| 1. |
- Abrahamsson, P. ‐A, et al.
(author)
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Immunohistochemical distribution of the three predominant secretory proteins in the parenchyma of hyperplastic and neoplastic prostate glands
- 1988
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In: The Prostate. - : Wiley. - 0270-4137 .- 1097-0045. ; 12:1, s. 39-46
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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.
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| 2. |
- Abrahamsson, P. ‐A, et al.
(author)
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Partial characterization of a thyroid‐stimulating hormone‐like peptide in neuroendocrine cells of the human prostate gland
- 1989
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In: The Prostate. - : Wiley. - 0270-4137 .- 1097-0045. ; 14:1, s. 71-81
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Journal article (peer-reviewed)abstract
- 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 β‐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 β‐subunit of TSH, not identical with the pituitary β‐subunit of TSH. On the other hand, this 32 kDa prostatic peptide may have certain structural elements in common with the pituitary β‐subunit of TSH, since it is recognized both with polyclonal antisera against TSH and with an antiserum against the carboxyterminal part of the β‐subunit of TSH.
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| 3. |
- Abrahamsson, Per-Anders, et al.
(author)
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Radioimmunoassay of beta-microseminoprotein, a prostatic-secreted protein present in sera of both men and women
- 1989
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In: Clinical Chemistry. - 0009-9147. ; 35:7, s. 1497-1503
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Journal article (peer-reviewed)abstract
- 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.
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| 4. |
- Laurent, Torvald C., et al.
(author)
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Urinary excretion of hyaluronan in man
- 1987
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In: Scandinavian Journal of Clinical and Laboratory Investigation. - 0036-5513 .- 1502-7686. ; 47:8, s. 793-799
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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.
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| 5. |
- Lilja, H., et al.
(author)
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Three predominant proteins secreted by the human prostate gland
- 1988
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In: The Prostate. - : Wiley. - 0270-4137 .- 1097-0045. ; 12:1, s. 29-38
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Journal article (peer-reviewed)abstract
- 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 γ‐seminoprotein), and β‐microsemi‐noprotein (β‐MSP; or β‐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 β‐MSP‐monospecific antisera as well.
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