Identification and function of proteolysis regulators in seminal fluid

LaFlamme, Brooke; Wolfner, Mariana F.

doi:10.1002/mrd.22130

Cited by 126 publications

(123 citation statements)

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“…Proteases, the effectors of proteolysis, are present in the seminal fluid of all animals investigated to date, but their role in reproduction is not well understood (LaFlamme and Wolfner 2013). Seminal fluid proteases are often activated at ejaculation, allowing for the possibility that either molecules from the male, the female, or both, are required for their activation.…”

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confidence: 99%

A Drosophila Protease Cascade Member, Seminal Metalloprotease-1, Is Activated Stepwise by Male Factors and Requires Female Factors for Full Activity

LaFlamme¹,

Avila²,

Michalski

et al. 2014

Genetics

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Females and males of sexually reproducing animals must cooperate at the molecular and cellular level for fertilization to succeed, even though some aspects of reproductive molecular biology appear to involve antagonistic interactions. We previously reported the existence of a proteolytic cascade in Drosophila melanogaster seminal fluid that is initiated in the male and ends in the female. This proteolytic cascade, which processes at least two seminal fluid proteins (Sfps), is a useful model for understanding the regulation of Sfp activities, including proteolysis cascades in mammals. Here, we investigated the activation mechanism of the downstream protease in the cascade, the astacin-family metalloprotease Seminal metalloprotease-1 (Semp1, CG11864), focusing on the relative contribution of the male and female to its activation. We identified a naturally occurring semp1 null mutation within the Drosophila Genetic Reference Panel. By expressing mutant forms of Semp1 in males homozygous for the null mutation, we discovered that cleavage is required for the complete activation of Semp1, and we defined at least two sites that are essential for this activational cleavage. These amino acid residues suggest a two-step mechanism for Semp1 activation, involving the action of at least two malederived proteases. Although the cascade's substrates potentially influence both fertility and sperm competition within the mated female, the role of female factors in the activation or activity of Semp1 is unknown. We show here that Semp1 can undergo its activational cleavage in male ejaculates, without female contributions, but that cleavage of Semp1's substrates does not proceed to completion in ejaculates, indicating an essential role for female factors in Semp1's full activity. In addition, we find that expression of Semp1 in virgin females demonstrates that females can activate this protease on their own, resulting in activity that is complete but substantially delayed.

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confidence: 99%

A Drosophila Protease Cascade Member, Seminal Metalloprotease-1, Is Activated Stepwise by Male Factors and Requires Female Factors for Full Activity

LaFlamme¹,

Avila²,

Michalski

et al. 2014

Genetics

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“…In terms of protease regulation of sperm biology, proteomic studies have identified a large number of proteases in seminal fluid from insects to mammals, but few of these proteins have well-described functions. 38 Additionally, while a number of serine proteases and serine protease inhibitors are produced by the mouse testis, 39 little is known about the signaling cascades they are involved in and how they may impact sperm motility. Our identification of SNF-10 as a protein required for responding to an extracellular protease represents an opportunity to study a signaling cascade initiated by a protease, and importantly, to learn how an SLC6 protein can be used by cells to gain motility.…”

Section: Snf-10 Is a Member Of The Slc6 Familymentioning

confidence: 99%

SNF-10 connects male-derived signals to the onset of sperm motility inC. elegans

Fenker¹,

Stanfield

2015

Worm

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Sperm from the nematode C. elegans gain motility during a process termed activation, which they initiate in response to specific environmental signals. During this process, a number of subcellular rearrangements occur, culminating in an altered morphology that allows the cell to crawl toward and fertilize oocytes. Both hermaphrodites and males produce sperm, and redundant, sex-biased pathways regulate the sperm's activation. The male-derived signal for sperm activation involves TRY-5, a trypsin-like serine protease in seminal fluid, but until recently it was unknown what factors were active downstream of TRY-5. In our recent paper, we reported the discovery of SNF-10, a solute carrier 6 (SLC6) family protein that is expressed by sperm and connects the activation signal to changes in sperm morphology and, ultimately, the onset of motility. Here, we review our recent results, focusing on potential models for SNF-10's function in C. elegans, and additionally discuss the role SLC6 transporters may play in male reproductive biology from invertebrates to mammals.

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“…The physiologic role of the proteins involves metabolic events that can suffer alteration during the sperm cryopreservation process. Soluble and structural proteins have an important role in the spermatozoa metabolism, which can interferes in the male fertility 11,12 , in the bull's fertility 13,14,15,16,17,18,19,20 and semen's freezability 10,21,22 .…”

Section: Discussionmentioning

confidence: 99%

Proteômica para investigar a congelabilidade do semen bovino

Roncoletta

Morani

Rodrigues³

et al. 2013

Braz. J. Vet. Res. Anim. Sci.

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The present study was undertaken the protein composition in 2D-electrophoretic pattern (2DE) of the seminal plasma (SP) can interfere in the semen bull freezability, and if we can use that for predicting semen bull freezability. Samples were obtained of 20 bulls (different breeds) with a minimum of 3 years history semen production in commercial semen collection Center. All animals ranged between 2 -7 years of age. The semen freezability was calculated by # of thawed and approved ejaculates / # of ejaculates submitted to cryopreservation (after semen evaluation and approved to submitted to freeze). The bulls were divided in 3 groups: HIGH (=>80% ejaculates approved); MEDIUM (>60% and <79% ejaculates approved); LOW (=<59% ejaculates approved); the pattern and criteria were the same used in the routine of the commercial semen Center. 68 gels were carried through by 2DE of SP samples indicated 225 detected spots with protein different amount (VION) comparing. Comparing bull´s semen freezability and VION of each spot found difference among 2 spots from High and Low, even considering just spots with % of detection frequency bigger than 75%. The taurine bulls demonstrated more homogeneous profile when comparing with zebu bulls, considering number and frequency of appearance of spots. The results showed that proteomics can be a useful tool to predict the semen freezability, but we´ll need to study better the interactions between sperm membrane, seminal plasma and extender to comprehend better which proteome phenotype interfere positive or negatively in the semen freezability.Keywords: Cattle. Proteins. Seminal Plasma. Cryopreservation. ResumoO objetivo do presente estudo foi avaliar se a composição proteica de plasma seminal, verificada por eletroforese bidimensional (2DE), pode interferir na congelabilidade do sêmen de touros, e se existe a possibilidade de predizer tal característica em touros doadores de sêmen. Amostras de 20 touros (diferentes raças) com mínimo de três anos de histórico de produção em Central de Coleta de sêmen foram coletadas. Todos os touros tinham de 2 a 7 anos de idade. A congelabilidade do sêmen foi calculada por n o de ejaculados aprovados pós-descongelação / n o de ejaculados submetidos à congelação (depois do crivo do padrão de qualidade da empresa para aprovar o ejaculado para ser submetido a congelação). Os touros foram divididos em três grupos: ALTA (=>80% aproveitamento de ejaculados encaminhados à congelação); MÉDIA (>60 a 79% ejaculados aprovados) e BAIXA (=<59% ejaculados aprovados). Sessenta e oito corridas de géis 2DE foram avaliadas nas amostras de plasma seminal, que detectaram 225 spots com quantidade de proteína diferente entre as mesmas (VION). Pela estatística utilizada, comparando-se a congelabilidade do sêmen com quantidade de proteína detectada de cada spot (VION), contatouse que 2 spots apresentaram-se com quantidade significativa de proteína diferente entre os dois grupos de congelabilidade do sêmen, considerando spots que foram detectados em mais de 75% das amost...

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Identification and function of proteolysis regulators in seminal fluid

Cited by 126 publications

References 199 publications

A Drosophila Protease Cascade Member, Seminal Metalloprotease-1, Is Activated Stepwise by Male Factors and Requires Female Factors for Full Activity

A Drosophila Protease Cascade Member, Seminal Metalloprotease-1, Is Activated Stepwise by Male Factors and Requires Female Factors for Full Activity

SNF-10 connects male-derived signals to the onset of sperm motility inC. elegans

Proteômica para investigar a congelabilidade do semen bovino

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