Prostate-specific antigen in serum occurs predominantly in complex with alpha 1-antichymotrypsin
(1991) In Clinical Chemistry 37(9). p.25-1618- Abstract
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... (More)
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.
(Less)
- author
- Lilja, H LU ; Christensson, A LU ; Dahlén, U ; Matikainen, M T ; Nilsson, O ; Pettersson, K and Lövgren, T
- organization
- publishing date
- 1991-09
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Animals, Antibodies, Monoclonal, Antigens, Neoplasm/blood, Biomarkers, Tumor/blood, Chromatography, Gel, Electrophoresis, Agar Gel, Electrophoresis, Polyacrylamide Gel, Epitopes/analysis, Female, Humans, Male, Mice, Mice, Inbred BALB C, Prostate-Specific Antigen, alpha 1-Antichymotrypsin/immunology
- in
- Clinical Chemistry
- volume
- 37
- issue
- 9
- pages
- 8 pages
- publisher
- American Association for Clinical Chemistry
- external identifiers
-
- scopus:0026077430
- pmid:1716536
- ISSN
- 0009-9147
- DOI
- 10.1093/clinchem/37.9.1618
- language
- English
- LU publication?
- yes
- id
- 2ac14579-6d2f-45c8-9f04-84bf770cc03d
- date added to LUP
- 2019-05-16 14:08:42
- date last changed
- 2024-09-04 18:57:54
@article{2ac14579-6d2f-45c8-9f04-84bf770cc03d, abstract = {{<p>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.</p>}}, author = {{Lilja, H and Christensson, A and Dahlén, U and Matikainen, M T and Nilsson, O and Pettersson, K and Lövgren, T}}, issn = {{0009-9147}}, keywords = {{Animals; Antibodies, Monoclonal; Antigens, Neoplasm/blood; Biomarkers, Tumor/blood; Chromatography, Gel; Electrophoresis, Agar Gel; Electrophoresis, Polyacrylamide Gel; Epitopes/analysis; Female; Humans; Male; Mice; Mice, Inbred BALB C; Prostate-Specific Antigen; alpha 1-Antichymotrypsin/immunology}}, language = {{eng}}, number = {{9}}, pages = {{25--1618}}, publisher = {{American Association for Clinical Chemistry}}, series = {{Clinical Chemistry}}, title = {{Prostate-specific antigen in serum occurs predominantly in complex with alpha 1-antichymotrypsin}}, url = {{http://dx.doi.org/10.1093/clinchem/37.9.1618}}, doi = {{10.1093/clinchem/37.9.1618}}, volume = {{37}}, year = {{1991}}, }