The Antigens and Autoantigens of the Seminal Vesicle

Orsini, Frank R.; Shulman, Sidney

doi:10.1084/jem.134.1.120

Cited by 13 publications

(3 citation statements)

References 16 publications

(14 reference statements)

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“…Further, incomplete recovery of-the applied proteins was a common occurrence, owing to protein precipitation on the column matrix, even in the presence of 3M-urea. This also was the experience of Orsini & Shulman (1971).…”

Section: Purification Of S V Basic Proteinmentioning

confidence: 70%

Androgen-dependent synthesis of basic secretory proteins by the rat seminal vesicle

Higgins¹,

Burchell²,

Mainwaring³

1976

Biochemical Journal

107

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1. Two basic proteins were purified from secretions of rat seminal vesicles by using Sephadex G-200 chromatography and polyacrylamide-gel electrophoresis under denaturing conditions. 2. It is not certain that these two proteins are distinct species and not subunits of a larger protein, but their properties are similar. Highly basic (pI = 9.7), they migrate to the cathode at high pH and their amino acid composition shows them to be rich in basic residues and serine. Threonine and hydrophobic residues are few. Both proteins are glycoproteins and have mol.wts. of 17000 and 18500. 3. Together these two proteins account for 25-30% of the protein synthesized by the vesicles, but they are absent from other tissues. 4. Changes in androgen status of the animal markedly affect these proteins. After castration, a progressive decrease in the basic proteins is observed and the synthesis of the two proteins as measured by [35S]methionine incorporation in vitro is is decreased. Testosterone administration in vivo rapidly restores their rates of synthesis. 5. These effects on specific protein synthesis are also observed for total cellular protein, and it is suggested that testosterone acts generally on the total protein-synthetic capacity of the cell and not specifically on individual proteins. Proliferative responses in the secretory epithelium may also be involved. 6. The extreme steroid specificity of the induction process suggests that the synthesis of these basic proteins is mediated by the androgen-receptor system. 7. The biological function of these proteins is not clear, but they do not appear to be involved in the formation of the copulatory plug.

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Section: Purification Of S V Basic Proteinmentioning

confidence: 70%

Androgen-dependent synthesis of basic secretory proteins by the rat seminal vesicle

Higgins¹,

Burchell²,

Mainwaring³

1976

Biochemical Journal

107

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“…species has been well documented (Esponda & Bedford, 1985;Shulman et al, 1966;Orsini & Shulman, 1971), but the effects on fertility of the antibodies raised has not been widely examined. Our results showed that the proteins of the seminal vesicle secretion (SVS) were allo-antigenic and induced the production of specific IgGs in serum, as estimated by ELISA and Western blotting.…”

Section: Figurementioning

confidence: 99%

Effect of antibodies against seminal vesicle secretion on fertility in the rat

Carballada

Esponda

1999

Zygote

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Fertile female Wistar rats were immunised against rat and mouse seminal vesicle secretion (SVS) to test the production of allo-antibodies and the effect of the antibodies elicited on fertility. Twenty-six per cent of the rat and mouse SVS-immunised females were infertile after the treatment. The sera were titrated by ELISA and used in Western blots to detect the proteins recognised. Although neither the antibody titres nor the proteins recognised by the sera showed a close relation with the degree of fertility, in all females the highest antibody titre in the fluids from the genital tract was found in the oviductal fluid and during the night of oestrus. This fact suggested that the site of action of the antibody could be the oviduct. Similar results were obtained using mouse SVS as immunogen – a fact that can be related to the antigenic similarity between the SVS of the two species. The antibodies react with the spermatozoa but not with eggs or embryos. Analyses performed on embryos collected from sterile females showed that there was a delay in fertilisation and normal embryogenesis. Our results suggest that SVS proteins are antigenic and that these antigens are bound to the spermatozoa and could take part in early pre-fertilisation events such as capacitation or sperm transport.

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“…PSA is not selective for malignant disease but is a tissue-specific kallikrein protease that indicates benign and cancerous proliferation of prostate tissue and cells. 11 The prostate specific antigen (PSA) has a concentration distribution from picogram to nanogram amounts in 100 μL of normal human plasma (NHP) from men, and so like many cytokines and regulatory factors it is often near or below UV−vis detection in normal patients. 12 The quantification of PSA over the complete range of NHP is challenging by ELISA 12 or mass spectral methods, 2 and many normal samples are below the detection limit of the assay.…”

Section: ■ Introductionmentioning

confidence: 99%

Pyridoxamine-5-phosphate Enzyme-Linked Immune Mass Spectrometric Assay Substrate for Linear Absolute Quantification of Alkaline Phosphatase to the Yoctomole Range Applied to Prostate Specific Antigen

Florentinus-Mefailoski

Marshall

2014

Anal. Chem.

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There is a need to measure proteins that are present in concentrations below the detection limits of existing colorimetric approaches with enzyme-linked immunoabsorbent assays (ELISA). The powerful enzyme alkaline phosphatase conjugated to the highly specific bacterial protein streptavidin binds to biotinylated macromolecules like proteins, antibodies, or other ligands and receptors with a high affinity. The binding of the biotinylated detection antibody, with resulting amplification of the signal by the catalytic production of reporter molecules, is key to the sensitivity of ELISA. The specificity and amplification of the signal by the enzyme alkaline phosphatase in ELISA together with the sensitivity of liquid chromatography electrospray ionization and mass spectrometry (LC-ESI-MS) to detect femtomole to picomole amounts of reporter molecules results in an ultrasensitive enzyme-linked immune mass spectrometric assay (ELIMSA). The novel ELIMSA substrate pyridoxamine-5-phosphate (PA5P) is cleaved by the enzyme alkaline phosphatase to yield the basic and hydrophilic product pyridoxamine (PA) that elutes rapidly with symmetrical peaks and a flat baseline. Pyridoxamine (PA) and (13)C PA were both observed to show a linear relationship between log ion intensity and quantity from picomole to femtomole amounts by liquid chromatography-electrospray ionization and mass spectrometry. Four independent methods, (i) internal (13)C isotope PA dilution curves, (ii) internal (13)C isotope one-point calibration, (iii) external PA standard curve, and (iv) external (13)C PA standard curve, all agreed within 1 digit in the same order of magnitude on the linear quantification of PA. Hence, a mass spectrometer can be used to robustly detect 526 ymol of the alkaline phosphatase streptavidin probe and accurately quantify zeptomole amounts of PSA against log linear absolute standard by micro electrospray on a simple ion trap.

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The Antigens and Autoantigens of the Seminal Vesicle

Cited by 13 publications

References 16 publications

Androgen-dependent synthesis of basic secretory proteins by the rat seminal vesicle

Androgen-dependent synthesis of basic secretory proteins by the rat seminal vesicle

Effect of antibodies against seminal vesicle secretion on fertility in the rat

Pyridoxamine-5-phosphate Enzyme-Linked Immune Mass Spectrometric Assay Substrate for Linear Absolute Quantification of Alkaline Phosphatase to the Yoctomole Range Applied to Prostate Specific Antigen

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