| 1. |
- Abrahamsson, P. ‐A, et al.
(author)
-
Immunohistochemical distribution of the three predominant secretory proteins in the parenchyma of hyperplastic and neoplastic prostate glands
- 1988
-
In: The Prostate. - : Wiley. - 0270-4137 .- 1097-0045. ; 12:1, s. 39-46
-
Journal article (peer-reviewed)abstract
- Prostatic acid phosphatase (PAP), prostate‐specific antigen (PSA), and β‐microseminoprotein (β‐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 β‐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 β‐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 β‐MSP‐immunoreactive cells. When semiquantitatively assessed, the incidence of PAP‐, PSA‐, and β‐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, β‐MSP, and a polyclonal antiserum against PAP. The almost identical distribution of PSA and β‐MSP in carcinomas of grades II and III suggests that PSA and β‐MSP are not less sensitive tumor markers than PAP for the monitoring of the course and the treatment of prostatic carcinomas.
|
|
| 2. |
- Laurent, Torvald C., et al.
(author)
-
Urinary excretion of hyaluronan in man
- 1987
-
In: Scandinavian Journal of Clinical and Laboratory Investigation. - 0036-5513 .- 1502-7686. ; 47:8, s. 793-799
-
Journal article (peer-reviewed)abstract
- A specific assay for hyaluronan (hyaluronic acid) has been applied to the determination of the polysaccharide in urine. The excretion in 22 healthy subjects was 330 micrograms/24 h (SD 77). The excretion was correlated with body weight and was therefore somewhat higher in males than in females. The molecular weight of the main fraction of urinary hyaluronan was in the range of 4000 to 12,000 in accordance with the hypothesis that it originates from blood and arises by glomerular filtration. A small fraction was of higher molecular weight and could have been produced in the urinary tract. Hyaluronan in male and female urine displayed the same molecular weight distributions. Patients with rheumatoid arthritis and primary biliary cirrhosis showed a two-fold and three-fold increase, respectively, of hyaluronan in urine with concurrently high levels of the polysaccharide in serum. A patient with Werner's syndrome displayed a ten-fold increase of the polysaccharide in both serum and urine.
|
|
| 3. |
- Lilja, H., et al.
(author)
-
Characterization of the predominant basic protein in human seminal plasma, one cleavage product of the major seminal vesicle protein
- 1984
-
In: Scandinavian Journal of Clinical and Laboratory Investigation. - : Informa UK Limited. - 0036-5513 .- 1502-7686. ; 44:5, s. 439-446
-
Journal article (peer-reviewed)abstract
- From liquefied human seminal plasma, we purified the predominant basic protein which appears following liquefaction of coagulated semen. The protein was purified in the presence of di-isopropylfluorophosphate to retard its degradation. Heparin-Sepharose® chromatography was followed by gel filtration (Biogel® P 60) and by fast performance liquid chromatography on a reversed phase column (C8). The basic protein is a single polypeptide chain with an apparent molecular mass of 12.8 kDa, and has a PI value between that of trypsinogen (9.3) and cytochrome C (10.3). The protein contains no carbohydrate, is rich in histidine, glutamate, and lysine, but is devoid of both cysteine and methionine. The amino-terminal portion of the protein sequence is unique: HNKQEGRDHDKSKG HFHRVVIHHKGGKAHRG-.A specific rabbit antiserum was raised against the 12.8 kDa basic protein. The protein was found to be unique to seminal plasma among all extracellular fluids examined. Three immunologically related 52 kDa, 71 kDa, and 76 kDa proteins were identified in seminal vesicle secretion when it had been reduced. Prostatic enzyme(s) degraded these proteins to the 12.8 kDa basic protein and several other basic proteins with apparent molecular masses below 18 kDa.
|
|
| 4. |
- Lilja, H., et al.
(author)
-
Liquefaction of coagulated human semen
- 1984
-
In: Scandinavian Journal of Clinical and Laboratory Investigation. - : Informa UK Limited. - 0036-5513 .- 1502-7686. ; 44:5, s. 447-452
-
Journal article (peer-reviewed)abstract
- Liquefaction of coagulated human semen was inhibited by o-phenanthroline; subsequent addition of Zn2+ reversed this inhibition, but not if the coagulum was repeatedly washed before Zn2+ was added. No liquefaction of the coagulum occurred when Fe2 was added (in a 1:3 molar ratio to o-phenanthroline), and the gel repeatedly washed. This o-phenanthroline-depleted coagulum was liquefied by resuspended pellet from ultracentrifuged pooled seminal plasma. In denatured and reduced semen coagulate, we identified the 52 kDa, 71 kDa, and 76 kDa protein bands of the predominant seminal vesicle protein. The protein was not present in the supernatant after centrifugation of coagulated semen, and it was degraded to several minor basic proteins when semen liquefied. These findings imply that the predominant seminal vesicle protein functions as the structural protein of coagulated semen. In much the same way as in ejaculated semen, the 52 kDa, 71 kDa, and 76 kDa protein bands in seminal vesicle secretion collected postmortem were digested to minor basic proteins after incubating the secretion with resuspended pellet from ultracentrifuged seminal plasma. This pellet contained the membrane-bound succinyl(alanine)3 -p- nitroanilide hydrolysing peptidase of prostatic origin which, like the liquefaction process, was active in the presence of EGTA, inhibited by non-chelated Zn2+, and inactivated by o-phenanthroline - an inactivation that was reversed by Zn2+.
|
|
| 5. |
- Lilja, H., et al.
(author)
-
Seminal vesicle-secreted proteins and their reactions during gelation and liquefaction of human semen.
- 1987
-
In: The Journal of clinical investigation. - 0021-9738. ; 80:2, s. 281-285
-
Journal article (peer-reviewed)abstract
- 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.
|
|
| 6. |
- Lilja, H., et al.
(author)
-
The predominant protein in human seminal coagulate
- 1985
-
In: Scandinavian Journal of Clinical and Laboratory Investigation. - : Informa UK Limited. - 0036-5513 .- 1502-7686. ; 45:7, s. 635-641
-
Journal article (peer-reviewed)abstract
- The predominant protein in human seminal vesicle secretion constitutes the structural protein of coagulated semen. This high molecular weight protein (HMW-SV-protein) is stable in seminal vesicle secretion during in vitro storage at 37 d̀C for at least 20 h, but is rapidly cleaved on mixing with prostatic proteases. Seminal coagulate, washed free of souble components, is dissoluble by 2 to 3 mol/1 of guanidine-HCl. Although dithiothreitol added to seminal coagulate does not liquify the clot, complexes between HMW-SV-proteins are broken up by reduction under denaturing conditions, which suggests that the non-covalent linkages of HMW-SV-proteins are essential in the clot. Prostatic proteases cleave the HMW-SV-protein during liquefaction of ejaculated semen to a series of labile proteins. These proteins are further cleaved to peptides of successively decreasing size after completed liquefaction. The cleavage of the HMW-SV-protein is the major cause of the fast shift of the electrophoretic pattern of seminal proteins if semen is stored without protease inhibitors.
|
|
| 7. |
- Sundkvist, Göran, et al.
(author)
-
Autonomic and peripheral nerve function in early diabetic neuropathy. Possible influence of a novel aldose reductase inhibitor on autonomic function
- 1987
-
In: Acta Medica Scandinavica. - 0001-6101. ; 221:5, s. 445-453
-
Journal article (peer-reviewed)abstract
- Autonomic and peripheral nerve functions as well as the possible short-term effect of a novel aldose reductase inhibitor (ARI) on neuropathy were evaluated in 30 male type I diabetics (age 25-44 years, mean 34; duration of diabetes 10-20 years, mean 34) with neurographic signs of peripheral neuropathy (PN). Autonomic neuropathy (AN) was established by the heart rate reactions to deep breathing (E/I ratio = vagal function) and to tilt (acceleration index = sympathetic and vagal functions; the brake index = vagal function). Twenty-nine patients, 13 with AN, completed the study. Among neurographic variables, only sural nerve function tests correlated with autonomic functions. Patients with AN showed significantly lower mean sensory action potential amplitudes (SAPA) sural, indicating axonal losses, than patients without AN (3.58 +/- 0.79 microV v. 7.34 +/- 1.12 microV; p less than 0.01). PN as measured by neurography did not improve during ARI treatment. On the other hand, vagal function (brake indices) improved (p less than 0.05) during ARI in AN patients.
|
|
