N-acetyl-beta-D-glucosaminidase (NAG) activity in human semen: its relation to gamma-glutamyl transpeptidase (gamma-GTP) activity in seminal plasma and reproductive tissues, and relation between seminal mucoprotein concentration and seminal NAG, and gamma-GTP activities

N-Acetyl-beta-D-glucosaminidase (NAG) and gamma-glutamyl transpeptidase (gamma-GTP) activities in seminal plasma obtained from male infertile patients and these activities in reproductive tissues obtained from cryptorchids and patients with bladder tumors were studied. Seminal mucoprotein concentration was also measured. The mean NAG and gamma-GTP activity in seminal plasma was 2,092 +/- 794 mU/ml and 10,942 +/- 4,179 mIU/ml, respectively. The mean seminal mucoprotein concentration was 28.0 +/- 5.7 mg/ml. In seminal plasma, a significant correlation was obtained between NAG and gamma-GTP (p less than 0.001). and between gamma-GTP and mucoprotein concentration (p less than 0.05). However, there was no correlation between NAG and mucoprotein concentration. In the reproductive tissue high gamma-GTP activity was observed in the testicular tissue and in the external gland of the prostate. The activity in the epididymis was higher in the tail than in the head. High NAG activity was observed in the epididymal head and in the internal gland of the prostate. In the testicular tissue, NAG activity was low. These findings showed that in the seminal plasma NAG and gamma-GTP activities were closely related but in the reproductive tissue, these activities located in different areas.     

Human chorionic gonadotropin beta-subunit in human semen

The level of human seminal chorionic gonadotropin beta-subunit (hCG beta) was determined by radioimmunoassay (RIA). The mean hCG beta level in 34 normal men was 3.7 +/- 1.6 ng/ml, which was much higher than that in serum. The mean hCG beta level for 20 patients with mild oligozoospermia (20-39 x 10(6) sperm/ml) was 2.5 +/- 0.8 ng/ml, that for 34 patients with severe oligozoospermia (1-19 x 10(6) sperm/ml) was 1.7 +/- 0.5 ng/ml, and that for 21 azoospermia was 1.5 +/- 0.6 ng/ml. Thus, the decrease of sperm count was correlated with the decrease of hCG beta. In 17 cases to which testicular biopsy was applied together with sperm counting, the seminal hCG beta level was found to positively correlate with the germinal cell index (the ratio germinal cell count/Sertoli cell count) and with the testicular volume. The level of seminal hCG beta was also found to correlate negatively with the levels of seminal LH and FSH and positively with the level of seminal testosterone. These findings suggest that the production of seminal hCG beta is a process of spermatogenesis and closely related to spermatogenesis. The level of hCG beta in serum was too low to detect, and no relation to that in seminal plasma could be investigated. However, in 6 cases with testicular tumor, the hCG beta level in serum was high, whereas that in seminal plasma was rather low probably because of unilateral secretion. Enhanced production of hCG beta by tumor tissues and the destruction of the blood-testis barrier by proliferation of tumor cells seemed to be one of the causes of this high hCG beta level in serum. The hCG beta levels in 13 vasectomized seminal plasma and the prostatic fluid samples collected from 3 normal men were 1.5 ng/ml, which was similar to those in azoospermic patients. These findings suggest that the seminal hCG beta level consists of the hCG beta secreted by the testis and about 1.5 ng/ml of hCG beta from the prostate. Based on these results, seminal hCG beta is thought to be secreted by the prostate and the process of spermatogenesis and the value of seminal hCG beta may serve as an effective index for the testicular function.     

Fibrinolytic parameters in spermatozoas and seminal plasma

Urokinase-type (u-PA) and tissue-type plasminogen activator antigen (t-PA) as well as plasminogen activator-inhibitor activity were determined in seminal plasma and lysates of the respective spermatozoas in 67 ejaculate of males in infertile marriage without genito urinary pathology. U-PA was determined by a competition RIA, t-PA by an ELISA and PAI by a spectrophotometric assay. 15 patients showed normozoospermia, 11 azoospermia and 41 oligoasthenoteratozoospermia (OAT-syndrome). In lysates of spermatozoas, significantly higher levels of both plasminogenactivators and PAI were found in patients with OAT syndrome as compared to those exhibiting normozoospermia. Whereas PAI was absent in the seminal plasma of normozoospermic ejaculate, patients with azoospermia (180 +/- 13 mU/ml.) and OAT-syndrome (60 +/- 5 mU/ml.) showed high PAI levels. The similarly high values of t-PA (190.8-227.8 ng./ml.) and u-PA (19.4-32 ng./ml.) in the same compartment confirm their predominantly prostatic origin and seem to have no influence on the quality of the ejaculate.     

The major 40-kDa glycoprotein in human prostatic fluid is identical to Zn-alpha 2-glycoprotein

A major 40-KDA protein secreted by human prostate was isolated from whole seminal plasma by sequential column chromatography on DEAE-Sepharose CL-6B, concanavalin A(Con A)-Sepharose, and Sephadex G-100. Although the purified preparation still contained minor contaminants, its amino acid composition was found to be identical to the one of a glycoprotein isolated previously from seminal plasma by Lin et al (1983). Antibodies against this protein were produced in rabbits and their use in immunoblotting experiments revealed the presence of the antigen in several tissues including the prostate, the liver, the heart, the kidney, the epididymis, and the testis. A radioimmunoassay confirmed these results and showed that blood serum concentrations of this protein were relatively high in men (81 +/- 3 micrograms/ml), women (68 +/- 3 micrograms/ml), and cord blood of newborns (32 +/- 1 micrograms/ml). The serum concentrations of this protein along with its physicochemical characteristics suggested that it could be identical to Zn-alpha 2-glycoprotein, a human serum protein previously isolated by Burgi and Schmid (1961). This hypothesis was confirmed by a double immunodiffusion analysis using a commercial anti-Zn-alpha 2-glycoprotein antiserum. Finally, in vitro translation of prostatic poly(A) + RNA in rabbit reticulocyte lysate in the presence of canine pancreatic microsomal membranes resulted in the formation of an immunoprecipitable 42-kDa band. These results show that Zn-alpha 2-glycoprotein can be synthesized in the prostate itself. The demonstration of high concentrations of this protein in prostatic tissue and prostatic secretion should facilitate the elucidation of its role in the prostate and in other tissues.     

Isolation from human seminal plasma of an abundant 16-kDa protein originating from the prostate, its identification with a 94-residue peptide originally described as beta-inhibin

In addition to other known markers of the human prostate, it was shown that the prostatic fraction of the split ejaculate was rich in a 16-kDa protein with properties not described previously. This protein was purified from human seminal plasma using ammonium sulfate precipitation, DEAE-Sepharose CL-6B ion exchange chromatography, and gel filtration on Sephadex G-100. The purified protein showed a single prominent spot on two-dimensional gel electrophoresis. The sequence of the first 40 amino acids that could be positively identified was identical to that of a prostatic secretory protein of 94 amino acids (PSP94) previously designated as beta-inhibin. Antibodies produced in rabbits against the purified protein were used to develop a radioimmunoassay. These antibodies appeared to recognize only the NH2-terminal portion of the native molecule since they did not react with a synthetic peptide composed of the 28 C-terminal residues. The radioimmunoassay showed that the concentration of the protein was 1320 +/- 183 micrograms/ml in the seminal plasma of adult fertile men and 1134 +/- 136 micrograms/ml in vasectomized patients. In hypertrophic and adenocarcinomatous prostates, the concentrations were 326 +/- 156 and 104 +/- 23 micrograms/ml, respectively, while values were lower than 0.060 micrograms/ml in the testis, epididymis, vas deferens and liver. The blood plasma concentration was 0.019 +/- microgram/ml in 23 asymptomatic men 45 to 65 years old and 0.115 +/- 0.036 microgram/ml in eight patients with prostate cancer.(ABSTRACT TRUNCATED AT 250 WORDS)     

Josamycin Concentration in Human Ejaculate and its Influence on Sperm Motility/Josamycinkonzentrationsbestimmung in menschlichem Ejakulat und deren Einfluß auf die Spermienmotilität

The concentration of josamycin was determined in the split ejaculate of 5 volunteers after oral administration for several days. One aim of this investigation was to examine the penetration of the macrolide antibiotic into the prostate and the seminal vesicles. 2.23 +/- 1.8 micrograms/ml josamycin was found in fraction I of the ejaculate, consisting mostly of prostatic secretion, and 1.56 +/- 1.37 micrograms/ml josamycin in fraction II comprising mainly secretions from the seminal vesicles. The concentrations of josamycin found in both fractions of the ejaculate are clearly comparable with serum levels of the antibiotic. Josamycin thus attains concentrations in the prostate and seminal vesicles which are effective against Mycoplasma and Chlamydia, pathogens of increasing importance in infections of the urogenital tract. In vitro studies on samples from 30 andrological patients showed that josamycin (0.5 micrograms/ml) did not impair, but even increased the motility of spermatozoa (p less than or equal to 0.01). On the basis of these results josamycin is recommended for the treatment of andrological patients. In particular, the specific antibacterial spectrum also indicates the use of this antibiotic for treatment of the partner when children are desired. The usual precautionary measures for pregnancy must then be adhered to.     

Two-dimensional electrophoresis of proteins in various fractions of the human split ejaculate

Two-dimensional electrophoresis of six fractions of split ejaculates from normal men (median age 23 years, n = 6) revealed large differences in the pattern of proteins found between the prostate-enriched fractions and secretions associated with the seminal vesicles. The glandular contributions were assessed using the concentrations of spermine, zinc and prostatic acid phosphatase (PAP) for prostatic secretion, and fructose and prostaglandin E for seminal vesicle secretion in the various fractions. Aside from PAP, four additional proteins were apparently associated with the prostatic fraction, one of which shared the biochemical characteristics of the specific ventral lobe protein of the rat prostate, prostatein (molecular mass 16 000, pI 4.8). The presumptive vesicular fractions contained a large number of low molecular mass proteins (10-20 000), with widely varying pI-values. The concentration of albumin and transferrin appeared to be highest in the sperm cell enriched fractions, indicating a major contribution to the ejaculate of testicular/epididymal origin.     

Origin of alkaline phosphatase of canine seminal plasma

The tissular origin of alkaline phosphatase was evaluated in canine seminal plasma. Alkaline phosphatase activity was most concentrated in the first fraction of the split ejaculate and was virtually undetectable in the third and fourth fractions. By contrast, arginine esterase, a known marker of dog prostatic secretion, was present in similar concentrations in all fractions of the split ejaculates analyzed by SDS gel electrophoresis. Similarly, arginine esterase was very abundant in secretory granules prepared from dog prostate homogenates, whereas these granules contained virtually no alkaline phosphatase. Among male sex accessory organs, alkaline phosphatase activity was very high in the epididymis and much lower in the testis and prostate. Furthermore, the specific activity in epididymal fluid collected from the cauda epididymis was about 10 times higher than in the corresponding epididymal homogenates. These results show that the major portion of alkaline phosphatase in dog seminal plasma does not come from the prostate but from the epididymis.     

Angiotensin converting enzyme in human seminal plasma is synthesized by the testis, epididymis and prostate

The activity of angiotensin converting enzyme (ACE) was assessed in human body fluids (serum, seminal plasma, prostatic secretions), in tissue extracts of the testis, epididymis, prostate and skeletal muscle, in split ejaculates and in seminal plasma obtained from patients before and after vasectomy. To ensure the specificity of the results the dependence of ACE activity on specific inhibitors was evaluated. Enzyme activity found in tissues of the male genital tract was considerably higher than that in serum and other tissues. ACE in human seminal plasma is synthesized by the testis, epididymis and prostate in different amounts.     

少弱精子症和正常生育男性精液中尿激酶及其受体含量的研究

目的:通过研究精子正常和异常男性精浆和精子中尿激酶及受体含量差异,以了解尿激酶及受体与男性生育力的关系。方法:采用双抗体夹心ELISA法测定22例正常生育男性和44例少弱精子症男性精浆和精子中尿激酶及受体的含量。结果:①正常男性精浆尿激酶平均含量为(4 803.69±602.78)mU/L,与少弱精子症组[(4 061.35±736.23)mU/L]相比,差异有显著性(P<0.01)。正常生育男性精子尿激酶平均含量为(30.29±3.16)mU/106个精子,与少弱精子症组[(20.51±4.2)mU/106个精子],差异有显著性(P<0.01)。②正常生育男性精子尿激酶受体平均含量为(12.97±3.11)mU/106个精子相比,与少弱精子症组[(6.09±1.45)mU/106个精子]相比,差异有显著性(P<0.01)。③精子和精浆中尿激酶含量和精子活率和活力呈显著正相关。结论:尿激酶和男性生育力相关,少弱精子症和正常生育男性精液中尿激酶及其受体含量存在差异。     

SERUM AND SEMEN PROSTATE SPECIFIC ANTIGEN CONCENTRATIONS ARE DIFFERENT IN YOUNG SPINAL CORD INJURED MEN COMPARED TO NORMAL CONTROLS

PURPOSE: Recent investigations have indicated that factors within the seminal plasma may contribute to the condition of low sperm motility in men with spinal cord injury. To determine whether the prostate gland functions normally in these men we chose prostate specific antigen (PSA) as a marker of prostatic function, and compared serum and semen concentrations in spinal cord injured and healthy noninjured men. MATERIALS AND METHODS: The study included 21 spinal cord injured men (mean age 33.3+/-1.2 years) and 22 noninjured normal men (mean age 30.3+/-1.5 years). Blood was obtained from subjects following at least 24 hours of abstinence from ejaculation and serum PSA was determined by modified enzyme immunoassay. Antegrade ejaculates from all subjects were frozen to -80 C, exactly 15 minutes after collection. Seminal plasma PSA was determined using Hybritech Tandem MP assay. RESULTS: Mean serum PSA concentration was 1.20+/-0.19 ng./ml. in spinal cord injured and 0.69+/-0.07 ng./ml. in noninjured men (p<0.02). Mean seminal plasma PSA concentration was 0.59+/-0.11 mg./ml. in spinal cord injured and 1.29+/-0.15 mg./ml. in noninjured men (p<0.001). CONCLUSIONS: Our findings of elevated serum and decreased seminal plasma PSA concentrations indicate that prostatic secretory dysfunction is present in men with spinal cord injury.     

Selenium, rubidium and zinc in human semen and semen fractions

The levels of selenium, rubidium and zinc were determined in samples of semen, seminal plasma and spermatozoa from men with suspected infertility, together with several parameters of semen quality. The proportion of whole semen selenium present in sperm increased with increasing sperm count from 0 to 40%. For rubidium 98 +/- 4% and for zinc 95 +/- 8% of the total amount in semen was contained in seminal plasma. In seminal plasma a positive correlation was found between the levels of zinc and selenium, and between the levels of zinc and rubidium, indicating that, like zinc, selenium and rubidium in seminal plasma also derive mainly from the prostate gland. Semen quality parameters, such as sperm motility, vitality, speed and morphology, were not correlated with the contents of the three elements in either whole semen or seminal plasma. As the seminal content of selenium is dependent on the proportion of prostatic secretion in seminal plasma and on the sperm count, and both factors can vary considerably, the selenium level of whole semen does not appear to be a suitable parameter for investigation of the relationship between selenium and semen quality. Provisional measurements suggest lower sperm selenium levels at abnormally low or high sperm counts.     

On the origin of prostaglandins in human seminal fluid

To evaluate the origin of seminal prostaglandins, genital tract fluids were analysed for prostaglandin content in two clinical situations. Six patients delivered semen samples before and after vasectomy. In these patients the prostaglandin concentration remained essentially unchanged although sperm density decreased to zero. In another patient secretory products from the testis and epididymis, and the ejaculate representing mainly the secretion of the seminal vesicles and the prostate gland, were collected separately. Secretions obtained from the testis and epididymis did not contain detectable amounts of prostaglandins, whilst in the ejaculate from the same patient the concentration was within normal limits. The results of the study show that the testis and epididymis do not contribute significantly to the prostaglandin content of human seminal fluid. The previous assumption that the seminal vesicles are the main source of seminal prostaglandins is thus supported.     

Zinc binding to major human seminal coagulum proteins

In vitro binding of zinc to proteins of the human ejaculate and of the various male accessory gland secretions was evaluated. The proteins were separated by sodium dodecyl sulfate gel electrophoresis and transferred to nitrocellulose filters that were subsequently incubated with 65ZnCl2. High levels of zinc binding were observed to approximately 20 protein bands (14 to 70 kDa) of the coagulated seminal plasma. There was only low binding to proteins of the spermatozoa and virtually no binding to any protein of the epididymal and prostatic fluids. When sperm liquefaction was allowed to occur, 65ZnCl2 binding to high-molecular weight proteins decreased rapidly, and after 15 min only the binding to proteins of molecular weights less than 25 kDa remained. In addition, zinc concentration was determined both in the centrifugate and in the supernatant after centrifugation of the coagulum. Zinc concentrations in the centrifugate and the supernatant were, respectively, 147 +/- 72 micrograms/g and 31 +/- 22 micrograms/g. The whole supernatant contained only 12% +/- 4% of total sperm zinc. Finally, in highly viscous sperm samples the concentration of zinc was not significantly different from that in normally liquefying sperm (167 +/- 87 micrograms/ml compared to 188 +/- 107 micrograms/ml). The main extracellular targets of prostatic zinc in humans are the secreted seminal vesicle proteins. The role of this binding remains unknown, however, because no direct relationship could be established between the concentrations of this metal and the phenomena of coagulation and liquefaction.     

Activity of testis angiotensin converting enzyme (ACE) in ejaculated human spermatozoa

Testicular angiotensin converting enzyme (ACE) isozyme is likely to play important functional roles in male reproduction. Several studies have shown that ACE is released from human spermatozoa during capacitation and that ACE is associated with reduced sperm motility. Recently, we established an assay to detect testicular ACE activity in human spermatozoa. The purpose of this study was to determine if testicular ACE activity is related to sperm motility in human ejaculates. Semen samples were collected from 80 infertile patients. According to the semen characteristics, they were divided into four (WHO) categories. Enzyme activities of ACE in spermatozoa (testicular ACE) and seminal plasma (somatic ACE) were spectrophotometrically determined. Total testicular ACE activity in spermatozoa was measured by solubilization of spermatozoa with Triton X-100. Membrane testicular ACE activity was measured in a sperm : PBS suspension. Sperm concentration and sperm motility were 136.6 +/- 154.1 x 10(6)/mL and 58.6 +/- 23.4%, respectively (mean +/- SD). Enzyme activities of membrane testicular ACE, total testicular ACE and somatic ACE were 0.273 +/- 1.219 microU/10(6) spermatozoa, 0.35 +/- 1.34 microU/10(6) spermatozoa and 684.7 +/- 226.6 mU/mL, respectively. A negative correlation was observed between sperm motility and membrane testicular ACE activity (p < 0.05). Membrane testicular ACE activity in 44 normal semen samples was 0.04 +/- 0.02 microU/10(6) spermatozoa, whilst that in 36 abnormal semen samples was 0.24 +/- 0.42 microU/10(6) spermatozoa. There was a significant difference between these two groups (p < 0.01). Membrane testicular ACE in sperm samples from normozoospermic men was significantly lower than that from oligoasthenozoospermic men (p < 0.05). These findings suggest that testicular ACE is released from normal functional spermatozoa for them to have fertilizing ability.     

Study of N-acetyl-beta-D-glucosaminidase (NAG) activity in the human semen

NAG activity in the human semen was measured using NAG kit. Plasma NAG activity in the semen was more than 500 times higher than that of urine, while in sperm, NAG activity was low. In a frozen condition, NAG activity in semen plasma did not change for more than five weeks. NAG activity in semen plasma of male infertility associated with oligozoospermia was 1,918 +/- 829 (M +/- S.D.) mU/ml. Among the reproductive tissue, high NAG activities were observed in epididymis and prostate. Our present study suggests that NAG in semen plasma must possess some active roles related to sperm maturation and/or sperm motility or both.     

Immunoassayable Somatomedin C in seminal plasma of azoospermic men

Somatomedin C is a Sertoli cell peptide and since measurements of other Sertoli cell products in semen have provided a useful indices of testicular function, it was considered pertinent to measure the semen levels of Somatomedin C. Somatomedin C was measured by RIA in seminal plasma of vasectomized subjects (n = 18), subjects with agenesis of the seminal vesicles and vasa deferentia (n = 6) and subjects with azoospermia resulting from seminiferous tubule damage without obstruction (n = 23). Normal fertile subjects (24 men with a sperm concentration greater than 20 X 10(6)/ml) were used as controls. In all subjects, seminal levels of transferrin were also measured as an index of Sertoli cell function. The majority of seminal Somatomedin C appears to derive from the testis and/or epididymis. However, in several normal controls seminal levels of Somatomedin C (median = 3.52; range = 1.10-15.67 U/ejaculate) were found to be within the range for vasectomized subjects (median = 0.78; range = 0.46-4.20 U/ejaculate). In subjects with azoospermia the seminal levels of Somatomedin C (median = 2.06; range = 0.60-10.12 U/ejaculate) were significantly lower (P less than 0.02) than in fertile controls. However, values for these two groups overlapped. It is concluded that Somatomedin C in semen is not a reliable index of seminiferous tubule function and does not appear to be of diagnostic value in male infertility.     

Evaluation of the effect of experimental cyclosporine toxicity on male reproduction and renal function. Reversal by concomitant human chorionic gonadotropin administration

Administration of cyclosporine to rats has been shown to impair testicular function, resulting in a decrease in sperm counts and fertility. In order to determine whether or not the deleterious effects of CsA could be reversed by hormonal therapy, mature male Sprague Dawley rats were treated with CsA (40 mg/kg/day, s.c.) alone or in combination with human chorionic gonadotropin (hCG) (5 micrograms/day/r; s.c.) for 14 days. Cyclosporine administration decreased the body weight (290 +/- 5.30 vs. 339 +/- 8.7 g; P less than 0.05) and reproductive organ weights (testis 1.49 +/- 0.42 vs. 1.60 +/- 0.03 g; epididymis 0.41 +/- 0.02 vs. 0.49 +/- 0.002 g; seminal vesicle 0.61 +/- 0.09 vs. 1.60 +/- 0.05 g; prostate 0.28 +/- 0.04 vs. 0.60 +/- 0.06 g; P less than 0.05) testicular sperm counts (5.80 +/- 0.42 vs. 8.49 +/- 0.48 x 10(7)/100 mg tissue; P less than 0.05) and epididymal sperm counts, (28.2 +/- 0.95 vs. 51 51.62 +/- 2.17 x 10(7)/100 mg tissue; P less than 0.05) and fertility (25% vs. 100%). Serum levels of LH were elevated (101.98 +/- 21.48 vs. 25.6 +/- 5.18 ng/ml; P less than 0.05) and testosterone was decreased (0.48 +/- 0.07 vs. 2.06 +/- 0.56 ng/ml; P less than 0.05). The administration of hCG to the CsA-treated rats restored the reproductive organ weights (testis 1.56 +/- 0.043 g; seminal vesicle 1.04 +/- 0.05 g; prostate 0.70 +/- 0.06 g) and sperm counts (testicular 7.88 +/- 1.0 x 10(7)/100 mg tissue; epididymal 59.86 +/- 4.16 x 10(7)/100 mg tissue; P less than 0.05) Serum levels of testosterone (18.63 +/- 4.45 ng/ml) and LH (431.65 +/- 31.41 ng/ml) were significantly elevated, as compared with control and CsA-treated groups (P less than 0.05). All the rats in the gonadotropin-treated group were fertile, as compared with 25% in the CsA-treated group. CsA reduced the kidney weight (1.17 +/- 0.02 vs. 1.27 +/- 0.03 g; P less than 0.05) and increased the levels of serum creatinine (0.97 +/- 0.07 vs. 0.59 +/- 0.03 mg/dl; P less than 0.05): these changes were ameliorated by the administration of hCG (kidney weight 1.35 +/- 0.03 g; creatinine 0.76 +/- 0.09 mg/dl).     

Testicular function in potential sperm donors: normal ranges and the effects of smoking and varicocele

Testicular exocrine (semen analysis) and endocrine (plasma LH, FSH, prolactin and testosterone) function was assessed in 119 consecutive healthy men presenting for screening as potential sperm donors. Since these volunteers were unbiased with respect to their fertility status, this sample of the general male population was suitable to determine normal ranges and the influence of a variety of physical (height, weight, standardized body weight, varicocele) and demographic (age, marital and fertility status, tobacco and alcohol consumption) factors on normal human testicular endocrine and exocrine function, without the confounding effects of bias in selection of subjects. The statistical distribution of all seminal parameters was non-gaussian, but cube-root transformation of the data normalized the distribution, allowing for parametric statistical analysis. The median (and 95% confidence limits) for the various semen parameters was 73.0 (10.6-235.3) million sperm per ml; 189.0 (12.6-868) million sperm per ejaculate; 50.4 (5.9-181.9) million motile sperm per ml; 133.0 (6.9-661.7) million motile sperm per ejaculate; 54.0 (7.0-172.9) million morphologically normal sperm per ml and 138.5 (7.5-672) million morphologically normal sperm per ejaculate. Testicular volume was correlated positively with measures of physique such as standardized body weight (r = 0.25, P less than 0.01) and body surface area (r = 0.30, P less than 0.002), and negatively with plasma levels of FSH (r = -0.31), P less than 0.002) but not LH. Sperm output was positively correlated with testicular volume (r = 0.28, P less than 0.005) and negatively correlated with plasma FSH (r = -0.31, P less than 0.002) and plasma LH (r = -0.31, P less than 0.002). Smoking was associated with a highly significant reduction in sperm output and motility. Men with varicocele (25%) were significantly taller, had slightly lower haemoglobin levels and moderate left (but not right) testicular atrophy, but neither seminal nor hormonal parameters were different from men without varicocele. There was no difference in any markers of human testicular function between men according to marital or fertility status, grades of moderate alcohol consumption or the presence of low titres of sperm antibodies.     

Kallikrein in the male reproductive system

Male genital organs were stained by the peroxidase-antiperoxidase (PAP) method to know the location of kallikrein. Sertoli cells of the testis, epithelial cells that existed from the body to the tail of the epididymis, and glandular cells of the prostate were specifically stained showing that kallikrein was produced in these cells. The concentration of kallikrein in the semen specimens mainly from patients with male sterility and from those who were subjected to vasoligation and in the prostatic fluid specimens from normal controls were measured by radioimmunoassay (RIA). The results of column chromatography suggested that kallikrein combined with the other substances to form a high molecular compound in the semen. The kallikrein level in the semen from the normal control was 40.4 +/- 21.3 ng/ml, which was more than 10 times that in the blood. The value tended to increase with the decrease of the number of spermatozoa. The kallikrein level in the semen from patients with azoospermia was 74.2 +/- 23.5 ng/ml, which was significantly higher than that of the normal control. There was no significant correlation between the kallikrein level and the sperm motility. The kallikrein level in the semen from the patients subjected to vasoligation, which did not contain the semen originated from the testis, and that in the prostatic fluid from the normal control were 20-28 ng/ml. That amount was considered to be secreted from the prostate. The oral administration of hog kallikrein tablet augmented seminal human kallikrein and Acid-P secretion. Moreover, an improvement of seminalysis was observed following long term administration of 600 U/day of hog kallikrein in the male infertile patients. This drug might be useful to treat the male infertile patients with this disorder.