Gelatinases and serine proteinase inhibitors of seminal plasma and the reproductive tract of turkey (Meleagris gallopavo)

Kotłowska, M.; Kowalski, Radosław Kajetan; Jankowski, Jan; Ciereszko, Andrzej

doi:10.1016/j.theriogenology.2004.07.020

Cited by 33 publications

(10 citation statements)

References 32 publications

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“…These results confirm the hypothesis that spermatozoa and seminal plasma can reduce the activity of hormone added to the seminal dose and consequently affect the ovulation induction in rabbit does. In seminal plasma and spermatozoa of mammals and avian species (Metayer et al 2002, Kotłowska et al 2005) numerous proteolytic enzymes have been found and GnRH analogues could be susceptible to peptidase degradation. Vicente et al (2011) suggest that seminal plasma is the main factor involved in the hormonal activity decrease.…”

Section: Discussionmentioning

confidence: 99%

Motility, mitochondrial membrane potential and ATP content of rabbit spermatozoa stored in extender supplemented with GnRH analogue [des-Gly10, D-Ala6]-LH-RH ethylamide

Gogol¹,

Trzcińska²,

Bryła³

2014

Polish Journal of Veterinary Sciences

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The present study was aimed to determine the effect of GnRH analogue [des-Gly10, D-Ala6]-LH-RH ethylamide on the quality of rabbit spermatozoa stored at 17 o C for 3 days. Semen from 5 bucks (13 ejaculates) was used in the experiment. Ejaculates were divided and diluted at a 1:10 ratio with rabbit semen extender Galap (IMV, France) (Control) or with Galap extender supplemented with GnRH analogue [des-Gly10, D-Ala6]-LH-RH ethylamide (50 μg/ml) and stored for 3 days. Sperm motility parameters, mitochondrial membrane potential (MMP) and ATP content were assessed on each day of the experiment. Motility analysis was performed using a computer-assisted sperm analysis (CASA) system. The following sperm motility parameters were recorded: total motile spermatozoa, progressively motile spermatozoa, curvilinear velocity, straight-line velocity, average path velocity, linearity, straightness and amplitude of lateral head displacement. MMP was evaluated using JC-1 fluorescent dye. ATP content was assessed using a bioluminescence method. The addition of GnRH analogue [des-Gly10, D-Ala6]-LH-RH ethylamide to Galap extender did not affect any of the quality parameters studied. However, in both groups (Control and GnRH), significant changes in motility parameters (except straight-line velocity) and proportion of spermatozoa showing high MMP and ATP content were observed throughout 3 days of storage.

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Section: Discussionmentioning

confidence: 99%

Motility, mitochondrial membrane potential and ATP content of rabbit spermatozoa stored in extender supplemented with GnRH analogue [des-Gly10, D-Ala6]-LH-RH ethylamide

Gogol¹,

Trzcińska²,

Bryła³

2014

Polish Journal of Veterinary Sciences

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“…Proteolysis regulators are a component of the seminal fluid of many animal taxa, including insects and other invertebrates [1]–[7], fish [8]–[10], birds [11], [12], and mammals [13]–[18]. However, the mechanisms by which seminal proteases act, and most of the processes they affect, in mated females are poorly understood.…”

Section: Introductionmentioning

confidence: 99%

The Drosophila melanogaster Seminal Fluid Protease “Seminase” Regulates Proteolytic and Post-Mating Reproductive Processes

2012

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Proteases and protease inhibitors have been identified in the ejaculates of animal taxa ranging from invertebrates to mammals and form a major protein class among Drosophila melanogaster seminal fluid proteins (SFPs). Other than a single protease cascade in mammals that regulates seminal clot liquefaction, no proteolytic cascades (i.e. pathways with at least two proteases acting in sequence) have been identified in seminal fluids. In Drosophila, SFPs are transferred to females during mating and, together with sperm, are necessary for the many post-mating responses elicited in females. Though several SFPs are proteolytically cleaved either during or after mating, virtually nothing is known about the proteases involved in these cleavage events or the physiological consequences of proteolytic activity in the seminal fluid on the female. Here, we present evidence that a protease cascade acts in the seminal fluid of Drosophila during and after mating. Using RNAi to knock down expression of the SFP CG10586, a predicted serine protease, we show that it acts upstream of the SFP CG11864, a predicted astacin protease, to process SFPs involved in ovulation and sperm entry into storage. We also show that knockdown of CG10586 leads to lower levels of egg laying, higher rates of sexual receptivity to subsequent males, and abnormal sperm usage patterns, processes that are independent of CG11864. The long-term phenotypes of females mated to CG10586 knockdown males are similar to those of females that fail to store sex peptide, an important elicitor of long-term post-mating responses, and indicate a role for CG10586 in regulating sex peptide. These results point to an important role for proteolysis among insect SFPs and suggest that protease cascades may be a mechanism for precise temporal regulation of multiple post-mating responses in females.

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“…Seminal fluid protease inhibitors have been identified in a wide range of organisms from insects to mammals (e.g., Laurell et al 1992;Ohlsson et al 1995;Murer et al 2001;Swanson et al 2001;Kotlowska et al 2005), suggesting that protease inhibitors play significant and possibly conserved roles in reproduction. Interestingly, comparative structural modeling has revealed that the mammalian and Drosophila seminal fluid protease inhibitors are similar in predicted protein structures and hence likely to share biochemical functions (Mueller et al 2004).…”

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confidence: 99%

Targeted Gene Deletion and Phenotypic Analysis of the Drosophila melanogaster Seminal Fluid Protease Inhibitor Acp62F

et al. 2008

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Internally fertilizing organisms transfer a complex assortment of seminal fluid proteins, a substantial fraction of which are proteolysis regulators. In mammals, some seminal protease inhibitors have been implicated in male infertility and these same molecular classes of protease inhibitors are also found in Drosophila seminal fluid. Here, we tested the reproductive functions of the Drosophila melanogaster seminal fluid protease inhibitor Acp62F by generating a precise deletion of the Acp62F gene. We did not detect a nonredundant function for Acp62F in modulating the egg laying, fertility, remating frequency, or life span of mated females. However, loss of Acp62F did alter a male's defensive sperm competitive ability, consistent with the localization of Acp62F to sperm storage organs. In addition, the processing of at least one seminal protein, the ovulation hormone ovulin, is slower in the absence of Acp62F.

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Gelatinases and serine proteinase inhibitors of seminal plasma and the reproductive tract of turkey (Meleagris gallopavo)

Cited by 33 publications

References 32 publications

Motility, mitochondrial membrane potential and ATP content of rabbit spermatozoa stored in extender supplemented with GnRH analogue [des-Gly10, D-Ala6]-LH-RH ethylamide

Motility, mitochondrial membrane potential and ATP content of rabbit spermatozoa stored in extender supplemented with GnRH analogue [des-Gly10, D-Ala6]-LH-RH ethylamide

The Drosophila melanogaster Seminal Fluid Protease “Seminase” Regulates Proteolytic and Post-Mating Reproductive Processes

Targeted Gene Deletion and Phenotypic Analysis of the Drosophila melanogaster Seminal Fluid Protease Inhibitor Acp62F

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