Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.15.1 (ACE)
 18,300 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The distribution of the angiotensin I converting enzyme (EC 3.4.15.1, ACE) in male reproductive systems of various vertebrates including non-mammalian species and properties of the genital ACEs were studied. In such mammals as rat, dog and pig, it has been found that ACE activity is only distributed in testis and epididymis (especially in the epididymal semen), but not in accessory sex glands such as prostate, seminal vesicle and coagulating gland. In the rat and dog, most of or all epididymal ACE has been found to resemble testicular ACEs rather than pulmonary ACE in molecular weight. Besides the studies on mammals, it has been found that the enzymes having characteristics of ACE are present in the genital systems of such lower vertebrates as bird (domestic fowl) and fish (carp).
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PMID:Distribution of angiotensin I converting enzyme in male reproductive systems of various vertebrates and properties of the genital enzymes. 255 11

Treatment with cadmium chloride (CdCl2) and cyproterone acetate (CA) depressed angiotensin converting enzyme (ACE) activity significantly in testes and epididymal regions of the adult rats compared to the corresponding untreated controls. Exogenous testosterone to CA-treated rats significantly increased the enzyme activity both in the testes and epididymis, the effect in the latter being very significant comparable to CA-treated and untreated controls. Testosterone failed to induce ACE activity in the testes and caput epididymis of 30 day-old immature rats, but the enzyme activity was detected in corpus and cauda epididymis. Our findings indicate that ACE activity in the testicular complex is possibly linked with androgen and is concerned with spermatogenesis and sperm maturation.
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PMID:Androgen dependence of testicular and epididymal angiotensin converting enzyme. 298 87

Angiotensin-converting enzyme (ACE, EC 3.14.5.1) is found in particulate fractions of the epididymis but not in soluble epididymal fractions or in the testis of 4-week-old rats. [3H]Captopril autoradiography of testis and epididymis from 4-week-old rats confirms the association of ACE with epididymal ducts but not the testis. ACE appears in the testis between 4 and 6 weeks of age. Soluble ACE is not detectable in the epididymis until 6-7 weeks of age. Within the epididymis, regions closest to the testis develop soluble ACE activity about 1 week before those nearest to the vas deferens. Hypophysectomy of 10 week-old-rats depletes greater than 95% of ACE activity from the testis and soluble fractions of the epididymis, with little change in ACE levels from particulate fractions of the epididymis. [3H]Captopril autoradiography after hypophysectomy reveals luminal and epithelial ACE in the epididymis. The presence of particulate ACE in the epididymis under conditions where there is no testicular ACE indicates that the two forms are synthesized separately. However, soluble ACE from the epididymis might be derived from the membrane-associated ACE of the testis. Such a relationship is supported by the lag of 1 week between the development of ACE in the initial segment of the epididymis and the tail of the epididymis, and by the occurrence of soluble epididymis ACE only in those animals with testicular ACE activity.
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PMID:Angiotensin-converting enzyme in the testis and epididymis: differential development and pituitary regulation of isozymes. 299 11

The localization of angiotensin converting enzyme (ACE) in the gonads of the normal rabbit was studied by immunofluorescence and immunoelectron microscopy. The enzyme is present in the cytoplasm of testicular spermatids and of epididymal and ejaculated spermatozoa, and on the surface of follicular and tubal oocytes. These findings support the hypothesis that ACE has a role in gamete maturation and in fertilization.
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PMID:Gametes contain angiotensin converting enzyme (kininase II). 300 98

The male reproductive tract contains two different isoenzymes of angiotensin I-converting enzyme (ACE), i.e., pulmonary and testicular ACE. The present study shows selectively the cellular distribution of the ACE isoenzymes in the reproductive tract of male rabbit, using indirect immunofluorescence or immunoperoxidase methods. Testicular ACE was found in the seminiferous tubules of the testes in spermatocytes containing mature spermatids, and in spermatids within the epididymal tubular lumen in sexually mature, but not in immature, rabbits. Epididymal tubular cells contained pulmonary ACE. In the young rabbit, epididymal tissue contained more ACE than that in adult rabbit, since ACE was observed in principal cells in addition to basal cells. In mature rabbit, ACE was observed in basal cells only. Strong staining for pulmonary ACE was observed in cells of the vas deferens in both young and adult rabbit. Therefore, synthesis of epididymal ACE, unlike the testicular isoenzyme, was not stimulated by sexual maturation. Enzymatically active ACE in seminal fluid corresponds to the pulmonary isoenzyme. The present study indicates that this seminal fluid ACE may originate from cells of the epididymal tubules, particularly those of the vas deferens. Endothelial cells of blood vessels lying in the interstitium of both testicular and epididymal tissue contained the pulmonary isoenzyme.
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PMID:Immunohistochemical localization of two angiotensin I-converting isoenzymes in the reproductive tract of the male rabbit. 300 4

The object of the present study was to characterize the selection-conditioned differentiation of the biological performance of laboratory mice having been selected for 13 generations at the age of 6 weeks to body mass (Du-6) as well as simultaneously to body mass and high physical capacity (Du-6 + LB) by parameters of fat metabolism. The improved physical capacity with unchanged body composition (Du-6 + LB) coincides with increasing activity of dehydrogenases supplying NADPH (glucose-6-phosphate-dehydrogenase, 6-phosphate-gluconate-dehydrogenase, NADP-malate-dehydrogenase, NADP-isocitrate-dehydrogenase) in the liver. The doubling of the fat content of the body (Du-6) was accompanied by a significant increase of the G-6-PDH- and fatty-acid synthetase activity in the fatty tissue. Furthermore, the growth-selected animals showed an intensified transformation of 14C-glucose substrate in the lipids of the epididymal fatty tissues occurring especially at the selection age (42nd day) as well as at the earlier date of ontogenesis (32nd day). The insulin stimulation capacity of the fat cells as to the glucose incorporation, however, remained unchanged.
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PMID:[Fat metabolism in growth-selected laboratory mice]. 354 Jun 77

A biochemical study has been made of the effects of low doses of alpha chlorohydrin on all the glycolytic enzymes and two key enzymes of phosphogluconate pathway i.e. glucose-6-phosphate dehydrogenase (G-6-PDH) and 6-phosphogluconate dehydrogenase (6-PGDH) of rat testis and epididymis. All the glycolytic enzymes of testis and epididymis are decreased after treatment with alpha chlorohydrin. G-6-PDH and 6-PGDH are decreased only in epididymis and not in the testis. LDH, ADH and glucose-6-phosphatase were also studied histochemically to show that the drug affects the glycolytic enzymes of epididymal cells and various testicular cell types of testis. Possible significance of these results is discussed.
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PMID:Effect of low doses of alpha chlorohydrin on the enzymes of glycolytic and phosphogluconate pathways in the rat testis and epididymis. 626 79

Testis and epididymis are known to have high amounts of angiotensin converting enzyme (dipeptidyl carboxypeptidase, EC 3.4.15.1). We investigated the localization of the enzyme in these tissues by an immunofluorescent technique and found that the enzyme was localized in the spermatids and residual bodies in the Sertoli cells of the testis. Furthermore, the enzyme was shown to be present in the cytoplasmic droplet of epididymal sperm and also in detached cytoplasmic droplets in semen. The enzyme was not detected in the interstitium of testis and epididymis except for the endothelial cells of the vessel.
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PMID:Localization of angiotensin converting enzyme (dipeptidyl carboxypeptidase) in swine sperm by immunofluorescence. 638 9

The influence of thyroidectomy on key epididymal enzymes of the Embden-Meyerhof and pentose phosphate pathway have been studied in pubertal and adult animals in relation to the serum hormone profile. Age related differences in the response of epididymal segments were observed with respect to hexokinase activity, although the other 2 key enzymes of the Embden-Meyerhof pathway (6-PFK and PK) were suppressed in all regions of the epididymis in both pubertal and adult rats. The enzymes involved in the pentose phosphate pathway (G-6-PDH and 6-PGDH) remained unaltered. The serum hormone profile revealed that while FSH and testosterone titres were reduced, LH and Prl were unaltered. Replacement of T4 in thyroidectomized animals maintained serum hormone levels and the activities of the enzymes studied at control levels. It is inferred that thyroid hormones may be one part of a complex mechanism that controls carbohydrate metabolism in the epididymis.
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PMID:Influence of hypothyroidism on epididymal enzymes involved in carbohydrate metabolism. Studies in pubertal and adult rats. 641 30

Angiotensin converting enzyme exists in two different isoforms, somatic and germinal, whose respective distributions and intracellular localizations have not been precisely determined. The differing biochemical and molecular characteristics of the two isozymes allowed the preparation of antibodies specific for each of the two angiotensin converting enzyme isoforms and of two nucleic acid probes, one of which was specific for the germinal isoform. Immunohistochemistry and in situ hybridization were used to determine the cell distribution of, respectively, the two isoforms and their corresponding messenger RNAs in the classically studied tissues of male adult humans and marmosets. Results provided by the two different methods were always concordant and were identical in the two species. The somatic angiotensin converting enzyme form was expressed uniquely in somatic tissues (vascular endothelial cells and at the brush border of renal proximal convoluted tubule, jejunal villus, and epididymal duct epithelia), and the germinal form was expressed uniquely in germinal cells with a precise stage-specific pattern, starting in round spermatids and finishing in spermatozoa. In situ hybridization documented the presence of somatic angiotensin converting enzyme messenger RNA in renal tubule epithelium, jejunal enterocytes, and epididymal epithelium and demonstrated that there was no direct correlation between the levels of angiotensin converting enzyme messenger RNA and the enzyme it encodes for, i.e., angiotensin converting enzyme, in a given epithelium. The significance of the ultraselective expression of germinal angiotensin converting enzyme and of its specific messenger RNA at a very precise stage of spermatogenesis remains uncertain.
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PMID:Gene expression and tissue localization of the two isoforms of angiotensin I converting enzyme. 838 57


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