Purpose: We defined the yield and nature of prostate cancer in the setting of population based, randomized prostate specific antigen (PSA) guided screening in men with PSA levels between 3 and 4 ng./ml. who were 50 to 65 years old at the time of randomization. Materials and Methods: Sextant biopsies were performed in 243 men with PSA of 3 to 4 ng./ml. Therapy decisions were based on core cancer le

β-Microseminoprotein is a 10-kDa disulphide-rich protein with unknown function which is present in the mucus of the airways, gastrointestinal tract and urogenital tract. In this paper, an investigation of the distribution of β-microseminoprotein in the human stomach is reported. Immunohistochemistry and in situ hybridization were used. β-Microseminoprotein was found to be localized mainly in the a

Objectives. To study the in vitro stability of free and complexed forms of prostate specific antigen (PSA) in blood samples in order to establish guidelines for specimen handling, in particular for the clinical utility of the analysis of percentage free PSA. Methods. Blood samples were collected and processed to generate serum, heparin plasma, and EDTA plasma. Three different two-site immunoassays

Purpose: In most previous studies of free-to-total serum prostate specific antigen (PSA) ratios, the specimens from patients with prostate cancer or those with benign prostatic hyperplasia (BPH) have not been highly characterized. We compared preoperative sera from post-radical prostatectomy patients with clinically significant cancers of at least 2 cm.3 to sera from those with BPH and large, biop

Prostate-specific antigen (PSA), produced by prostate cells, provides an excellent serum marker for prostate cancer. It belongs to the human kallikrein family of enzymes, a second prostate-derived member of which is human glandular kallikrein-1 (hK2). Active PSA and hK2 are both 237-residue kallikrein-like proteases, based on sequence homology. An hK2 model structure based on the serine protease f

Semenogelin I and semenogelin II constitute the major gel-forming proteins in human semen. The gel proteins were rapidly solubilized and separated from spermatozoa in ejaculates collected at pH 9.7 in buffer containing 4 mol/l urea and dithiothreitol. This protected the semenogelins from proteolytic degradation by prostate-specific antigen, and allowed their isolation by affinity chromatograph:g o

Objectives. To discover whether the proteolytic activity of prostate- specific antigen (PSA) affects the structure and function of parathyroid hormone-related protein (PTHrP), as both are abundant components of human seminal plasma. Methods. The ability of PTHrP to act as a substrate was studied by incubating a synthetic polypeptide, consisting of 34 amino acid residues of the amino-terminal domai

ABSTRACT: The secretory function of the human prostate and the seminal vesicles is a prerequisite for gel formation and liquefaction of semen, but the relation to poor sperm motility and low sperm count in infertile men remains to be clarifyed. Our aim was to evaluate the secretory function of the prostate and the seminal vesicles in normozoospermic men (n=35) and in asthenozoospermic men, who wer

BACKGROUND: Lynch syndrome is a rare familial cancer syndrome caused by pathogenic variants in the mismatch repair genes MLH1, MSH2, MSH6, or PMS2, that cause predisposition to various cancers, predominantly colorectal and endometrial cancer. Data are emerging that pathogenic variants in mismatch repair genes increase the risk of early-onset aggressive prostate cancer. The IMPACT study is prospect

β microseminoprotein (β inhibin, PSP94), an unglycosylated protein of 94 amino acids with unknown function, is one of the predominating proteins in the secretion of the human prostate gland. In this work the authors have demonstrated that the expression of β microseminoprotein is not restricted to the prostate and that the protein has a previously unrecognized widespread occurrence in the human bo

Analyses of the proteins of azoospermic ejaculates from subjects with defective seminal vesicles demonstrated that three prostatic‐secreted proteins were predominant. Prostatic acid phosphatase (PAP), prostate‐specific antigen (PSA; or γ‐seminoprotein), and β‐microsemi‐noprotein (β‐MSP; or β‐inhibin), were identified as the three predominant proteins secreted by the normal human prostate gland. Im

The comparison of measurements of fibronectin and lactoferrin in ejaculates from vasectomized men, subjects with functional deficiency or aplasia of the seminal vesicles, and reference subjects provided evidence that both the fibronectin and the lactoferrin in human seminal fluid originate from the seminal vesicles and the ampullae. The fibronectin is incorporated in the framework of the seminal g

Prostatic acid phosphatase (PAP), prostate‐specific antigen (PSA), and β‐microseminoprotein (β‐MSP) were regularly localized immunohistochemically to the epithelium of the acini and that of the ducts in the nodules of 24 cases of benign prostatic hyperplasia. The immunohistochemical distribution of these three prostatic‐secreted proteins was also examined, with monoclonal antisera against PAP and

A 33-kD glycoprotein, known as the 'prostate-specific antigen', was purified to homogeneity from human seminal plasma. The prostatic protein was identified as a serine protease, and its NH2-terminal sequence strongly suggests that it belongs to the family of glandular kallikreins. The structural protein of human seminal coagulum, the predominant protein in seminal vesicle secretion, was rapidly cl

The predominant protein in human seminal vesicle secretion constitutes the structural protein of coagulated semen. This high molecular weight protein (HMW-SV-protein) is stable in seminal vesicle secretion during in vitro storage at 37 d̀C for at least 20 h, but is rapidly cleaved on mixing with prostatic proteases. Seminal coagulate, washed free of souble components, is dissoluble by 2 to 3 mol/1

Most of the γglutamyltransferase occurring in semen was found to be bound to the membranes of prostatic organelles, as is the case with Mg+plus;-Ca+plus;-dependent ATPase, and Zn+plus;-dependent peptidase hydrolysing succinyl (alanine)3-paranitroanilide. Organelie-bound γglutamyltransferase was released in a water-soluble form by papain. Charge shift electrophoresis revealed the presence in semina

Serum γ-glutamyltransferase (EC 2.3.2.2) showed microheterogeneity on electrofocusing, owing to variations in sialic acid content. We investigated the isoform patterns of papain-treated serum samples on agarose gels containing nonionic detergent and ampholytes in the low pH range. Serum from cases of cholestasis show seven bands with γ-glutamyltransferase activity. These same bands were also found

Normal post-ejaculatory proteolytic changes in human seminal plasma rapidly distort its electrophoretic protein pattern. This invalidates the electrophoretic evaluation of the content in the secretion from the accessory sex glands. Both agarose and sodium dodecylsulphate polyacrylamide gel electrophoresis (SDS-PAGE) were used to study the proteolytic changes and how they could be modified by vario