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H Lilja

Publications and source records attributed to H Lilja.

At least 127 records · Page 7Linked to original sources
PubMed1992

Molecular cloning of epididymal and seminal vesicular transcripts encoding a semenogelin-related protein.

Freshly ejaculated human semen has the appearance of a loose gel in which the predominant structural protein components are the seminal vesicle-secreted semenogelins (Sg). The primary structure of the 439-residue SgI has previously been obtained by cDNA cloning. This cDNA cross-hybridizes to a larger transcript coding for a second secretory protein, SgII. Here we report the almost complete structure of a precursor of SgII established by lambda gt11 clones isolated from epididymal and seminal vesicular cDNA libraries. The deduced amino acid sequence of the 559-residue mature protein has a molecular weight of 62,931 but an increase in weight may be provided by asparagine-linked oligosaccharide attachment at residue 249. SgII, which has 78% overall identity with SgI, contains eight 60-residue regions that display conspicuous internal sequence similarity, whereas SgI only contains six of these regions. The SgII structure is translated from an open reading frame in a polyadenylylated 2.4-kilobase transcript. The message is abundant in the seminal vesicles but rare in the epididymis.

Amino Acid Sequence↗
PubMed1992

Protein C inhibitor in human body fluids. Seminal plasma is rich in inhibitor antigen deriving from cells throughout the male reproductive system.

An assay was developed for the measurement of human protein C inhibitor antigen (PCI) in blood plasma and other biological fluids. Both native PCI, modified inhibitor, and complexes of inhibitor with activated protein C or plasma kallikrein could be measured with the assay. Inhibitor antigen concentrations were found to be very high in seminal plasma (greater than 200 mg/liter), more than 40 times the concentration of PCI found in blood plasma. The inhibitor in seminal plasma was unable to form complexes with activated protein C. Gel filtration and immunoblotting findings indicated that the inhibitor in seminal plasma is present in a high molecular mass complex or cleaved to its modified form. As PCI antigen was absent from seminal plasma of patients with dysfunctional seminal vesicles, the seminal vesicle glands would appear to be the major source of seminal plasma PCI, a conclusion supported by immunohistochemical demonstration of the presence of PCI epitopes in the secretory epithelium of the seminal vesicles. Specific PCI immunoreactivity was also shown to be present in the testes, the epididymis glands, and the prostate, suggesting the inhibitor to have a complex or multiple function in the male reproductive system. Conclusive evidence of a local synthesis of PCI in the four male sex glands was provided by Northern blot analysis of RNA from these organs.

Adolescent↗
PubMed1991

Molecular cloning and sequence analysis of the cDNA encoding the human acrosin-trypsin inhibitor (HUSI-II).

A complete cDNA clone encoding the human acrosin-trypsin inhibitor HUSI-II has been isolated from a cDNA library of human testis and completely sequenced. The cDNA of 594 bp contained an open reading frame of 252 base pairs. The deduced amino acid sequence comprised the complete amino acid sequence of HUSI-II and a putative signal peptide. Northern blotting analysis revealed that HUSI-II is synthesized in testis, epididymis and seminal vesicle, but not in the prostate gland.

Amino Acid Sequence↗
PubMed1991

Prostate-specific antigen in serum occurs predominantly in complex with alpha 1-antichymotrypsin.

Immunologic measurements of the serum concentration of prostate-specific antigen (PSA), an abundant prostatic-secreted serine proteinase, are frequently used to monitor patients with prostate cancer, though it has not been ascertained whether this immunoreactivity represents a PSA zymogen, the active proteinase, or PSA complexed to extracellular proteinase inhibitors. To characterize the PSA immunoreactivity in serum, we used monoclonal antibodies produced against PSA and a polyclonal rabbit IgG against alpha 1-antichymotrypsin in the design of three noncompetitive PSA assays: assay T, which detected PSA both when present as the active proteinase and when complexed to alpha 1-antichymotrypsin; assay F, which recognized the active proteinase but most poorly detected PSA complexed to alpha 1-antichymotrypsin; and assay C, which was specific for PSA complexed to alpha 1-antichymotrypsin. We used the three assays to measure PSA immunoreactivity in 64 patients' sera and in the effluent after gel chromatography of sera from four patients. This identified an 80- to 90-kDa complex between PSA and alpha 1-antichymotrypsin as the predominant fraction of the PSA immunoreactivity in blood plasma; an immunoreactive 25- to 40-kDa compound was the minor fraction.

Animals↗
PubMed1991

Regulation of cystatin C activity by serine proteinases.

The effect of four human serine proteinases on the human cysteine proteinase inhibitor, cystatin C, has been studied in vitro. Neutrophil elastase in catalytic amounts was observed to rapidly cleave cystatin C at neutral pH, thereby giving rise to a modified form of the inhibitor lacking the N-terminal Ser1-Val10 decapeptide. The two other leukocyte serine proteinases, cathepsin G and neutrophil proteinase 4, did not catalytically hydrolyse cystatin C bonds. Neither had the seminal plasma serine proteinase, prostate-specific antigen, any effect on cystatin C. The physiological implications of neutrophil elastase catalysed modification of cystatin C are discussed, and recent findings indicating that this reaction also occurs in vivo are reviewed.

Amino Acid Sequence↗
PubMed1990

Enzymatic activity of prostate-specific antigen and its reactions with extracellular serine proteinase inhibitors.

Prostate-specific antigen (PSA) is one of the three most abundant prostatic-secreted proteins in human semen. It is a serine proteinase that, in its primary structure, manifests extensive similarities with that of the Arg-restricted glandular kallikrein-like proteinases. When isolated from semen by the addition of chromatography on aprotinin-Sepharose to a previously described procedure, PSA displayed chymotrypsin-like activity and cleaved semenogelin and the semenogelin-related proteins in a rapid and characteristic pattern, but had no trypsin-like activity. About one third of the purified protein was found to be enzymatically inactive, due to cleavage carboxy-terminal of Lys145. Active PSA formed SDS-stable complexes with alpha 1-antichymotrypsin, alpha 2-macroglobulin-analogue pregnancy zone protein. PSA formed inhibitory complexes with alpha 1-antichymotrypsin at a molar ratio of 1:1, a reaction in which PSA cleaved the inhibitor in a position identical to that reported from the reaction between chymotrypsin and alpha 1-antichymotrypsin. The formation of stable complexes between PSA and alpha 1-antichymotrypsin occurred at a much slower rate than that between chymotrypsin and alpha 1-antichymotrypsin, and at a similar or slightly slower rate than that between PSA and alpha 2-macroglobulin. When added to normal blood plasma in vitro, active PSA formed stable complexes both with alpha 2-macroglobulin and alpha 1-antichymotrypsin. This complex formation may be a crucial determinant of the turnover of active PSA in intercellular fluid or blood plasma in vivo.

Amino Acid Sequence↗
PubMed1990

Species- and organ-specificity of secretory proteins derived from human prostate and seminal vesicles.

Polyclonal antibodies against semenogelin (SG) isolated from human seminal vesicle secretion and acid phosphatase (PAP), beta-microseminoprotein (beta-MSP), and Prostate-Specific Antigen (PSA) derived from human prostatic fluid, as well as a monoclonal antibody against beta-MSP were used for immunocytochemical detection of the respective antigens in different organs from different species. SG immunoreactivity was detected in the epithelium of the pubertal and adult human and in monkey seminal vesicle, ampulla of the vas deferens, and ejaculatory duct. PAP, beta-MSP, and PSA immunoreactivities were detected in the pubertal and adult human prostate and the cranial and caudal monkey prostate. With the exception of a weak PSA immunoreactivity in the proximal portions of the ejaculatory duct, none of the latter antisera reacted with seminal vesicle, ampullary, and ejaculatory duct epithelium. Among the non-primate species studied (dog, bull, rat, guinea pig) only the canine prostatic epithelium displayed a definite immunoreactivity with the PAP antibody and a moderate reaction with the PSA antibody. No immunoreaction was seen in bull and rat seminal vesicle and canine ampulla of the vas deferens with the SG antibody. The same was true for the (ventral) prostate of rat, bull, and dog for beta-MSP. The epithelium of the rat dorsal prostate showed a slight cross-reactivity with the monoclonal antibody against beta-MSP and one polyclonal antibody against PSA. The findings indicate a rather strict species-dependent expression of human seminal proteins which show some similarities in primates, but only marginal relationship to species with different physiology of seminal fluid.

Acid Phosphatase↗
PubMed1990

Three predominant prostatic proteins.

Prostatic acid phosphatase (PAP), prostate-specific antigen (PSA; or gamma-seminoprotein), and beta-microseminoprotein (beta-MSP; PSP94 or beta-inhibin) are the three predominant proteins secreted by the normal human prostate gland. In the epithelium of normal and hyperplastic prostatic acini and ducts PAP, PSA and beta-MSP have an identical immunohistochemical localization. Highly differentiated (grade I) carcinomas contain an almost equal number of PAP-, PSA- and beta-MSP-immunoreactive cells; the incidence of these cells is lower and they display a greater staining variability in the moderately and poorly (grade II-III) differentiated tumours. Especially in poorly differentiated tumours PSA seems to be a more sensitive immunohistochemical marker than PAP or prostatic carcinomas. Moreover, the use of PAP as a marker for prostatic carcinomas is complicated by the reported structural similarities between the prostatic secreted acid phosphatase and lysosomal acid phosphatase occurring in all tissues. The use of beta-MSP as a marker for prostatic carcinomas may be limited by indications of non-prostatic production of this protein.

Acid Phosphatase↗
PubMed1990

Cell biology of semenogelin.

Semenogelin is the predominant protein in human semen. It is synthetised by the secretory epithelium of the seminal vesicles as a 461 amino acid precursor protein. Following cleavage of a predominantly hydrophobic signal peptide, the secreted protein contains 439 amino acid residues. The amino acid sequence of semenogelin has a repetitive structure, but it displays no significant homology to any other characterized translation product. In the seminal vesicle secretion, semenogelin occurs in disulphide-linked high molecular mass complexes together with two less abundant 71 and 76 kDa proteins. These proteins have a very close antigenic and structural relationship to semenogelin, but contrary to semenogelin one or both of these semenogelin-related proteins are also expressed by the secretory epithelium of the epididymis. Semenogelin and the semenogelin-related proteins are the major proteins involved in the gelatinous entrapment of ejaculated spermatozoa. Antigenic epitopes common to these proteins are localised to the locomotive parts of the spermatozoa. The spermatozoa become progressively motile when gel-forming proteins are fragmented by the kallikrein-like protease, prostate-specific antigen, and the gel dissolves.

Amino Acid Sequence↗
PubMed1990

Fetal ECG waveform analysis should improve fetal surveillance in labour.

Fetal heart rate (FHR) and fetal electrocardiogram (ECG) recordings were obtained from a scalp electrode with maternal thigh as reference and used for ST waveform analysis in 201 patients in labour. Nearly 45% had suspicious or abnormal FHR traces whilst only 27% had T/QRS ratio greater than 0.25 (mean +/- 2 SD). A normal T/QRS ratio identified 99.3% of fetuses with normal buffering capacity in cord artery blood. Of 13 infants with a cord artery blood pH less than 7.15, standard bicarbonate was less than 15.0 mmol/l in five who had an average T/QRS ratio less than 0.25 throughout labour. Of the eight with respiratory acidosis, five had an increase in T/QRS ratio greater than 0.25 for longer than 20 minutes prior to delivery, in two the ratio increased during the last few minutes and one had no change (pH 7.14). Persistent elevation of T/QRS in the first stage of labour identified those with decrease in buffer capacity in cord arterial blood (sensitivity of 94.1%). Acute hypoxia was recognized by the rapid rise in T/QRS. The specificity of T/QRS to identify fetuses at risk increased by combining the ST waveform analysis with FHR changes.

Electrocardiography↗
PubMed1990

Beta microseminoprotein is not a prostate-specific protein. Its identification in mucous glands and secretions.

Beta microseminoprotein (beta inhibin, PSP94), an unglycosylated protein of 94 amino acids with unknown function, is one of the predominating proteins in the secretion of the human prostate gland. In this work the authors have demonstrated that the expression of beta microseminoprotein is not restricted to the prostate and that the protein has a previously unrecognized widespread occurrence in the human body. According to radioimmunoassay, beta microseminoprotein immunoreactivity is present in many nonprostatic body fluids. The highest concentrations were found in secretions from the respiratory tract; in tracheobronchial fluid sometimes even at concentrations comparable to that in seminal plasma (about 1 g/l). Intermediate concentrations were found in gastric juice and some samples of secretion from the uterine cervix, whereas tears, saliva, pancreatic juice, bile, and mucus from the colon had low concentrations. According to gel chromatography, the molecular size of the beta microseminoprotein immunoreactivity present in tracheal fluid, gastric juice, and secretion from the uterine cervix did not differ from that of beta microseminoprotein in seminal plasma. The beta microseminoprotein immunoreactive component present in gastric juice had the same amino-terminal amino acid sequence as prostatic beta microseminoprotein (14 residues identified in material purified from gastric juice), providing further evidence for chemical identity of a nonprostatic beta microseminoprotein with the prostatic protein. Immunohistochemical staining with affinity-purified antibodies demonstrated the presence of beta microseminoprotein in many tissues, including the goblet cells in the tracheobronchial epithelium, tracheobronchial submucosal glands, certain mucosal cells in the antrum of the stomach, some glands of Brunner in the duodenum, and in parts of the mucosa of the colon. At least in the respiratory tract, the staining was localized to mucus-containing cells. beta microseminoprotein immunoreactivity also was localized to the cilia of the ciliated epithelium in the respiratory tract, the fallopian tubes, and the Gartner ducts of the uterine cervix. The pattern of tissue distribution of beta microseminoprotein found in this work indicates a connection of beta microseminoprotein with mucous secretions.

Adult↗
PubMed1989

Molecular cloning of a small prostate protein, known as beta-microsemenoprotein, PSP94 or beta-inhibin, and demonstration of transcripts in non-genital tissues.

In order to study the gene expression of the seminal plasma protein beta-microseminoprotein, also known as PSP94 and beta-inhibin, clones encoding this protein were isolated from a cDNA library constructed in lambda gt11. Nucleotide sequencing confirmed the structure of a previously cloned cDNA. By northern blot analysis identical sized transcripts were demonstrated in the prostate, the respiratory (tracheal, bronchial and lung) tissues and the antrum part of the gastric mucosa. Thus, the protein is not primarily associated with male reproductive function. Although probably of no physiological significance, a slight structural similarity to the ovarian inhibin beta-chains was identified in the C-terminal half of the molecule.

Amino Acid Sequence↗
PubMed1989

The microheterogeneity of desialylated alpha 1-antichymotrypsin: the occurrence of two amino-terminal isoforms, one lacking a His-Pro dipeptide.

ACT (alpha 1-antichymotrypsin), a serine antiproteinase with specificity against neutrophil cathepsin G, is homologous with alpha 1-antitrypsin, plasminogen activator inhibitor and angiotensinogen, all with known amino-terminal microheterogeneity. Here we report that the two predominant isoforms of desialylated ACT obtained on isoelectric focusing correspond to a microheterogeneity at the amino terminus of ACT: one isoform (His-Pro-Asn-Ser-Pro-) and a two residues shorter isoform (Asn-Ser-Pro-). The relative occurrence of the two isoforms was comparable both in normal plasma, acute-phase plasma and plasma from subjects with heterozygous familial ACT deficiency. When desialylated ACT, isolated by affinity chromatography from ACT-deficient, normal or acute-phase plasma, was compared with regard to mass and charge microheterogeneity, we found no significant differences in either respect. Nor was the isoform pattern of desialylated plasma from patients with rheumatoid arthritis different. Although the occurrence of heterozygous familial ACT deficiency implies genotypic variation, isolated ACT from patients with the trait was not found to exhibit any phenotypic variation detectable by standard electrophoretic methods.

Amino Acid Sequence↗
PubMed1989

Semenogelin, the predominant protein in human semen. Primary structure and identification of closely related proteins in the male accessory sex glands and on the spermatozoa.

The predominant protein in human semen, semenogelin, was characterized by lambda gt11 clones isolated from a seminal vesicular cDNA library. One clone, carrying a cDNA insert of 1606 nucleotides and a polyadenylated tail, coded for the entire semenogelin precursor. An open reading frame of 1386 nucleotides encodes a signal peptide and the mature protein of 439 amino acid residues, in which residues 85-136 are identical with a previously characterized semenogelin fragment. The polypeptide chain displays a most conspicuous region of internal sequence homology where 46 of the 58 amino acid residues at positions 259-316 are repeated at positions 319-376. An abundant seminal vesicular transcript of 1.8 kilobases (kb) codes for semenogelin. Two additional transcripts, one seminal vesicular 2.2-kb species and one epididymal 2.0-kb species, code for related proteins that have a close structural relationship as well as antigenic epitopes in common with semenogelin. Semenogelin and the semenogelin-related proteins are the major proteins involved in the gelatinous entrapment of ejaculated spermatozoa. Antigenic epitopes common to these proteins are localized to the parts of the spermatozoa involved in locomotion. The spermatozoa become progressively motile as the gel-forming proteins are fragmented by the kallikrein-like protease, prostate-specific antigen, and the gel dissolves.

Amino Acid Sequence↗
PubMed1989

Partial characterization of a thyroid-stimulating hormone-like peptide in neuroendocrine cells of the human prostate gland.

Immunohistochemical identification of the most prevalent type of neuroendocrine (NE) cells in the human prostate gland can be made with polyclonal antisera against human thyroid-stimulating hormone (TSH). A TSH-like peptide was characterized by analysis of prostatic tissue homogenates with sodium dodecyl sulfate-polyacrylamide gel (SDS-PAGE) electrophoresis followed by immunoblotting. A single protein band, with an apparent mass of about 32 kDa after reduction, was identified both with polyclonal antisera against human TSH and with a polyclonal antiserum raised against a synthetic peptide corresponding to the carboxyterminal part of the beta-subunit of human TSH. The TSH-like prostatic peptide identified here is, on the basis of its molecular mass and absence of immunoreactivity with an antiserum raised against a synthetic peptide representing the mid-portion of the beta-subunit of TSH, not identical with the pituitary beta-subunit of TSH. On the other hand, this 32 kDa prostatic peptide may have certain structural elements in common with the pituitary beta-subunit of TSH, since it is recognized both with polyclonal antisera against TSH and with an antiserum against the carboxyterminal part of the beta-subunit of TSH.

Aged↗
PubMed1989

Electrocardiographic waveform changes and catecholamine responses during acute hypoxia in the immature and mature fetal lamb.

The aim of the present study was to investigate the changes in electrocardiographic waveform and the release of catecholamines in the fetal lamb during nonacidemic fetal hypoxia. Chronically instrumented fetal lambs were subjected to reproducible hypoxia by reduction of the maternal placental blood flow. This was achieved by complete obstruction of the maternal aorta for 60 seconds. The fetuses were divided into an immature (119 to 126 days, n = 10) and a mature group (129 to 141 days, n = 6). Both groups of fetuses had a marked fall in oxygen tension (from 2.43 +/- 0.12 to 1.46 +/- 0.12 and 2.22 +/- 0.15 to 1.11 +/- 0.17 kilopascals [kPa] in the immature and mature groups, respectively) and in oxygen saturation (from 48% +/- 3% to 17% +/- 2% and 49% +/- 3% to 15% +/- 3%, respectively), but only modest changes occurred in pH and carbon dioxide tension. Basal fetal catecholamine concentrations did not differ between the groups but increased more significantly in the mature group with acute hypoxia. An increase in the T wave amplitude of the fetal electrocardiogram occurred in both groups during the latter part of occlusion with peak values shortly after removal of the occlusion. A linear correlation was found between the plasma epinephrine concentration and the T/QRS ratio in the mature group. Fetuses in both groups showed a marked bradycardia of similar magnitude during the occlusion but differed during the early phase of heart rate recovery by a slower acceleration of heart rate in the mature group. In connection with this marked bradycardia, the mature group showed a significant rise in mean arterial blood pressure at end of the occlusion. We suggest that fetal maturity has a significant influence no only on the release of catecholamines during nonacidemic hypoxia but also on the cardiovascular reaction pattern and changes in the ST waveform.

Acute Disease↗