PubMed · 4141077
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A Stepień, E Buczyński, M Lopuszyńska. [Chromolipids].. https://pubmed.ncbi.nlm.nih.gov/4141077/
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BACKGROUND: The incidence and mortality of prostate cancer are increasing at alarming rates, partially due to an aging population. Early detection of prostate cancer, using clinically sensitive procedures and/or tumor markers (e.g., prostate-specific antigen [PSA]), is of prime importance. However, the choice of therapeutic interventions for prostate cancer at the time of diagnosis is largely dependent on clinical and pathologic staging and prediction of the degree of aggressiveness of the disease. Clinically applicable prognostic markers are urgently needed to assist in the selection of optimal therapy. METHODS: Literature review of the potential diagnostic and prognostic markers for human prostate cancer. RESULTS: Well-established tissue prognostic indicators, including histologic grade, margin positivity, pathologic stage, intraglandular tumor extent, and DNA ploidy, are not reviewed in this paper. Recently, a number of novel markers have been identified. In this paper, we begin with a discussion of a number of well-established as well as investigational diagnostic markers and then focus on evaluation of prognostic markers. Diagnostic markers that have prognostic value and investigational prognostic markers are also discussed. CONCLUSIONS: Currently, only PSA is utilized for early diagnosis and monitoring of prostate cancer. A number of potential prognostic markers warrant further investigation. Multimarker analysis is implicated.
Activin A, a homodimer of the betaA subunit of inhibin, is a member of the TGF-beta family. It is a multifunctional molecule regulating the growth, differentiation, and survival of a variety of cells. Treatment with activin A to an androgen-sensitive human prostatic cancer cell line LNCaP resulted in growth and morphological change and those were accompanied by up-regulation of prostatic differentiation markers prostate-specific antigen (PSA) and prostatic acid phosphatase (PAP). In addition, the expression of androgen receptor was also enhanced by activin treatment. These results suggest that activin has significant influence on LNCaP cells.
Most newly synthesized lysosomal enzymes contain a transient carbohydrate modification, mannose 6-phosphate (Man-6-P), which signals their vesicular transport from the Golgi to the lysosome via Man-6-P receptors (MPRs). We have examined Man-6-P glycoproteins in human urine by using a purified soluble fragment of the soluble cation-independent MPR (sCI-MPR) as a preparative and analytical affinity reagent. In a survey of urine samples from seven healthy subjects, the pattern of Man-6-P glycoproteins detected with iodinated sCI-MPR as a probe in a blotting assay was essentially identical in each, regardless of sex or age. Two bands of approx. 100 and 110 kDa were particularly prominent. Man-6-P glycoproteins in human urine were purified by affinity chromatography on immobilized sCI-MPR. Seven distinct bands revealed by SDS/PAGE and Coomassie Blue staining were subjected to N-terminal sequence analysis. The prominent 100 and 110 kDa Man-6-P glycoproteins were identified as N-acetylglucosamine-6-sulphatase and alpha-glucosidase respectively. This identification was confirmed by molecular mass determinations on the two major bands after deglycosylation. Sequence analysis revealed arylsulphatase A and several previously unidentified proteins as minor species. Man-6-P glycoproteins were also purified on an analytical scale to determine the proportion of a number of lysosomal enzyme activities represented by the mannose-6-phosphorylated forms. The lysosomal enzymes in urine containing the highest proportion of mannose-6-phosphorylated form were beta-mannosidase (82%), hexosaminidase (27%) and alpha-glucosidase (24%). The profiles of Man-6-P glycoproteins detected by blotting in urine and plasma were not similar, suggesting that the urinary species are not derived from the bloodstream.