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- 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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- Ulvsbäck, M., et al.
(author)
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Molecular cloning of a small prostate protein, known as beta-microsemenoprotein, PSP94 or beta-inhibin, and demonstration of transcripts in non-genital tissues
- 1989
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In: Biochem Biophys Res Commun. ; 164:3, s. 5-1310
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Journal article (peer-reviewed)abstract
- 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.
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- Weiber, Håkan
(author)
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Human Beta-microseminoprotein expression, with special reference to gastric mucosa, atrophic corpus gastritis and gastric carcinoids
- 1999
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Doctoral thesis (other academic/artistic)abstract
- Human Beta-microseminoprotein is a 94 amino acid protein with 10 cysteins present in seminal plasma and on many mucosal surfaces in the body. The function of the protein is unknown. The purpose of this investigation was to study the distribution of Beta-microseminoprotein in the human body, especially in the stomach. The latter was studied under both normal and pathological conditions. A radioimmunoassay for measuring of Beta-microseminoprotein was developed. Tracheobronchial secretion and seminal plasma contain about 1 g/L, gastric juice about 1 mg/L and serum from men and women contain about 1-10 mg/L Beta-microseminoprotein. The synthesis and secretion of Beta-microseminoprotein in gastric mucosa was proved by demonstration of Beta-microseminoprotein mRNA in the mucosa and presence of higher values of Beta-microseminoprotein in gastric juice devoid of tracheobronchial contribution, than in serum. Immunohistochemical staining of the stomach mucosa revealed mucin producing cells (M cells) and cells with endocrine characteristics (E cells) to contain Beta-microseminoprotein. Investigations showed that the majority of E cells also contain chromogranin A and gastrin. Atrophic corpus gastritis entails hyperplasia and hypertrohpy of the E cells and raises serum concentrations of Beta-microseminoprotein. Immunohistochemical presence of Beta-microseminoprotein in gastric carcinoid tumours correlate with tumour progression, which could be of value in the follow up of patients with gastric carcinoid disease.
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- Weiber, Håkan, et al.
(author)
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β microseminoprotein is not a prostate-specific protein. Its identification in mucous glands and secretions
- 1990
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In: American Journal of Pathology. - 0002-9440. ; 137:3, s. 593-604
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Journal article (peer-reviewed)abstract
- β microseminoprotein (β 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 β microseminoprotein is not restricted to the prostate and that the protein has a previously unrecognized widespread occurrence in the human body. According to radioimmunoassay, β 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 β microseminoprotein immunoreactivity present in tracheal fluid, gastric juice, and secretion from the uterine cervix did not differ from that of β microseminoprotein in seminal plasma. The β microseminoprotein immunoreactive component present in gastric juice had the same amino-terminal amino acid sequence as prostatic β microseminoprotein (14 residues identified in material purified from gastric juice), providing further evidence for chemical identity of a nonprostatic β microseminoprotein with the prostatic protein. Immunohistochemical staining with affinity-purified antibodies demonstrated the presence of β 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 in mucus-containing cells. β 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 β microseminoprotein found in this work indicates a connection of β microseminoprotein with mucous secretions.
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