as the T/QRS ratio. No infant was clinically hypoxic. Only 26% of the 46 patients studied had a continuously normal CTG whereas 67% had no ST waveform abnormalities. A relation was found between the two variables as the mean T/QRS ratio increased from 0.20 (SD 0.11) during epochs of normal CTG to 0.27 (SD 0.17) with CTG changes. A linear correlation (r = 0.58, P less than 0.01) was found between the T/QRS ratio before birth and the cord plasma lactate values.

Electrocardiography↗
PubMed1985

A kallikrein-like serine protease in prostatic fluid cleaves the predominant seminal vesicle protein.

A 33-kD glycoprotein, known as the "prostate-specific antigen," was purified to homogeneity from human seminal plasma. The prostatic protein was identified as a serine protease, and its NH2-terminal sequence strongly suggests that it belongs to the family of glandular kallikreins. The structural protein of human seminal coagulum, the predominant protein in seminal vesicle secretion, was rapidly cleaved by the prostatic enzyme, which suggests that this seminal vesicle protein may serve as the physiological substrate for the protease. The prostatic enzyme hydrolyzed arginine- and lysine-containing substrates with a distinct preference for the former. All synthetic substrates tested were poor substrates for the enzyme. Synthetic Factor XIa substrate (pyro-glutamyl-prolyl-arginine-p-nitroanilide), and the synthetic kallikrein substrate (H-D-prolyl-phenylalanyl-arginine-p-nitroanilide) were hydrolyzed with maximum specific activities at 23 degrees C of 79 and 34 nmol/min per mg and Km values of 1.0 and 0.45 mM, respectively. Synthetic substrates for plasmin, chymotrypsin, and elastase were either not hydrolyzed by the enzyme at all, or only hydrolyzed very slowly.

Body Fluids↗