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Article: Knockout mouse models of sperm flagellum anomalies.

Escalier, Denise

2006 Volume 12, Issue 4, Page(s) 449–461

Abstract: To date, 21 knockout mouse models are known to bear specific anomalies of the sperm flagellum structures leading to motility disorders. In addition, genes responsible for flagellar defects of two well-known spontaneous mutant mice have recently been ... ...

Abstract	To date, 21 knockout mouse models are known to bear specific anomalies of the sperm flagellum structures leading to motility disorders. In addition, genes responsible for flagellar defects of two well-known spontaneous mutant mice have recently been identified. These models reveal genetic factors, which are required for the proper assembly of the axoneme, the annulus, the mitochondrial sheath and the fibrous sheath. Many of these genetic factors follow unexpected cellular pathways to act on sperm flagellum morphogenesis. These mouse models may bear anomalies which are restricted to the spermatozoa or display more complex phenotypes that often include neuropathies and/or cilia-related diseases. In human, several structural disorders of the sperm flagellum found in brothers or consanguineous men probably have a genetic origin, but the genes involved have not yet been identified. The mutant mice we present in this review are invaluable models, which can be used to identify potential candidate genes for infertile men with specific sperm flagellum anomalies.
MeSH term(s)	Animals ; Humans ; Infertility, Male/genetics ; Infertility, Male/pathology ; Male ; Mice ; Mice, Knockout ; Sperm Tail/pathology ; Spermatogenesis/genetics
Language	English
Publishing date	2006-07
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1286738-x
ISSN	1460-2369 ; 1355-4786
ISSN (online)	1460-2369
ISSN	1355-4786
DOI	10.1093/humupd/dml013
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Article: New insights into the assembly of the periaxonemal structures in mammalian spermatozoa.

Escalier, Denise

Biology of reproduction

2003 Volume 69, Issue 2, Page(s) 373–378

Abstract: Disruption of Ube2b in the mouse has revealed that the regular and symmetric organization of the fibrous sheath of the sperm flagella is dependent on expression of the ubiquitin-conjugating enzyme UBE2B. These data could cast light on how a component of ... ...

Abstract	Disruption of Ube2b in the mouse has revealed that the regular and symmetric organization of the fibrous sheath of the sperm flagella is dependent on expression of the ubiquitin-conjugating enzyme UBE2B. These data could cast light on how a component of the ubiquitin-proteasome pathway participates in the assembly of flagellar periaxonemal structures. Data in the literature support the notion of involvement of ubiquitin-proteasome pathways in the assembly of cytoskeletal components in somatic cells. This review attempts to integrate recent knowledge regarding flagellar components that could be related to proteasome components and, therefore, could be targets of UBE2B in the spermatid. An attempt is made to characterize the human flagellar anomalies of infertile patients, which are the closest to those of Ube2b-deficient mice. These new insights regarding the assembly of mammalian sperm flagella provide a basis for studying the ontogenesis of flagellar accessory structures and suggest leads for medical and genetic investigations.
MeSH term(s)	Animals ; Humans ; Male ; Mice ; Organelles/physiology ; Organelles/ultrastructure ; Protein Processing, Post-Translational/physiology ; Sperm Tail/physiology ; Sperm Tail/ultrastructure ; Spermatogenesis/physiology ; Spermatozoa/physiology ; Spermatozoa/ultrastructure ; Ubiquitin-Conjugating Enzymes/genetics
Chemical Substances	UBE2B protein, human (EC 2.3.2.23) ; Ubiquitin-Conjugating Enzymes (EC 2.3.2.23)
Language	English
Publishing date	2003-08
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	1118-6
ISSN	1529-7268 ; 0006-3363
ISSN (online)	1529-7268
ISSN	0006-3363
DOI	10.1095/biolreprod.103.015719
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Article: Malformations de l'appareil flagellaire du spermatozoïde impliquées dans l'infertilité chez l'homme.

Escalier, Denise / Touré, Aminata

Medecine sciences : M/S

2012 Volume 28, Issue 5, Page(s) 503–511

Abstract: The assembly of sperm flagella involves specific components and processes that are still poorly defined. Several morphological defects of the different structures that compose the axoneme have been described and associated to human male infertility. ... ...

Title translation	Morphological defects of sperm flagellum implicated in human male infertility.
Abstract	The assembly of sperm flagella involves specific components and processes that are still poorly defined. Several morphological defects of the different structures that compose the axoneme have been described and associated to human male infertility. These morphological defects can be classified in 15 main categories. Most of them have been associated to consanguinity and/or familial cases, suggesting their genetic origin. However, so far only few genes have been causally involved.
MeSH term(s)	Axoneme/pathology ; Axoneme/ultrastructure ; Humans ; Infertility, Male/etiology ; Infertility, Male/genetics ; Infertility, Male/pathology ; Male ; Mitochondria/pathology ; Mitochondria/ultrastructure ; Models, Biological ; Sperm Tail/pathology ; Sperm Tail/physiology ; Sperm Tail/ultrastructure ; Spermatogenesis/genetics ; Spermatogenesis/physiology ; Spermatozoa/abnormalities ; Spermatozoa/pathology ; Spermatozoa/physiology ; Spermatozoa/ultrastructure
Language	French
Publishing date	2012-05
Publishing country	France
Document type	English Abstract ; Journal Article ; Review
ZDB-ID	632733-3
ISSN	1958-5381 ; 0767-0974
ISSN (online)	1958-5381
ISSN	0767-0974
DOI	10.1051/medsci/2012285015
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Article: Genetic approach to male meiotic division deficiency: the human macronuclear spermatozoa.

Escalier, Denise

Molecular human reproduction

2002 Volume 8, Issue 1, Page(s) 1–7

Abstract: Human macronuclear spermatozoa (also termed large-headed or macrocephalic spermatozoa) are tetraploid and represent a mammalian model of meiotic division deficiency (MDD). Their genetic origin is strongly suggested by the existence of familial cases. ... ...

Abstract	Human macronuclear spermatozoa (also termed large-headed or macrocephalic spermatozoa) are tetraploid and represent a mammalian model of meiotic division deficiency (MDD). Their genetic origin is strongly suggested by the existence of familial cases. They arise from spermatocytes I with a blockage of organelle displacement at the pachytene stage which disables the assembly of a bipolar meiotic spindle. Spermiogenesis can sometimes be complete, showing that meiotic divisions and spermiogenesis can be decoupled. However, the microtubular manchette is unilateral leading to an irregular sperm nucleus. A severe MDD phenotype also exhibits atrophic flagella. Another MDD phenotype is characterized by arrest at the round spermatid stage, suggesting the existence of factors coordinating meiosis and spermatid differentiation. An attempt is made herein to understand why MDD spermatocytes escape the pachytene and spindle-assembly checkpoints. These human MDD are revisited in the light of Drosophila mutants for cell cycle factors, meiosis division-promoting factors and microtubule components. Several human genes are known to be homologous to genes involved in male MDD in Drosophila mutants, and their number will soon be increased. These candidate genes open the way to investigation of human genes possibly mutated in patients with macronuclear spermatozoa and/or macronuclear spermatids.
MeSH term(s)	Animals ; Disease Models, Animal ; Humans ; Infertility, Male/etiology ; Male ; Meiosis/physiology ; Models, Biological ; Spermatogenesis/physiology ; Spermatozoa/cytology ; Spermatozoa/physiology
Language	English
Publishing date	2002-01
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	1324348-2
ISSN	1460-2407 ; 1360-9947
ISSN (online)	1460-2407
ISSN	1360-9947
DOI	10.1093/molehr/8.1.1
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Zs.A 4482: Show issues

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Article ; Online: New fibrous sheath anomaly in spermatozoa of men with consanguinity.

Escalier, Denise / Albert, Martine

Fertility and sterility

2006 Volume 86, Issue 1, Page(s) 219.e1–9

Abstract: Objective: The cause of the sperm motility impairment was investigated in infertile men.: Design: Case report.: Setting: University-based andrology laboratory.: Patients: Two unrelated consanguineous patients.: Intervention(s): None.: Main ...

Abstract	Objective: The cause of the sperm motility impairment was investigated in infertile men. Design: Case report. Setting: University-based andrology laboratory. Patients: Two unrelated consanguineous patients. Intervention(s): None. Main outcome measure(s): The sperm flagella lengths were measured using quantitative analysis software and their ultrastructural anomalies were quantitatively recorded. Result(s): A total of 67.5% of the flagella were truncated, and 100% lacked the medium region of the ribs of the fibrous sheath. Conclusion(s): The data suggested a morphogenetic anomaly at the stage where rib precursors are formed during spermiogenesis. The consanguinity of these patients suggested a genetic origin for this newly discovered anomaly of the human sperm's fibrous sheath. The family tree appears to indicate an autosomal recessive inheritance.
MeSH term(s)	Adult ; Consanguinity ; Female ; Genetic Predisposition to Disease/genetics ; Humans ; Infertility, Male/genetics ; Infertility, Male/pathology ; Male ; Pedigree ; Sperm Count ; Spermatozoa/abnormalities ; Spermatozoa/classification ; Spermatozoa/pathology
Language	English
Publishing date	2006-07
Publishing country	United States
Document type	Case Reports ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80133-1
ISSN	1556-5653 ; 0015-0282
ISSN (online)	1556-5653
ISSN	0015-0282
DOI	10.1016/j.fertnstert.2005.12.042
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Article: XMR, a dual location protein in the XY pair and in its associated nucleolus in mouse spermatocytes.

Escalier, Denise / Garchon, Henri-Jean

Molecular reproduction and development

2005 Volume 72, Issue 1, Page(s) 105–112

Abstract: Xlr and Xmr are sex-specific genes which are expressed during the meiotic prophase I in the mouse. In spermatocytes, XMR concentrates on the asynapsed regions of the XY chromosomes, suggesting that XMR plays a role in sex chromosome condensation and ... ...

Abstract	Xlr and Xmr are sex-specific genes which are expressed during the meiotic prophase I in the mouse. In spermatocytes, XMR concentrates on the asynapsed regions of the XY chromosomes, suggesting that XMR plays a role in sex chromosome condensation and silencing. The present study shows that in the mouse, XMR also concentrates in the nucleolus which is closely associated with the XY chromosome pair. In this species, the formation of a large fibrillo-granular nucleolus signals the activation of the ribosomal genes, but release of pre-ribosomal particles is inhibited. Using laser confocal microscopy we characterized the distribution of XMR in the XY body relative to the XY chromatin and the nucleolus. Immunoelectron microscopy showed that XMR concentrates in the fibrillo-granular component and the granular component (GC) of the nucleolus. In (T[X;16]16H) mouse spermatocytes, the nucleolus displays little or no activity and does not associate with the XY pair. XMR concentrated only on the XY chromosomes in (T[X;16]16H) mouse spermatocytes. These data suggest that XMR could play a role both in the XY pair and the nucleolus associated to the sex chromosomes.
MeSH term(s)	Animals ; Cell Nucleolus/genetics ; Cell Nucleolus/metabolism ; Cell Nucleolus/ultrastructure ; Chromatin Assembly and Disassembly/genetics ; Chromatin Assembly and Disassembly/physiology ; Gene Silencing/physiology ; Male ; Mice ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Spermatocytes/physiology ; Spermatocytes/ultrastructure ; X Chromosome/genetics ; X Chromosome/metabolism ; X Chromosome/ultrastructure ; Y Chromosome/genetics ; Y Chromosome/metabolism ; Y Chromosome/ultrastructure
Chemical Substances	Nuclear Proteins ; Slx protein, mouse ; Xlr nuclear protein, mouse
Language	English
Publishing date	2005-09
Publishing country	United States
Document type	Journal Article
ZDB-ID	20321-x
ISSN	1098-2795 ; 1040-452X
ISSN (online)	1098-2795
ISSN	1040-452X
DOI	10.1002/mrd.20268
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Article: Asthénozoospermie humaine et anomalies de l'annulus.

Lhuillier, Pierre / Escalier, Denise / Gacon, Gérard / Dulioust, Emmanuel / Touré, Aminata

Medecine sciences : M/S

2010 Volume 26, Issue 8-9, Page(s) 688–689

Title translation	Human asthenozoospermia and structural defects of the annulus.
MeSH term(s)	Animals ; Asthenozoospermia/diagnosis ; Asthenozoospermia/etiology ; Fertility ; Humans ; Infertility, Male ; Male ; Mice ; Sperm Motility
Language	French
Publishing date	2010-08
Publishing country	France
Document type	News
ZDB-ID	632733-3
ISSN	1958-5381 ; 0767-0974
ISSN (online)	1958-5381
ISSN	0767-0974
DOI	10.1051/medsci/2010268-9688
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Article: Un transporteur d'anions est essentiel à la mobilité des spermatozoïdes.

Lhuillier, Pierre / Escalier, Denise / Gacon, Gérard / Touré, Aminata

Medecine sciences : M/S

2008 Volume 24, Issue 3, Page(s) 226–228

Title translation	An anion transporter is essential for spermatozoa motility.
MeSH term(s)	Animals ; Anion Transport Proteins/deficiency ; Anion Transport Proteins/genetics ; Anion Transport Proteins/physiology ; Antiporters/deficiency ; Antiporters/genetics ; Antiporters/physiology ; Contraception/methods ; Humans ; Infertility, Male/genetics ; Infertility, Male/physiopathology ; Male ; Mice ; Mice, Knockout ; Phenotype ; Phosphorylation ; Protein Processing, Post-Translational ; Sperm Capacitation/physiology ; Sperm Motility/physiology ; Sperm Tail/ultrastructure
Chemical Substances	Anion Transport Proteins ; Antiporters ; SLC26A8 protein, human ; Slc26a8 protein, mouse
Language	French
Publishing date	2008-03
Publishing country	France
Document type	News
ZDB-ID	632733-3
ISSN	1958-5381 ; 0767-0974
ISSN (online)	1958-5381
ISSN	0767-0974
DOI	10.1051/medsci/2008243226
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Article ; Online: Evaluation of sperm nuclear integrity in patients with different percentages of decapitated sperm in ejaculates.

Rondanino, Christine / Duchesne, Véronique / Escalier, Denise / Jumeau, Fanny / Verhaeghe, France / Peers, Marie-Claire / Mitchell, Valérie / Rives, Nathalie

Reproductive biomedicine online

2015 Volume 31, Issue 1, Page(s) 89–99

Abstract: The decapitated sperm defect is a rare type of teratozoospermia responsible for male infertility. Spermatozoa from patients affected by this syndrome are used for intracytoplasmic sperm injection (ICSI) although little is known about their DNA integrity. ...

Abstract	The decapitated sperm defect is a rare type of teratozoospermia responsible for male infertility. Spermatozoa from patients affected by this syndrome are used for intracytoplasmic sperm injection (ICSI) although little is known about their DNA integrity. This study evaluated sperm nuclear alterations in four patients and ten fertile men (control group). Sperm samples were examined by light, transmission electron and high-magnification contrast microscopy and analysed after terminal deoxynucleotidyltransferase-mediated dUTP nick end labelling, aniline blue staining and fluorescence in-situ hybridization. Spermatozoa from patients presented varying degrees of decapitation, along with morphological and ultrastructural head abnormalities. Whereas the proportion of spermatozoa with fragmented DNA and numerical chromosome abnormalities was similar in patients 1-3 and controls, the percentage of spermatozoa with hypocondensed chromatin was higher in patients 1-3 than in fertile men. Patient 4 presented a distinct phenotype, with an increased proportion of flagellated spermatozoa with DNA strand breaks as well as increased aneuploidy and diploidy rates compared with controls and with patients 1-3. No successful pregnancy resulted from ICSI although embryos were obtained for three patients. The morphological defects and the nuclear alterations observed in spermatozoa of patients with the decapitated sperm syndrome may have contributed to ICSI failures.
MeSH term(s)	Adult ; Cell Nucleus/ultrastructure ; Chromosome Aberrations ; DNA Fragmentation ; Humans ; Infertility, Male/genetics ; Infertility, Male/pathology ; Male ; Microscopy, Electron, Transmission ; Semen Analysis ; Sperm Injections, Intracytoplasmic ; Sperm Motility ; Spermatozoa/physiology ; Spermatozoa/ultrastructure
Language	English
Publishing date	2015-07
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2113823-0
ISSN	1472-6491 ; 1472-6483
ISSN (online)	1472-6491
ISSN	1472-6483
DOI	10.1016/j.rbmo.2015.04.002
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Zs.A 5792: Show issues

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Article ; Online: Septins at the annulus of mammalian sperm.

Toure, Aminata / Rode, Baptiste / Hunnicutt, Gary R / Escalier, Denise / Gacon, Gérard

Biological chemistry

2011 Volume 392, Issue 8-9, Page(s) 799–803

Abstract: The annulus is an electron-dense ring structure connecting the midpiece and the principal piece of the mammalian sperm flagellum. Proteins from the septin family have been shown to localize to the annulus. A septin complex is assembled early in ... ...

Abstract	The annulus is an electron-dense ring structure connecting the midpiece and the principal piece of the mammalian sperm flagellum. Proteins from the septin family have been shown to localize to the annulus. A septin complex is assembled early in spermiogenesis with the cochaperone DNAJB13 and, in mature sperm, associates with Testis Anion Transporter 1; SLC26A8 (Tat1), a transmembrane protein of the SLC26 family. Studies in mice have shown that the annulus acts as a barrier to protein diffusion and controls correct organization of the midpiece. Consistent with these findings, absence of the annulus is associated with flagellum differentiation defects and asthenozoospermia in humans.
MeSH term(s)	Animals ; Anion Transport Proteins/metabolism ; Antiporters/metabolism ; Asthenozoospermia/metabolism ; Asthenozoospermia/physiopathology ; Heat-Shock Proteins/metabolism ; Humans ; Infertility, Male/metabolism ; Infertility, Male/physiopathology ; Male ; Mice ; Models, Biological ; Protein Binding ; Sperm Tail/metabolism ; Sperm Tail/physiology ; Spermatozoa/metabolism ; Spermatozoa/physiology
Chemical Substances	Anion Transport Proteins ; Antiporters ; DNAJB13 protein, human ; Heat-Shock Proteins ; SLC26A8 protein, human
Language	English
Publishing date	2011-08
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1334659-3
ISSN	1437-4315 ; 1431-6730 ; 1432-0355
ISSN (online)	1437-4315
ISSN	1431-6730 ; 1432-0355
DOI	10.1515/BC.2011.074
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