Expression of enkephalin-degrading enzymes in human semen and implications for sperm motility

Subirán, Nerea; Agirregoitia, Ekaitz; Valdivia, Asier; Ochoa, Carmen; Casis, Luı́s; Irazusta, Jon

doi:10.1016/j.fertnstert.2007.06.056

Cited by 40 publications

(49 citation statements)

References 28 publications

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“…Aminopeptidase N (APN/CD13) and neutral endopeptidase 24:11 (NEP/CD10) are surface membrane multifunctional enzymes and both are present in human sperm cells [4,5]. Therefore, the aim of this study was to investigate the involvement of APN/CD13 and NEP/ CD10 in motility of human capacitated spermatozoa.…”

Section: Introductionmentioning

confidence: 99%

Control of APN/CD13 and NEP/CD10 on sperm motility

Subirán¹,

Pinto²,

Agirregoitia³

et al. 2010

Asian J Androl

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Aminopeptidase N (APN/CD13) and neutral endopeptidase (NEP/CD10) are enzymes present in human sperm cells and involved in regulation of sperm motility of noncapacitated spermatozoa. We investigated the involvement of APN/CD13 and NEP/CD10 in motility and in kinematic parameters of human capacitated spermatozoa. Sperm cells isolated by a discontinuous Percoll gradient (40%-80%) followed up by swim-up techniques were incubated with the APN/CD13-specific inhibitor, leuhistin (100 µmol L -1 ), and the NEP/CD10-specific inhibitor, thiorphan (1 µmol L -1 ). The complete inhibition of both APN/CD13 and NEP/CD10 improved sperm motility. Spermatozoa incubated with the APN/CD13-specific inhibitor leuhistin showed asymmetrical trajectories, whereas sperm trajectories were more regular after treatment with the NEP/CD10-specific inhibitor thiorphan. In conclusion, APN/CD13 and NEP/CD10 modulate the motility of capacitated spermatozoa, although each of the enzymes seems to participate in the control of different aspects of sperm motility. Therefore, both inhibitors may be useful for sperm activation at different functional stages of spermatozoa.

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Section: Introductionmentioning

confidence: 99%

Control of APN/CD13 and NEP/CD10 on sperm motility

Subirán¹,

Pinto²,

Agirregoitia³

et al. 2010

Asian J Androl

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“…In this snake, spermatozoa become increasingly more motile from the proximal to the distal region (Almeida-Santos et al 2004). Regarding the presence of examined peptidase activities in the spermatozoa, the identification of their anatomical sources need to be investigated; for example, in the acrosomal complex, which is known in all vertebrate taxa as an enzyme-rich organelle that facilitates spermatozoal penetration into the ovum (Subirán et al 2008). In squamates, the acrosomal complex is highly compartimentalized (Gribbins et al 2007), and this compartimentalization has been suggested as an aid to the sequential release of acrosomal enzymes (Talbot 1991).…”

Section: Rattlesnake Seminal Peptidasesmentioning

confidence: 99%

“…Many peptides, such as angiotensins (Angs; Fraser et al 2006), kinins (Blaukat 2003), substance P, enkephalins (Sastry et al 1991), endorphin (El-Haggar et al 2006), oxytocin (OXT), vasopressin (AVP; Assinder et al 2000), LHRH (Amory & Bremner 2003), TRH, and fertilization-promoting peptide (FPP; Green et al 1996), as well some peptidases, particularly aminopeptidases (APs) and oligopeptidases have been related to seminal physiology in mammals (Fernández et al 2002, Subirán et al 2008. In this sense, Ang I and II are hydrolyzed by acid AP (APA; EC 3.…”

Section: Introductionmentioning

confidence: 99%

“…Until the present, earlier studies of human seminal fractions evaluated the distribution of only three of the above-mentioned peptidases: APN (Fernández et al 2002, Subirán et al 2008, PAP, and POP . APN was detected in soluble (S-) and solubilized membrane-bound fractions (MFs) of seminal plasma (SP) and prostasomes (PRs; Fernández et al 2002).…”

Section: Introductionmentioning

confidence: 99%

“…APN was detected in soluble (S-) and solubilized membrane-bound fractions (MFs) of seminal plasma (SP) and prostasomes (PRs; Fernández et al 2002). In sperm, APN was detected in the equatorial segment of the upper post-acrosomal region of the head, in the neck, and along the tail (Subirán et al 2008). Alterations of APN levels in human semen were associated with different abnormalities in the sperm of subfertile patients .…”

Section: Introductionmentioning

confidence: 99%

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Peptidase activities in Crotalus durissus terrificus semen

Marinho

Almeida‐Santos²,

Carneiro³

et al. 2008

Reproduction

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To understand the role of peptidases in seminal physiology of Crotalus durissus terrificus, activity levels of representative enzymes in semen and their sensitivities to inhibitors, cofactors, and peptide hormones were evaluated. The existence of seminal fractions and the association of peptidases with these fractions were also characterized for the first time in snakes. The prominent inhibitors of aminopeptidases (APs) were amastatin for acid, basic, and neutral; bestatin for basic; and diprotin A for dipeptidyl-IV. Cystyl and prolylimino APs were similarly susceptible to the majority of these inhibitors. The basic and neutral were characterized as metallo-peptidases, acid AP was activated by MnCl 2 , and cystyl, prolyl-imino, and type I pyroglutamyl were characterized as sulphydryl-dependent APs. Angiotensin II, vasotocin, bradykinin, fertilization-promoting peptide, and TRH altered the majority of these peptidase activities; these peptides are possible substrates and/or modulators of these peptidases. Peptidase activities were found in all seminal fractions: seminal plasma (SP), prostasome-like (PR) structures, and soluble (S-) and membrane-bound fractions (MFs) of spermatozoa. The levels of activity of each peptidase varied among different seminal fractions. In SP, the higher activities were puromycin-insensitive neutral and basic APs. In PR, the higher activity was puromycin-insensitive neutral AP. In spermatozoa, the higher activity in subcellular SF was puromycinsensitive neutral, while in MF both puromycin-sensitive and -insensitive neutral APs were equally higher than the other examined peptidases. Data suggested that these peptidases, mainly basic and neutral, have a high relevance in regulating seminal functions of C. d. terrificus. Reproduction (2008) 136 767-776

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