Dipeptidyl carboxypeptidase from human seminal plasma

Depierre, D; Bargetzi, Jean-Pierre; Roth, Marc

doi:10.1016/0005-2744(78)90049-9

Cited by 42 publications

(15 citation statements)

References 23 publications

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“…Soluble ACE in the epididymis could not be derived from particulate epididymal ACE because the soluble but not the particulate form is found in the initial segment of the epididymis (10). Soluble ACE from seminal plasma seems to be distinct from soluble ACE in the epididymis since it is more similar to lung ACE than testicular ACE in molecular weight and immunological properties (20,21).…”

Section: Discussionmentioning

confidence: 97%

Angiotensin-Converting Enzyme in the Testis and Epididymis: Differential Development and Pituitary Regulation of Isozymes*

et al. 1985

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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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Section: Discussionmentioning

confidence: 97%

Angiotensin-Converting Enzyme in the Testis and Epididymis: Differential Development and Pituitary Regulation of Isozymes*

et al. 1985

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“…High ACE activity has been determined in human seminal plasma (739). The soluble ACE in seminal fluid resembles the detergent-solubilized lung enzyme more than the detergent-solubilized testicular enzyme (150,180). The active enzyme in seminal fluid corresponds to the pulmonary polypeptide (45, 372).…”

Section: Male Reproductive Tractmentioning

confidence: 99%

Physiology of Local Renin-Angiotensin Systems

Paul

Mehr²,

Kreutz³

2006

Physiological Reviews

1,512

1,371

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Since the first identification of renin by Tigerstedt and Bergmann in 1898, the renin-angiotensin system (RAS) has been extensively studied. The current view of the system is characterized by an increased complexity, as evidenced by the discovery of new functional components and pathways of the RAS. In recent years, the pathophysiological implications of the system have been the main focus of attention, and inhibitors of the RAS such as angiotensin-converting enzyme (ACE) inhibitors and angiotensin (ANG) II receptor blockers have become important clinical tools in the treatment of cardiovascular and renal diseases such as hypertension, heart failure, and diabetic nephropathy. Nevertheless, the tissue RAS also plays an important role in mediating diverse physiological functions. These focus not only on the classical actions of ANG on the cardiovascular system, namely, the maintenance of cardiovascular homeostasis, but also on other functions. Recently, the research efforts studying these noncardiovascular effects of the RAS have intensified, and a large body of data are now available to support the existence of numerous organ-based RAS exerting diverse physiological effects. ANG II has direct effects at the cellular level and can influence, for example, cell growth and differentiation, but also may play a role as a mediator of apoptosis. These universal paracrine and autocrine actions may be important in many organ systems and can mediate important physiological stimuli. Transgenic overexpression and knock-out strategies of RAS genes in animals have also shown a central functional role of the RAS in prenatal development. Taken together, these findings may become increasingly important in the study of organ physiology but also for a fresh look at the implications of these findings for organ pathophysiology.

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“…ACE is a membrane-bound enzyme and is mainly lo cated in the caveolae of the luminal surface of the lung endothelial cell [7,8], However, it could also be detected in body fluids such as Angiotensin-I-converting enzyme (ACE, EC 3.4.15.1), a dipeptidyl carboxypeptidase, was first isolated from horse plasma [ 1 ] and is thought to be a key enzyme in the reninangiotensin and kallikrein-bradykinin sys tem. ACE liberates the octapeptide angioten sin II from the decapeptide angiotensin I by cleaving the C-terminal dipeptide histidyl-L-blood, seminal plasma [9], lymph [10] and urine [11]. ACE has become of clinical inter est since elevation of this enzyme has been found in serum of patients with sarcoidosis of the lung [12].…”

Section: Introductionmentioning

confidence: 99%

Assay and Biochemical Characterization of Angiotensin-I-Converting Enzyme in Cerebrospinal Fluid

Schweisfurth¹,

Schiöberg-Schiegnitz²

1984

Enzyme

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A spectrofluorimetric method was adapted for determination of angiotensin-Iconverting enzyme (ACE) in untreated native cerebrospinal fluid (CSF). Benzyloxycarbonylphenylalanyl- histidyl-leucine was applied as enzyme substrate. The biochemical behavior of ACE of CSF (CACE) was studied. The pH optimum was found to be 8.0 using borax phosphate buffer. The determination of Km was 10.7 ± 3.3 (SD) μmol/1. ACE could be blocked by 8-hydroxyquinoline (100%) and phenanthroline (80%), but only slight inhibition was observed by teprotide (43%), EDTA (40%) and captopril (31%). The influence of various drugs on CACE was also tested. The different biochemical behavior of CACE compared to serum ACE suggested that an isoenzyme exists in CSF. CACE has been found to be elevated in neuroimmunological and inflammatory disorders of the nervous system compared to levels in healthy controls.

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Dipeptidyl carboxypeptidase from human seminal plasma

Cited by 42 publications

References 23 publications

Angiotensin-Converting Enzyme in the Testis and Epididymis: Differential Development and Pituitary Regulation of Isozymes*

Angiotensin-Converting Enzyme in the Testis and Epididymis: Differential Development and Pituitary Regulation of Isozymes*

Physiology of Local Renin-Angiotensin Systems

Assay and Biochemical Characterization of Angiotensin-I-Converting Enzyme in Cerebrospinal Fluid

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