Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0376358 (prostate cancer)
 59,338 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Prostate-specific antigen (PSA) is a tissue-specific glycoprotein identified by Wang in 1979. It is synthesized in the prostate independently of prostatic acid phosphatase (PAP). A total of 199 subjects were divided into four groups: controls aged less than 50 years, controls aged more than 50 years, patients with benign prostatic hyperplasia (BPH) and patients with prostatic carcinoma. PSA cut-off value was set at 10 ng/ml (mean for the BPH group plus 2 SD). With this cut-off value PSA could not be used as an early predictor of prostatic carcinoma. The association of PSA and PAP in prostatic cancer increases the number of patients with positive biological markers.
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PMID:Serum prostate-specific antigen determination in prostatic carcinoma. 245 94

In our previous report, monoclonal antibody PR92 has defined prostate- and breast tumor-associated PR92 antigen. The molecular nature of PR92 antigen, especially the epitope involved in specific interaction with PR92 monoclonal antibody, is described. PR92 antigen was purified from the cell extract or tissue culture medium of prostate cancer cell line DU145 by means of monoclonal antibody-coupled Sepharose 4B affinity chromatography, followed by a Sephacryl S-500 chromatography. Physical and chemical characterization, coupled with high-performance liquid chromatography, determined that PR92 antigen is a glycoprotein with a molecular weight of about 470,000, comprising repeating subunits of about 44,000. Sialic acid was found to form a critical part, while D-galactose and N-acetylgalactosamine were also involved, in the epitope structure. PR92 antigen is rich in serine, threonine, proline, glycine, and alanine and poor in aromatic amino acid residues. The carbohydrate moieties may be predominantly O-linked to polypeptide chains which contribute directly or indirectly to maintain the integrity of the epitope. Elucidation of the molecular nature of PR92 antigen may help understand the mechanism of shedding into the body fluids during tumor progression.
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PMID:Molecular characterization of the epitope in prostate and breast tumor-associated PR92 antigen. 246 8

Prostatic specific antigen (PSA), glycoprotein with molecular weight of 34000, was first identified by Wang and Coll. in prostatic tissue initially; then Papsidero and Wang purified PSA in the sera of patients with prostatic cancer. We determined PSA concentration in 132 serum samples obtained from 111 patients affected by prostatic carcinoma: of these 61 had untreated prostatic cancer (6 had a stage A disease, 10 stage B, 19 stage C and 26 stage D) and 50 were variously treated (17 with cyproterone acetate, 11 with estramustine phosphate, 10 with LH-RH analogues, 9 underwent radical prostatectomy and 3 radiation therapy alone). Each patients was assigned a histological grade according to Gaeta, by means of a perineal transrectally guided prostatic biopsy. At periodical follow-ups of treated subjects, patients' state and neoplastic evolution were considered. Serum PSA has been measured by a competitive radioimmunoassay (PSA-Double antibody, Diagnostic Product Corporation) in which 125-I-labeled PSA competes with PSA in the samples for antibody sites. The antibody-bound fraction is then precipitated and counted. Since manipulation of the prostate gland may lead to elevated PSA levels, patients' samples were obtained prior to rectal examination, biopsy or surgical procedures. On the basis of a preliminary study of samples from healthy blood donors, we fixed the cut-off value at 2.9 ng/ml. In patients with untreated prostatic carcinoma PSA serum mean value was 26.33 ng/ml (range 0.5-100), resulting elevated in 56/61 (90,16%) patients.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:[Prostate-specific antigen (PSA): diagnostic and prognostic implications in the evaluation of carcinoma of the prostate]. 246 27

The determination of gamma-seminoprotein (gamma-Sm) (also called prostate-specific antigen [PSA], prostate antigen [PA], or p30) in human serum has been recently demonstrated to be more sensitive and specific for diagnosing prostate cancer and monitoring the condition of patients with prostate cancer than the prostatic acid phosphatase (PAP) test. Because the gamma-Sm (PSA) test seems likely to replace the PAP test in the area of urology and study of prostate-specific antigens is expanding, we have reviewed physicochemical properties and clinical significance of two prostate-specific antigens, gamma-Sm (PSA) and beta-microseminoprotein (beta-MSP). Both proteins have been proved to originate in the prostate gland and have not been detected in any other human tissues by an immunohistologic study. The usefulness of gamma-Sm and beta-MSP in determining the origin of metastatic tumors has also been shown. gamma-Sm is a glycoprotein with a molecular weight of 26,079 for the peptide portion, of which the amino acid sequence is identical to so-called PSA and homologous with serine proteases (the kallikrein family). Its chymotrypsin-like activity with a unique substrate specificity has also been demonstrated. The molecular weight of beta-MSP is 10,652 from the amino acid sequence, in which the protein has been shown to contain no alanine residue.
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PMID:Two prostate-specific antigens, gamma-seminoprotein and beta-microseminoprotein. 265 6

Over 600 hybridomas were derived from the immunization of mice with live cells and aqueous extracts of the human prostatic carcinoma cell line PC3. A total of 26 hybridomas with restricted reactivities were selected, subcloned and antibodies tested on a variety of tumor and normal cells. Seven monoclonal antibodies showed reactivity for prostate cancer and other tumor cell lines, including breast carcinomas. Three of the antibodies obtained after immunization with live cells reacted with live cells only and three of the four antibodies obtained after immunization with cell extract reacted with cell extracts and spent culture media. The fourth antibody in the latter group was reactive only in the immunoperoxidase staining assay. Antibody PrS5 recognized a 90,000 molecular weight molecule from 125I-surface-labeled cells in immunoprecipitation analysis. Antibodies PrE3 and PrD8 detected a nonacid glycolipid pentasaccharide from PC3 cells and meconium, and a glycoprotein of 115,000 molecular weight from 125I-surface-labeled red blood cells. The similar patterns of reactivity in RIAs and antigen analysis suggest that antibodies PrE3 and PrD8 recognize the same molecule. The results emphasize the usefulness of immunohistochemistry in the testing of monoclonal antibodies and the impact of the form in which the antigen is presented on the resultant antibody specificity.
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PMID:Monoclonal antibody-defined antigens of human prostate cancer cell line PC3. 351 28

The current investigation describes the purification and partial characterization of a new adenocarcinoma-associated antigen (ACAA). ACAA is a large molecular weight glycoprotein (Mr 790,000 by size chromatography on Sepharose CL-6B) that migrates in the alpha 1 region upon electrophoresis and is eluted from a DEAE-cellulose column at a 0.1 M NaCl concentration. ACAA is immunochemically and biochemically different from carcinoembryonic antigen, alpha-fetoprotein, pancreatic oncofetal antigen, human pancreatic tissue antigen, CA 19-9, ferritin, and acute-phase proteins. Assays for ACAA were carried out using a solid-phase sandwich enzyme immunoassay. The results indicate that ACAA is present in sera of all individuals. Patients with cancer have higher serum levels of ACAA than normal individuals. The greatest frequency of elevated serum values of ACAA was seen in patients with lung and pancreatic cancers followed by colorectal, breast, and prostate cancer. The measurement of ACAA levels may be valuable in the diagnosis and clinical management of patients with certain cancers.
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PMID:Purification, partial characterization, and clinical evaluation of an adenocarcinoma-associated antigen. 353 83

Peripheral serum levels of testosterone, immunoreactive oestrogens (E2), FSH, LH, prolactin and growth hormone (hGH) and two steroid-sensitive proteins, 'pregnancy-associated alpha 2-glycoprotein' (alpha 2-PAG) and sex hormone binding globulin (SHBG), were measured in patients with prostatic cancer before treatment and after orchidectomy or during combined oral and intramuscular oestrogen treatment. Following orchidectomy, the serum levels of testosterone and E2 decreased whilst the levels of FSH and LH increased significantly. No changes were noted in the serum levels of alpha 2-PAG, SHBG or prolactin. Oestrogen treatment significantly decreased the serum levels of testosterone, FSH and LH whilst levels of alpha 2-PAG, SHBG and prolactin were increased significantly. Serum levels of hGH during oestrogen treatment were significantly higher than in patients subjected to orchidectomy. These data are at variance with the established dogma of the oestrogen/androgen balance as a physiological regulator or liver protein synthesis, and indicate that factors other than the endogenous steroids may be operative. hGH may play an important role in this respect.
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PMID:Influence of orchidectomy or oestrogen treatment on serum levels of pregnancy associated alpha 2-glycoprotein and sex hormone binding globulin in patients with prostatic cancer. 392 1

In order to measure beta1-SP1-glycoprotein (SP1), on RIA system by the 2-antibody method was established as a measuring method of the low concentration range. SP1 concentrations were measured by this method in the sera of women in early pregnancy, in the amniotic fluids of late pregnancy, in the sera of malignant tumour patients. Furthermore, SP1 concentrations in the sera of women in early pregnancy as well as E2, E3, progesterone and HCG concentrations in the same samples were measured, and correlations between them were examined. 1) The minimum sensitivity of this measuring system was 3ng/ml. The optimum concentration of samples was between 10 approximately 660ng/ml. 2) The correlation between the data obtained by this RIA method and the SRID method was as close as r = 0.9287. 3) SP1 concentrations in the sera of women in early pregnancy were 0.17 +/- 0.12 microgram/ml in the fifth week of pregnancy, showing an almost straight increase during the course of pregnancy, and were 31.62 +/- 3.20 microgram/ml in the 13th week of pregnancy. 4) SP1 concentrations in amniotic fluids were 1.09 approximately 2.20 microgram/ml and were equal to about 1% of SP1 concentrations in the sera of women in late pregnancy. SP1 concentrations in the sera of umbilical cord blood were 0.13 approximately microgram/ml, which were equal to about 0.1% of SP1 concentrations in the sera of women in late pregnancy. 5) SP1 was detected in all four samples of the choriocarcinoma patients' sera, and the concentrations were 25 approximately 2,600ng/ml. Sp1 was detected in 6 of the 15 samples of the cervical carcinoma patients' sera, and the detection rate was 40%. SP1 was detected in 3 of the 6 samples of the leukemia patients' sera and 1 of the 4 samples of the prostatic cancer patients' sera. SP1 detection rates and concentrations appeared to increase in the sera of cervical carcinoma and leukemia patients in accordance with the progress of the diseases. SP1 concentrations in the sera of women in early pregnancy were not correlative to measured E2 and E3 concentrations in the same samples, but there was a significant correlation with progesterone and HCG concentrations. The RIA method for measuring SP1, which we have established, is available for measuring SP1 in the low concentration range. The method is expected to be applied clinically, such as in examinations in early pregnancy, and will be available in fundamental studies such as attempts to measure the SP1 movement in malignant tumour patients, in cooperation with studies of the meaning of SP1 production at pregnancy.
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PMID:[Studies for a sensitive radioimmunoassay of beta1-Sp1-glycoprotein (SP1) (author's transl)]. 697 Jan 46

The [3H]estramustine-binding macromolecule in human prostate was partially characterized using a number of chromatographic procedures. Although human estramustine-binding protein (HEMBP) had a marked tendency to aggregate in several systems, a molecular weight of about 54,000 was determined by gel filtration on Sephacryl S-200 Superfine and high-performance liquid chromatography. A sedimentation-coefficient of about 3.6S was obtained for HEMBP when analyzed by sucrose density gradient centrifugation. Isoelectric focusing in polyacrylamide gels indicated an isoelectric point of 4.7 to 4.8, which was in agreement with the elution position of HEMBP following chromatofocusing on Polybuffer Exchanger 94. Furthermore, HEMBP was eluted from diethylaminoethyl-Sepharose with 0.23 M KCl, was retained by concanavalin A-Sepharose (indicating that HEMBP is a glycoprotein), but did not interact with Affi-Gel Blue. Special efforts were concentrated on establishing that HEMBP was a species distinct from human serum albumin. Separation between the [3H]estramustine-labeled HEMBP and the [3H]estramustine-human serum albumin complex was obtained both on sucrose density gradients by chromatography on Affi-Gel Blue, by chromatofocusing, by gel filtration, by isoelectric focusing, and on concanavalin A-Sepharose by affinity chromatography. Twenty-two of 27 human benign hyperplastic prostate cytosol samples were found to contain protein immunochemically similar to estramustine-binding protein (EMBP) purified from rat ventral prostate as determined by the EMBP radioimmunoassay method. Concentrations from 0.2 to 139.6 ng EMBP per mg of total cytosolic protein (mean, 19.3) were determined. Furthermore, four of seven prostatic cancer specimens as well as two of two normal prostatic specimens were also found to contain rat EMBP-immunoreactive material. The unequivocal demonstration of the presence of a HEMBP is of great potential interest in consideration of estramustine phosphate (Estracyt) therapy against prostatic carcinoma. It is not inconceivable that the concentration of HEMBP in the carcinomatous tissue will be of significance in determining the drug uptake in the malignant tissue.
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PMID:Partial characterization and "quantitation" of a human prostatic estramustine-binding protein. 706 4

Three new potential biomarkers--PAC, PMA, and the 7E11-C5 glycoprotein--have been identified. All three have unique features that could augment current diagnostic and therapeutic modalities. Some of the important characteristics of these potential markers are summarized in Table 1. Further studies will be required to determine if any of them will provide clinical information beyond that provided by PSA and if they will have a significant impact on the management of patients with prostate cancer. The MAb 7E11-C5 (CYT-356), now in clinical trials, promises to offer new strategies for radioimmunodetection and radioimmunotherapy of prostate cancer.
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PMID:Biomolecular and clinical characteristics of PSA and other candidate prostate tumor markers. 750 67


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