Assay of testicular angiotensin‐converting enzyme activity in human spermatozoa

Kamata, Makiko; Hu, Jianguo; Shibahara, Hiroaki; Nakagawa, Hachiro

doi:10.1046/j.1365-2605.2001.00288.x

Cited by 9 publications

(11 citation statements)

References 22 publications

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“…Early occurrence of ACE in epithelial cells of the mesonephros and the Wolffian duct has already been reported (Schütz et al, 1996). The suggestion that epididymal fluid ACE derives from tACE (Wong & Uchendu, 1991;Gatti et al, 1999), however, is not supported by our study and recently published quantitative data of others (Kamata et al, 2001). 3) contribute probably most to its predominant occurrence in the epididymal fluid (El-Dorry et al, 1983;Berg et al, 1986).…”

Section: Tubules Of Adults (K Pauls and Fe Franke Unpublished Observcontrasting

confidence: 98%

“…Former work employed enzymatic approaches, autoradiographic methods and polyclonal antisera in order to localize ACE in testis and epididymis (Pandey et al, 1984;Strittmatter et al, 1985;Velletri et al, 1985;Berg et al, 1986;Brentjens et al, 1986;Williams et al, 1992). The problem of separating ACE isoforms in seminal fluids and in ejaculated spermatozoa still remains a challenge (Köhn et al, 1998;Kamata et al, 2001). The problem of separating ACE isoforms in seminal fluids and in ejaculated spermatozoa still remains a challenge (Köhn et al, 1998;Kamata et al, 2001).…”

Section: Introductionmentioning

confidence: 99%

“…The collected data, however, are not always concurrent and particularly scarce in humans (Vivet et al, 1987;Sibony et al, 1993). The problem of separating ACE isoforms in seminal fluids and in ejaculated spermatozoa still remains a challenge (Köhn et al, 1998;Kamata et al, 2001).…”

Section: Introductionmentioning

confidence: 99%

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Isoforms of angiotensin I-converting enzyme in the development and differentiation of human testis and epididymis

Pauls¹,

Metzger

Steger

et al. 2003

Andrologia

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Angiotensin I-converting enzyme (ACE; CD143, Kininase II, EC 3.4.15.1) is known to be crucial for male fertility in animal models. We therefore studied its testicular (tACE) and somatic (sACE) isoforms in foetal and adult human testis and epididymis using monoclonal antibodies and cRNA probes. During spermatogenesis, tACE was found only in differentiating germ cells and was the only isoform within the seminiferous tubules of adult men. Although tACE mRNA was present in spermatocytes, tACE protein was initially found in post-meiotic step 3 spermatids and increased markedly during further differentiation. The enzyme was strictly confined to the adluminal membrane site of elongating spermatids and was localized at the neck and midpiece region of released and ejaculated spermatozoa. In contrast, sACE was expressed heterogeneously in Leydig cells and endothelial cells of the testicular interstitium, and homogeneously along the luminal surface of epithelial cells lining the ductuli efferents, corpus and cauda of epididymis, and vas deferens. The cell- and site-restricted pattern of sACE corresponded to that found in foetal tissues except an additional and transient expression of sACE in foetal germ cells and foetal Sertoli cells. Our study documents for the first time in humans the regulation and unique cellular distribution of ACE isoforms during the ontogenesis of the lower male genital tract.

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Section: Tubules Of Adults (K Pauls and Fe Franke Unpublished Observcontrasting

confidence: 98%

Section: Introductionmentioning

confidence: 99%

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Isoforms of angiotensin I-converting enzyme in the development and differentiation of human testis and epididymis

Pauls¹,

Metzger

Steger

et al. 2003

Andrologia

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“…Preparation of ACE and Immunoblotting-Somatic ACE was purified from human seminal plasma by using lisinopril-coupled Sepharose as described (12). Immunoblotting was done with anti-somatic ACE antibodies as described (12).…”

Section: Methodsmentioning

confidence: 99%

Angiotensin-converting Enzyme Degrades Alzheimer Amyloid β-Peptide (Aβ); Retards Aβ Aggregation, Deposition, Fibril Formation; and Inhibits Cytotoxicity

Hu¹,

Igarashi²,

Kamata³

et al. 2001

Journal of Biological Chemistry

Self Cite

329

218

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We have demonstrated that the angiotensin-converting enzyme (ACE) genotype is associated with Alzheimer's disease (AD) in the Japanese population (1). To determine why ACE affects susceptibility to AD, we examined the effect of purified ACE on aggregation of the amyloid ␤-peptide (A␤) in vitro. Surprisingly, ACE was found to significantly inhibit A␤ aggregation in a dose response manner. The inhibition of aggregation was specifically blocked by preincubation of ACE with an ACE inhibitor, lisinopril. ACE was confirmed to retard A␤ fibril formation with electron microscopy. ACE inhibited A␤ deposits on a synthaloid plate, which was used to monitor A␤ deposition on autopsied brain tissue. ACE also significantly inhibited A␤ cytotoxicity on PC12 h. The most striking fact was that ACE degraded A␤ by cleaving A␤-(1-40) at the site Asp 7 -Ser 8 . This was proven with reverse-phase HPLC, amino acid sequence analysis, and MALDI-TOF/MS. Compared with A␤-(1-40), aggregation and cytotoxic effects of the degradation products A␤-(1-7) and A␤-(8 -40) peptides were reduced or virtually absent. These findings led to the hypothesis that ACE may affect susceptibility to AD by degrading A␤ and preventing the accumulation of amyloid plaques in vivo.Progressive cerebral dysfunction in Alzheimer's disease (AD) 1 is accompanied by innumerable extracellular amyloid deposits in the form of senile plaque and microvascular amyloid. Amyloid protein is derived from the integral membrane polypeptide, ␤-amyloid precursor protein (␤APP). The released 39 -43 residue amyloid ␤-peptide (A␤) may subsequently undergo aggregation to form amyloid fibrils under the influence of various amyloid-associated factors (2). The aggregation and deposition of A␤ has been linked to the toxic effects causing cell damage in AD. Because A␤ is present in both normal and AD subjects, an answer to the question of why A␤ accumulates in AD but not in the normal brain may lead to a possible cure for AD.Angiotensin-converting enzyme (ACE; dipeptidyl carboxypeptidase, EC 3.4.15.1) is a membrane-bound ectoenzyme. It catalyzes the conversion of angiotensin I (AngI) to angiotensin II (AngII), which plays an important role in blood pressure and body fluid and sodium homeostasis (3). The cloning of the ACE gene revealed a 287-bp insertion (I)/deletion (D) polymorphism in intron 16. The serum ACE activity of the ACE DD genotype was twice as high as that of the ACE II genotype (4). The ACE genotype is considered to be associated with hypertension, coronary artery disease, left ventricular hypertrophy, myocardial infarction, and diabetic nephropathy (5-7). In particular, the ACE DD genotype is considered to be a risk factor for vascular diseases.We have compared the distribution of an I/D polymorphism of the gene coding for ACE in 133 Japanese sporadic AD patients and 257 control subjects (1). The association between AD and ACE genotypes or alleles was found to be significant. The frequency of the ACE II genotype was 1.4ϫ higher in AD than in controls, whereas that of ACE DD gen...

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“…Adherent spermatozoa may be released through the membrane tACE1. A portion of tACE1 is released from spermatozoa during capacitation, whereas other portions of tACE1 may be released during the sperm passage up the female reproductive tract to increase its binding capacity to the ZP [72]. In addition to its important role in capacitation, tACE1 has also been shown to participate in egg–sperm fusion.…”

Section: Testis Acesmentioning

confidence: 99%

Angiotensin-Converting Enzymes Play a Dominant Role in Fertility

Pan

Zhan

Fang

et al. 2013

IJMS

104

103

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According to the World Health Organization, infertility, associated with metabolic syndrome, has become a global issue with a 10%–20% incidence worldwide. An accumulating body of evidence has shown that the renin–angiotensin system is involved in the fertility problems observed in some populations. Moreover, alterations in the expression of angiotensin-converting enzyme-1, angiotensin-converting enzyme-2, and angiotensin-converting enzyme-3 might be one of the most important mechanisms underlying both female and male infertility. However, as a pseudogene in humans, further studies are needed to explore whether the abnormal angiotensin-converting enzyme-3 gene could result in the problems of human reproduction. In this review, the relationship between angiotensin-converting enzymes and fertile ability is summarized, and a new procedure for the treatment of infertility is discussed.

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Assay of testicular angiotensin‐converting enzyme activity in human spermatozoa

Cited by 9 publications

References 22 publications

Isoforms of angiotensin I-converting enzyme in the development and differentiation of human testis and epididymis

Isoforms of angiotensin I-converting enzyme in the development and differentiation of human testis and epididymis

Angiotensin-converting Enzyme Degrades Alzheimer Amyloid β-Peptide (Aβ); Retards Aβ Aggregation, Deposition, Fibril Formation; and Inhibits Cytotoxicity

Angiotensin-Converting Enzymes Play a Dominant Role in Fertility

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