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Article ; Online: Reproductive tract modifications of the boar sperm surface.

Gadella, Bart M

2017 Volume 84, Issue 9, Page(s) 822–831

Abstract: The sperm cell has a unique, polarized, and segregated surface that is modified extensively by the changing environments in both the male and the female reproductive tracts. The sperm cannot refresh its surface, as protein translation and membrane ... ...

Abstract	The sperm cell has a unique, polarized, and segregated surface that is modified extensively by the changing environments in both the male and the female reproductive tracts. The sperm cannot refresh its surface, as protein translation and membrane recycling by intracellular vesicular transport have ceased upon its maturation. So, how is the sperm surface modified in the reproductive tracts and how do these processes affect fertilization? This review traces these modifications as boar sperm travels from their liberation from the Sertoli cell into the lumen of seminiferous tubules of the testis to the site of fertilization in the ampulla of the oviduct in the sow, via an artificial insemination route. The effect of sperm dilution for artificial insemination, as well as more extensive sperm processing for in vitro fertilization, cryopreservation, or sex sorting, are also discussed with respect to how these procedures affect sperm surface organization and fertilization capacity.
Language	English
Publishing date	2017-09
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	20321-x
ISSN	1098-2795 ; 1040-452X
ISSN (online)	1098-2795
ISSN	1040-452X
DOI	10.1002/mrd.22821
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Article ; Online: Inducing ciliation in equine oviduct epithelial cell monolayers

Leemans, Bart / Marchand, Joshepine HEAM / Soom, Ann van / Gadella, Bart M / Stout, Tom AE

Journal of Equine Veterinary Science. 2023 June, v. 125 p.104658-

2023

Abstract: Recently, we developed re-differentiated equine oviduct epithelial cell (EOEC) monolayers in Transwell inserts. EOEC monolayers demonstrated various in vivo-like morphological characteristics, but often lacked secondary cilia. The monolayers were ... ...

Abstract	Recently, we developed re-differentiated equine oviduct epithelial cell (EOEC) monolayers in Transwell inserts. EOEC monolayers demonstrated various in vivo-like morphological characteristics, but often lacked secondary cilia. The monolayers were classified as low (<1% secondary cilia) or high (>5% secondary cilia) spontaneously re-differentiated, with the latter in the minority (5-10%). Interestingly, only high re-differentiated monolayers responded to Notch inhibition by developing in vivo-like secondary ciliation rates, i.e. over 50% ciliated cells. In this study, we aimed to consistently generate high re-differentiated monolayers. We first assessed whether secondary cilia formation was affected by donor mare, cycle stage and/or experiment. For this, harvested oviduct explants were cultured for 10 days at a concentration of 10 × 10⁶ EOECs per 9.6 cm² well, to yield a confluent de-differentiated monolayer in conventional wells. Subsequently, the monolayers were trypsinized and the EOECs were reseeded onto the microporous membrane of hanging inserts at a concentration of 0.3 × 10⁵ EOECs per 0.33 cm² insert. Three days after seeding, the EOECs were triggered to re-differentiate by air-liquid interface introduction (ALI). After 1 and 2 months in culture, EOEC monolayers were fixed and their phenotype was assessed by combined immunofluorescence staining to detect cilia (mouse anti-acetylated α-tubulin antibody; Alexa 488-conjugated goat anti-mouse secondary antibody),cell nuclei (Hoechst 33342) and actin filaments (Alexa 568-conjugated phalloidin). Neither cell donor nor cycle stage had any effect on secondary ciliation rates, whereas experimental modifications did. In 3/15 experiments, >95% of the monolayers demonstrated high re-differentiated monolayers. To discover the source of experimental variation, the seeding concentration of the de-differentiated EOECs was varied between 0.1 and 10 × 10⁵ EOECs per 0.33 cm² insert; this did not affect secondary ciliation rates. In a third experiment, the effect of varying the seeding concentration of the harvested oviduct explant EOECs used to establish the de-differentiated monolayers, between 1 and 30 × 10⁶ EOECs per 9.6 cm² well, was evaluated. EOECs harvested from de-differentiated monolayers 10 days after oviduct explant seeding at 1 or 5 × 10⁶ EOECs per well supported the formation of high re-differentiated monolayers in >95% of cases. Within 1 month after ALI, >50% and >30% of the re-differentiated EOECs showed secondary cilia after initial seeding of 1 and 5 × 10⁶ oviduct explant EOECs per well, respectively. Notch-inhibition helped to further increase secondary ciliation rates to >70% in the re-differentiated monolayers. We conclude that initial oviduct explant EOEC seeding concentration is critical to subsequently generating monolayers that closely resemble in vivo oviduct epithelia.
Keywords	actin ; antibodies ; epithelial cells ; fluorescent antibody technique ; goats ; liquid-air interface ; mares ; mice ; microporous membranes ; oviducts ; phalloidine ; phenotype ; sowing ; veterinary medicine
Language	English
Dates of publication	2023-06
Publishing place	Elsevier Inc.
Document type	Article ; Online
ZDB-ID	2102631-2
ISSN	1542-7412 ; 0737-0806
ISSN (online)	1542-7412
ISSN	0737-0806
DOI	10.1016/j.jevs.2023.104658
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Article ; Online: The fate of porcine sperm CRISP2 from the perinuclear theca before and after in vitro fertilization†.

Zhang, Min / Bromfield, Elizabeth G / Helms, J Bernd / Gadella, Bart M

Biology of reproduction

2022 Volume 107, Issue 5, Page(s) 1242–1253

Abstract: In a previous study, we reported that porcine sperm cysteine-rich secretory protein 2 (CRISP2) is localized in the post-acrosomal sheath-perinuclear theca (PT) as reduction-sensitive oligomers. In the current study, the decondensation and removal of ... ...

Abstract	In a previous study, we reported that porcine sperm cysteine-rich secretory protein 2 (CRISP2) is localized in the post-acrosomal sheath-perinuclear theca (PT) as reduction-sensitive oligomers. In the current study, the decondensation and removal of CRISP2 was investigated during in vitro sperm capacitation, after both the induction of the acrosome reaction and in vitro fertilization. Confocal immunofluorescent imaging revealed that additional CRISP2 fluorescence appeared on the apical ridge and on the equatorial segment (EqS) of the sperm head following capacitation, likely due to cholesterol removal. After an ionophore A23187-induced acrosome reaction, CRISP2 immunofluorescence disappeared from the apical ridge and the EqS area partly not only owing to the removal of the acrosomal shroud vesicles, but to its presence in a subdomain of EqS. The fate of sperm head CRISP2 was further examined post-fertilization. In vitro matured porcine oocytes were co-incubated with boar sperm cells for 6-8 h and the zygotes were processed for CRISP2 immunofluorescent staining. Notably, decondensation of CRISP2, and thus of the sperm PT, occurred while the sperm nucleus was still fully condensed. CRISP2 was no longer detectable in fertilized oocytes in which sperm nuclear decondensation and paternal pronucleus formation were apparent. This rapid dispersal of CRISP2 in the PT is likely regulated by redox reactions for which its cysteine-rich domain is sensitive. Reduction of disulfide bridges within CRISP2 oligomers may be instrumental for PT dispersal and elimination.
MeSH term(s)	Male ; Swine ; Animals ; Cysteine ; Semen ; Spermatozoa/metabolism ; Acrosome Reaction ; Fertilization in Vitro/veterinary
Chemical Substances	Cysteine (K848JZ4886)
Language	English
Publishing date	2022-05-04
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1118-6
ISSN	1529-7268 ; 0006-3363
ISSN (online)	1529-7268
ISSN	0006-3363
DOI	10.1093/biolre/ioac169
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Article ; Online: Characterization of acrosin and acrosin binding protein as novel CRISP2 interacting proteins in boar spermatozoa.

Zhang, Min / Chiozzi, Riccardo Zenezini / Bromfield, Elizabeth G / Heck, Albert Jr / Helms, J Bernd / Gadella, Bart M

Andrology

2023 Volume 11, Issue 7, Page(s) 1460–1471

Abstract: Background: Previously, we reported that cysteine-rich secretory protein 2 is involved in high molecular weight complexes in boar spermatozoa. These cysteine-rich secretory protein 2protein complexes are formed at the last phase of sperm formation in ... ...

Abstract	Background: Previously, we reported that cysteine-rich secretory protein 2 is involved in high molecular weight complexes in boar spermatozoa. These cysteine-rich secretory protein 2protein complexes are formed at the last phase of sperm formation in the testis and play a role in sperm shaping and functioning. Objectives: This study aimed to identify cysteine-rich secretory protein 2 interacting partners. These binding partner interactions were investigated under different conditions, namely, non-capacitating conditions, after the induction of in vitro sperm capacitation and subsequently during an ionophore A23187-induced acrosome reaction. Materials and methods: The incubated pig sperm samples were subjected to protein extraction. Extracted proteins were subjected to blue native gel electrophoresis and native immunoblots. Immunoreactive gel bands were excised and subjected to liquid chromatography-mass spectrometry (LC-MS) analysis for protein identification. Protein extracts were also subjected to CRISP2 immunoprecipitation and analyzed by LC-MS for protein identification. The most prominent cystein-rich secretory protein 2 interacting proteins that appeared in both independent LC-MS analyses were studied with a functional in situ proximity interaction assay to validate their property to interact with cystein-rich secretory protein 2 in pig sperm. Results: Blue native gel electrophoresis and native immunoblots revealed that cystein-rich secretory protein 2 was present within a ∼150 kDa protein complex under all three conditions. Interrogation of cystein-rich secretory-protein 2-immunoreactive bands from blue native gels as well as cystein-rich secretory protein 2 immunoprecipitated products using mass spectrometry consistently revealed that, beyond cystein-rich secretory protein 2, acrosin and acrosin binding protein were among the most abundant interacting proteins and did interact under all three conditions. Co-immunoprecipitation and immunoblotting indicated that cystein-rich secretory protein 2 interacted with pro-acrosin (∼53 kDa) and Aacrosin binding protein under all three conditions and additionally to acrosin (∼35 kDa) after capacitation and the acrosome reaction. The colocalization of these interacting proteins with cystein-rich secretory protein 2 was assessed via in situ proximity ligation assays. The colocalization signal of cystein-rich secretory protein 2 and acrosin in the acrosome seemed dispersed after capacitation but was consistently present in the sperm tail under all conditions. The fluorescent foci of cystein-rich secretory protein 2 and acrsin binding protein colocalization appeared to be redistributed within the sperm head from the anterior acrosome to the post-acrosomal sheath region upon capacitation. Discussion and conclusion: These results suggest that CRISP2 may act as a scaffold for protein complex formation and dissociation to ensure the correct positioning of proteins required for the acrosome reaction and zona pellucida penetration.
MeSH term(s)	Male ; Animals ; Swine ; Acrosin/metabolism ; Cysteine/metabolism ; Semen/metabolism ; Spermatozoa/metabolism ; Proteins/metabolism ; Acrosome ; Sperm Capacitation ; Protein Binding
Chemical Substances	Acrosin (EC 3.4.21.10) ; Cysteine (K848JZ4886) ; Proteins
Language	English
Publishing date	2023-03-09
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2696108-8
ISSN	2047-2927 ; 2047-2919
ISSN (online)	2047-2927
ISSN	2047-2919
DOI	10.1111/andr.13413
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Article: A stallion spermatozoon’s journey through the mare’s genital tract: In vivo and in vitro aspects of sperm capacitation

Maitan, Paula / Bromfield, Elizabeth G. / Stout, Tom A.E. / Gadella, Bart M. / Leemans, Bart

Animal reproduction science. 2021 Sept. 04,

2021

Abstract: Conventional in vitro fertilization is not efficacious when working with equine gametes. Although stallion spermatozoa bind to the zona pellucida in vitro, these gametes fail to initiate the acrosome reaction in the vicinity of the oocyte and cannot, ... ...

Abstract	Conventional in vitro fertilization is not efficacious when working with equine gametes. Although stallion spermatozoa bind to the zona pellucida in vitro, these gametes fail to initiate the acrosome reaction in the vicinity of the oocyte and cannot, therefore, penetrate into the perivitelline space. Failure of sperm penetration most likely relates to the absence of optimized in vitro fertilization media containing molecules essential to support stallion sperm capacitation. In vivo, the female reproductive tract, especially the oviductal lumen, provides an environmental milieu that appropriately regulates interactions between the gametes and promotes fertilization. Identifying these ‘fertilization supporting factors’ would be a great contribution for development of equine in vitro fertilization media. In this review, a description of the current understanding of the interactions stallion spermatozoa undergo during passage through the female genital tract, and related specific molecular changes that occur at the sperm plasma membrane is provided. Understanding these molecular changes may hold essential clues to achieving successful in vitro fertilization with equine gametes.
Keywords	acrosome reaction ; female genitalia ; female reproductive system ; mares ; oocytes ; plasma membrane ; sperm capacitation ; spermatozoa ; stallions ; zona pellucida
Language	English
Dates of publication	2021-0904
Publishing place	Elsevier B.V.
Document type	Article
Note	Pre-press version
ZDB-ID	429674-6
ISSN	1873-2232 ; 0378-4320
ISSN (online)	1873-2232
ISSN	0378-4320
DOI	10.1016/j.anireprosci.2021.106848
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Article ; Online: The less conserved metal-binding site in human CRISP1 remains sensitive to zinc ions to permit protein oligomerization.

Sheng, Jie / Gadella, Bart M / Olrichs, Nick K / Kaloyanova, Dora V / Helms, J Bernd

Scientific reports

2021 Volume 11, Issue 1, Page(s) 5498

Abstract: Cysteine-rich secretory proteins (CRISPs) are a subgroup of the CRISP, antigen 5 and PR-1 (CAP) superfamily that is characterized by the presence of a conserved CAP domain. Two conserved histidines in the CAP domain are proposed to function as a ... ...

Abstract	Cysteine-rich secretory proteins (CRISPs) are a subgroup of the CRISP, antigen 5 and PR-1 (CAP) superfamily that is characterized by the presence of a conserved CAP domain. Two conserved histidines in the CAP domain are proposed to function as a Zn
MeSH term(s)	Binding Sites ; Humans ; Membrane Glycoproteins/chemistry ; Membrane Glycoproteins/genetics ; Membrane Glycoproteins/metabolism ; Protein Multimerization ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Zinc/chemistry ; Zinc/metabolism
Chemical Substances	CRISP1 protein, human ; Membrane Glycoproteins ; Recombinant Proteins ; Zinc (J41CSQ7QDS)
Language	English
Publishing date	2021-03-09
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-021-84926-y
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Article: Membrane Remodeling and Matrix Dispersal Intermediates During Mammalian Acrosomal Exocytosis.

Leung, Miguel Ricardo / Ravi, Ravi Teja / Gadella, Bart M / Zeev-Ben-Mordehai, Tzviya

Frontiers in cell and developmental biology

2021 Volume 9, Page(s) 765673

Abstract: To become fertilization-competent, mammalian sperm must undergo a complex series of biochemical and morphological changes in the female reproductive tract. These changes, collectively called capacitation, culminate in the exocytosis of the acrosome, a ... ...

Abstract	To become fertilization-competent, mammalian sperm must undergo a complex series of biochemical and morphological changes in the female reproductive tract. These changes, collectively called capacitation, culminate in the exocytosis of the acrosome, a large vesicle overlying the nucleus. Acrosomal exocytosis is not an all-or-nothing event but rather a regulated process in which vesicle cargo disperses gradually. However, the structural mechanisms underlying this controlled release remain undefined. In addition, unlike other exocytotic events, fusing membranes are shed as vesicles; the cell thus loses the entire anterior two-thirds of its plasma membrane and yet remains intact, while the remaining nonvesiculated plasma membrane becomes fusogenic. Precisely how cell integrity is maintained throughout this drastic vesiculation process is unclear, as is how it ultimately leads to the acquisition of fusion competence. Here, we use cryoelectron tomography to visualize these processes in unfixed, unstained, fully hydrated sperm. We show that paracrystalline structures within the acrosome disassemble during capacitation and acrosomal exocytosis, representing a plausible mechanism for gradual dispersal of the acrosomal matrix. We find that the architecture of the sperm head supports an atypical membrane fission-fusion pathway that maintains cell integrity. Finally, we detail how the acrosome reaction transforms both the micron-scale topography and the nanoscale protein landscape of the sperm surface, thus priming the sperm for fertilization.
Language	English
Publishing date	2021-12-10
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2737824-X
ISSN	2296-634X
ISSN	2296-634X
DOI	10.3389/fcell.2021.765673
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Article ; Online: HDL mediates reverse cholesterol transport from ram spermatozoa and induces hyperactivated motility.

Bernecic, Naomi C / de Graaf, Simon P / Leahy, Tamara / Gadella, Bart M

Biology of reproduction

2021 Volume 104, Issue 6, Page(s) 1271–1281

Abstract: Reverse cholesterol transport or cholesterol efflux is part of an extensive plasma membrane remodeling process in spermatozoa that is imperative for fertilization. For ram spermatozoa, sheep serum is well known to support in vitro fertilization (IVF), ... ...

Abstract	Reverse cholesterol transport or cholesterol efflux is part of an extensive plasma membrane remodeling process in spermatozoa that is imperative for fertilization. For ram spermatozoa, sheep serum is well known to support in vitro fertilization (IVF), but knowledge of its explicit role is limited. Though, it is postulated to elicit cholesterol efflux owing to the presence of high-density lipoproteins (HDLs) that interact with transmembrane cholesterol transporters, such as adenosinetriphosphate (ATP)-binding cassette transporter A1 (ABCA1) and scavenger receptor class B, type I (SR-BI). In this study, we report that both sheep serum and HDLs were able to elicit cholesterol efflux alone by up to 20-40% (as measured by the boron dipyrromethene (BODIPY)-cholesterol assay). Furthermore, when the antagonists glibenclamide and valspodar were used to inhibit the function of ABCA1 and SR-BI or ABCA1 alone, respectively, cholesterol efflux was only marginally reduced (8-15%). Nevertheless, it is likely that in ram spermatozoa, a specific facilitated pathway of cholesterol efflux is involved in the interaction between cholesterol acceptors and transporters. Interestingly, exposure to HDLs also induced hyperactivated motility, another critical event required for successful fertilization. Taken together, this study details the first report of the dual action of HDLs on ram spermatozoa, providing both an insight into the intricacy of events leading up to fertilization in vivo as well as demonstrating the possible application of HDL supplementation in media for IVF.
MeSH term(s)	Animals ; Biological Transport ; Cholesterol/metabolism ; Lipoproteins, HDL/metabolism ; Male ; Sheep, Domestic/physiology ; Sperm Motility ; Spermatozoa/metabolism
Chemical Substances	Lipoproteins, HDL ; Cholesterol (97C5T2UQ7J)
Language	English
Publishing date	2021-03-02
Publishing country	United States
Document type	Journal Article
ZDB-ID	1118-6
ISSN	1529-7268 ; 0006-3363
ISSN (online)	1529-7268
ISSN	0006-3363
DOI	10.1093/biolre/ioab035
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Article ; Online: A stallion spermatozoon's journey through the mare's genital tract: In vivo and in vitro aspects of sperm capacitation.

Maitan, Paula / Bromfield, Elizabeth G / Stout, Tom A E / Gadella, Bart M / Leemans, Bart

Animal reproduction science

2021 Volume 246, Page(s) 106848

Abstract	Conventional in vitro fertilization is not efficacious when working with equine gametes. Although stallion spermatozoa bind to the zona pellucida in vitro, these gametes fail to initiate the acrosome reaction in the vicinity of the oocyte and cannot, therefore, penetrate into the perivitelline space. Failure of sperm penetration most likely relates to the absence of optimized in vitro fertilization media containing molecules essential to support stallion sperm capacitation. In vivo, the female reproductive tract, especially the oviductal lumen, provides an environmental milieu that appropriately regulates interactions between the gametes and promotes fertilization. Identifying these 'fertilization supporting factors' would be a great contribution for development of equine in vitro fertilization media. In this review, a description of the current understanding of the interactions stallion spermatozoa undergo during passage through the female genital tract, and related specific molecular changes that occur at the sperm plasma membrane is provided. Understanding these molecular changes may hold essential clues to achieving successful in vitro fertilization with equine gametes.
Language	English
Publishing date	2021-09-14
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	429674-6
ISSN	1873-2232 ; 0378-4320
ISSN (online)	1873-2232
ISSN	0378-4320
DOI	10.1016/j.anireprosci.2021.106848
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Article ; Online: Cumulus cells protect the oocyte against saturated free fatty acids.

Aardema, Hilde / Vos, Peter L A M / Gadella, Bart M

Animal reproduction

2018 Volume 15, Issue Suppl 1, Page(s) 737–750

Abstract: In the cow a major characteristic of metabolic stress is an elevated level of plasma free fatty acid, due to increased lipid mobilization from adipose tissue. Elevated levels of free fatty acids in blood (complexed to albumin) are associated with ... ...

Abstract	In the cow a major characteristic of metabolic stress is an elevated level of plasma free fatty acid, due to increased lipid mobilization from adipose tissue. Elevated levels of free fatty acids in blood (complexed to albumin) are associated with increased lipotoxicity in non-adipose tissue. An overview is provided on the negative impact of free fatty acids and the metabolic stress imposed on the oocyte and early embryo and thus on bovine fertility. There is increasing evidence that
Language	English
Publishing date	2018-08-03
Publishing country	Brazil
Document type	Journal Article
ZDB-ID	2227229-X
ISSN	1984-3143 ; 1984-3143
ISSN (online)	1984-3143
ISSN	1984-3143
DOI	10.21451/1984-3143-AR2018-0063
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