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)

Palliative hormonotherapy is the choice treatment for disseminated prostatic cancer. The response rate oscillates between 80% and 90% and the mean probability of life expectancy exceeds two years with a substantial improvement in life quality. Hormone dependence of prostate cancer depends as a last instance on the existence of cellular clones with different sensitivity. Finally, the serial monitoring with the specific prostatic antigen allows an objectivation of the response and the early detection of the hormone refractory status.
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PMID:[Hormone therapy in prostate cancer: clinical results]. 169 93

Gamma-seminoprotein (gamma-Sm), a potential new marker for prostate cancer, has been evaluated with a sandwich-type enzyme immunoassay (EIA). This assay system has been confirmed to have a sensitivity and detectable range of 3.0 and 3.0-100 ng/ml, respectively, with a high reproducibility (approximately equal to 6% coefficient of variation between assays). A total of 256 serum samples were drawn from normal Japanese subjects for detection of gamma-Sm. Serum gamma-Sm was undetectable (less than 3.0 ng/ml) in 26 samples from 26 females. In 230 male cases, serum gamma-Sm levels ranged from less than 3.0 to 4.0 ng/ml. These values were not related to age. An upper normal limit of 3.6 ng/ml was calculated for 99 percentile Japanese males (n = 103) over 50 years of age. Serum gamma-Sm was detected in 192 untreated male patients with urological diseases. Gamma Sm levels (mean +/- SD) in each disease were as follows: prostate cancer (n = 64) 11.0 +/- 17.9 ng/ml; benign prostatic hypertrophy (n = 50), 3.02 +/- 0.113; bladder cancer (n = 58), 3.13 +/- 0.514; and renal adenocarcinoma (n = 30), 3.26 +/- 1.01. Serum gamma-Sm levels were statistically higher (p less than 0.05) in the prostate cancer group, however, there was no statistical difference in gamma-Sm levels among clinical stages or histopathologic grades. Furthermore, serum gamma-Sm values showed no correlation (r = 0.3870) with prostatic acid phosphatase (PAP), but were slightly correlated to prostate antigen (PA) levels (r = 0.6980) in patients with prostate cancer. These results suggest that gamma-Sm is a potential tumor marker of prostate cancer and that serially detected serum gamma-Sm levels could be used to monitor the disease.
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PMID:Clinical evaluation of gamma-seminoprotein in prostate cancer. 242 39

For production of monoclonal antibodies (McAbs), hybrid cells were prepared by fusion of spleen cells of BALB/c mice immunized with the human prostatic cancer cell line PC-82 and the P3-X6(3)Ag8.653 murine myeloma cell line. Supernatants of approximately 500 hybrid clones were screened for prostate specific antibodies using an ELISA on PC-82 cells. A selection of antibodies was further tested for their specificity on a large series of different tissues. A broad cross reactivity pattern was obtained. Most cross reactivity was with pancreatic tissue, kidney, and bowel. One antibody turned out to react with prostate stromal cells. Two McAbs (ER-Pr 1 and ER-Pr 2) reacted solely with prostatic epithelium. Monoclonal antibody affinity chromatography combined with SDS-PAGE showed that both antibodies were directed against a 35-kD protein. Immunoblotting revealed that this protein is identical to prostatic antigen (PA). The epitope detected by ER-Pr 1 and ER-Pr 2 was largely preserved after formalin-fixation of prostatic tissues which renders these antibodies very suitable for routine examination of tissue sections.
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PMID:Characterization of monoclonal antibodies raised against the prostatic cancer cell line PC-82. 242 90

The authors review recent developments in the immunodiagnosis of prostatic cancer. Monoclonal antibodies to prostatic acid phosphatase, prostate-specific antigen, and several human prostate and prostate-cancer-related components are available. Prostatic acid phosphatase and prostatic antigen assays are still the only immunologic tools with clinical applications.
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PMID:Immunologic markers and the diagnosis of prostatic cancer. 620 6

Current imaging modalities used to stage prostate cancer clinically fail to detect extracapsular disease in a significant subset of patients. A molecular based peripheral blood assay using the reverse transcriptase polymerase chain reaction has recently been shown to be a highly sensitive staging modality for detecting extraprostatic disease preoperatively. The assay uses primers that are specific for prostate specific antigen (PSA). We compare the application of the reverse transcriptase polymerase chain reaction assay using primers specific for the human prostate specific membrane antigen with results obtained from the same specimens by reverse transcriptase polymerase chain reaction for PSA. Prostate specific membrane antigen, a recently cloned prostatic antigen, is a transmembrane glycoprotein that has been described as prostate specific. These assays were applied to ribonucleic acids extracted from the peripheral blood lymphocyte fraction of 80 patients with clinically localized prostate cancer. In addition, blood specimens from 20 female patients, 20 young male patients, 25 age-matched control men under treatment for benign prostatic hypertrophy and 20 men with established, untreated metastatic prostate cancer were tested. All 3 groups of noncancer patients had negative polymerase chain reactions for PSA as well as prostate specific membrane antigen. Of 20 metastatic prostate cancer patients 16 (80%) had positive polymerase chain reactions for PSA, while only 10 (50%) had positive results for prostate specific membrane antigen. Among the 80 patients with clinically localized disease (stages T1 to T2cN0M0), 27 and 19 had positive polymerase chain reaction for PSA and prostate specific membrane antigen, respectively, from blood specimens obtained preoperatively. Analyzing the final pathology in each patient with the reverse transcriptase polymerase chain reaction assay identified a significantly stronger correlation with tumor invasion using the results of the PSA test rather than the results of the prostate specific membrane antigen reverse transcriptase polymerase chain reaction test (67% versus 34% sensitivity for detecting capsular penetration, 87% versus 46% sensitivity for detecting disease to the surgical margin and 83% versus 16% sensitivity for detecting seminal vesicle invasion). In contrast to the reverse transcriptase polymerase chain reaction assay for PSA, a similar assay done for prostate specific membrane antigen did not correlate with pathological stage of prostate cancer.
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PMID:Molecular staging of prostate cancer. II. A comparison of the application of an enhanced reverse transcriptase polymerase chain reaction assay for prostate specific antigen versus prostate specific membrane antigen. 753 52

Between October 1990 and June 1993, 112 patients underwent fine needle aspiration cytology and core needle biopsy of the prostate under transrectal ultrasonographic guidance. They were suspected of having prostatic cancer from the prostatic antigen level, digital rectal examination and/or transrectal ultrasonography. Twenty seven of the 112 cases (24%) were diagnosed with prostatic cancer. Their cytological diagnoses showed 22 class IV or V, 2 class III, and 3 class I or II. Efficiency, false negative rate and false positive rate were 86%, 11% and 0% in fine needle aspiration cytology. We could obtain sufficient samples for fine needle aspiration cytology in all cases. No severe complication was observed. However, we missed 3 patients, in fine needle aspiration cytology, who were strongly suspected of having prostatic cancer, and reexamination or additional core needle biopsy would have been necessary on 15 of the 112 patients (13%) who showed false negative or class III cytological results, if we had screened prostatic cancer only by fine needle aspiration cytology. In conclusion, fine needle aspiration cytology may not be as useful as core needle biopsy to screen prostatic cancer.
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PMID:[Fine needle aspiration cytology in screening of prostatic cancer]. 754 Nov 80

Gamma-seminoprotein (gamma-Sm) is one of the serine proteinases in seminal plasma, and is well known as a tumor marker of prostate cancer. In the blood, a major portion of gamma-Sm combines with alpha 1 antichymotrypsin (ACT), a serine proteinase inhibitor. We developed a sensitive enzyme immunoassay (EIA) for the gamma-Sm-ACT complex using two different monoclonal antibodies (MoAbs). One MoAb, prepared against gamma-Sm, is used for the capture, and the other, prepared against ACT, is conjugated with horseradish peroxidase and used for detection. The detectable range of this assay in clinical applications was from 0.2 to 50 units/ml. The intra-assay coefficients of variation (CV%) obtained from ten repeated assays of three sera were 3.6 to 5.5%. The mean gamma-Sm-ACT complex concentration in the sera of normal individuals was determined to be 0.86 +/- 0.11 units/ml for males (n = 50) and 0.11 +/- 0.08 units/ml for females (n = 54). There was no significant increase in the level of the complex with increasing age in males. The ratio of the gamma-Sm-ACT complex to free gamma-Sm tended to be significantly higher in patients with prostate cancer than in those with benign prostatic hyperplasia.
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PMID:[Specific quantification of gamma-seminoprotein-alpha 1 antichymotrypsin complex in serum by monoclonal antibody-based enzyme immunoassay]. 855 80

The human kallikrein family consists of three members, hK1, hK2, and hK3 [prostate-specific antigen (PSA)]. PSA is a widely accepted marker for prostate cancer. The mRNAs for both hK2 and PSA are localized predominantly to prostate epithelium and are regulated by androgens. In addition, hK2 has 78% amino acid homology to PSA. Although similarities to PSA make hK2 a potential prostate cancer marker, they also impede biochemical characterization of hK2 in those human tissues and body fluids where PSA is abundant. To study the expression, biosynthesis, and processing of hK2, recombinant hK2 was expressed in the adenovirus-induced Syrian hamster tumor cell line AV12-664 (AV12-hK2). Expression of hK2 was analyzed by Western blots and ELISA using monoclonal antibodies HK1G 464.3 [specific for prohK2 (phK2)] and HK1D 106.4 [specific for phK2 and mature hK2 (hK2)1. Western blot and ELISA analyses showed that phK2 was secreted into the media by AV12-hK2 cells on day 1 and was gradually converted to the mature form of hK2 by day 7. N-terminal amino acid sequencing verified the Western blot and ELISA data. This demonstrates for the first time that hK2 is secreted as phK2 and converted to hK2 extracellularly. In addition, hK2 detected in day 4-7 AV12-hK2-spent media was enzymatically active. Recombinant hK2 was also expressed in human prostate carcinoma cell lines, PC3 (PC3-hK2) and DU145 (DU145-hK2), that do not express endogenous hK2 or PSA. Similar to AV12-hK2 cells, both cell lines secreted phK2 that was converted to hK2 extracellularly. phK2 was the major form detected in the spent media of PC3-hK2 cells, even after 7 days, indicating a slow conversion of phK2 to hK2. hK2 was the predominant form detected in the spent media of DU145-hK2 starting on day 1, indicating the rapid conversion of phK2 to hK2. In this study, we demonstrate that hK2 exists in different forms and is secreted as phK2. phK2 is then converted to enzymatically active hK2 extracellularly.
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PMID:Expression of human glandular kallikrein, hK2, in mammalian cells. 896 92

The development of monoclonal antibodies directed against prostatic kallikrein hK2 prompted us to evaluate its content, along with that of hK3 (prostate-specific antigen), in human prostate carcinoma. Seventy tumors categorized according to the M.D. Anderson Hospital classification (grade I to IV) were analyzed by immunohistochemistry. The staining intensity or the kallikrein content of benign prostatic hyperplasia glandular tissue (used as control) and of grade I tumors appeared similar. In grade II to IV tumors, histochemical data revealed highly variable hK2 or hK3 content in approximately 25% of tumors. Such patterns are consistent with a current observation related to heterogeneity of prostate tumors. In addition, a few tumors did not express hK3 (n = 3), hK2 (n = 3), or both (n = 3), indicating that some growth patterns of prostatic neoplasia are associated with a lack of secretion or storage of hK3 or hK2 for immunodetection. This statement also appears relevant to metastases. It was interesting to note that 4% of hK3-negative tumors had detectable hK2. Because of the importance of hK3 as a serum marker of prostate disorder, this study addresses for the first time the question of the relative importance of both hK3 and hK2 in the immunohistochemical diagnosis of prostatic tumors. We conclude that hK2 may add new information to prostate cancer diagnosis and characterization.
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PMID:Immunohistochemical study suggesting a complementary role of kallikreins hK2 and hK3 (prostate-specific antigen) in the functional analysis of human prostate tumors. 903 61

Our work was undertaken to compare the relative efficiency of 2 purified prostatic kallikreins, namely, hK2 and prostate-specific antigen (PSA or hK3), in the activation of single-chain urokinase (scuPA). We found that hK2 converts scuPA into an active enzyme with an efficiency equal to approximately 1/50 that of plasmin. During the activation of scuPA by hK2, two fragments of 33 and 22 kDa were generated. The NH2-terminal amino acid sequence of the 33 kDa fragment showed that hK2 cleaved scuPA between Lys158 and Ile159. In contrast to a previous report by another group, our purified hK3 preparation containing no trypsin-like contaminants was totally unable to activate scuPA. Our results show that kallikrein hK2 has plasmin-like activity and suggest that it could be the initiator of a proteolytic cascade leading to prostatic cancer invasion.
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PMID:Prostatic kallikrein hK2, but not prostate-specific antigen (hK3), activates single-chain urokinase-type plasminogen activator. 918 Jan 62


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