Mammalian Sperm Acrosome: Formation, Contents, and Function

Abou-Haïla, A; Tulsiani, D. R. P.

doi:10.1006/abbi.2000.1880

Cited by 215 publications

(184 citation statements)

References 85 publications

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“…3D), although neither of these genes was detected in the microarray study, likely due to sensitivity issues with gene expression arrays. 32 We also attempted to confirm an increase in the expression of several other genes that may be involved in secretion, including glutamate receptor (Grin2c), 33 non voltage-gated sodium channel (Scnn1a), 34,35 and sperm acrosome associated 1 (Spaca1), 36,37 but were unable to validate upregulation of these genes. Taken together, our results suggest that Isl-1 may mediate increased β-cell functionality through a subset of genes involved in protein trafficking, metabolism, development, signal transduction and transcriptional regulation.…”

Section: β-Cell Function In Pdx1mentioning

confidence: 99%

Elevation of transcription factor Islet-1 levels in vivo increases β-cell function but not β-cell mass

Liu

Walp

May

2012

Islets

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Section: β-Cell Function In Pdx1mentioning

confidence: 99%

Elevation of transcription factor Islet-1 levels in vivo increases β-cell function but not β-cell mass

Liu

Walp

May

2012

Islets

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“…The acrosome is a large, Golgi-derived lysosome-like organelle that overlies the nucleus in the apical region of the sperm head. This organelle secretes enzymes such as the serine protease, acrosin, which helps sperm penetration into the zona pellucida (Abou-Haila & Tulsiani 2000). In addition to the secretion of enzymes, the acrosome reaction brings exposure of the inner acrosomal membrane to the outside by breaking the organelle.…”

Section: Introductionmentioning

confidence: 99%

The mechanism of sperm–oocyte fusion in mammals

Kaji¹,

Kudo²

2004

Reproduction

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Sperm-oocyte fusion is one of the most impressive events in sexual reproduction, and the elucidation of its molecular mechanism has fascinated researchers for a long time. Because of the limitation of materials and difficulties in analyzing membrane protein -protein interactions, many attempts have failed to reach this goal. Recent studies involving gene targeting have clearly demonstrated the various molecules that are involved in sperm-oocyte binding and fusion. Sperm ADAMs (family of proteins with a disintegrin and metalloprotease domain), including fertilin a, fertilin b and cyritestin, have been investigated and found to be important for binding rather than for fusion and painstaking studies have raised suspicions that their putative receptors, oocyte integrins, are necessary for the sperm -oocyte interaction. Recently, several studies have focused the spotlight on CD9 and glycosylphosphatidylinositol (GPI)-anchored proteins on oocytes, and epididymal protein DE on sperm, as candidate molecules involved in sperm-oocyte fusion. Lack of, or interference with the function of, these proteins can disrupt the sperm -oocyte fusion without changing the binding. In this review we highlight the candidate molecules involved in the sperm-oocyte interaction suggested from the recent progress in this research field.

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“…In addition, the sperm head contains the acrosome, an enzyme-filled membrane-enclosed vesicle that is required for the sperm-egg binding and the penetration of egg vestments during fertilization (26). The acrosome is formed from vesicles and saccules derived from the Golgi apparatus during the initial steps of spermiogenesis (27). Another important sperm-specific structure is the tail, which is responsible of energy production and mobility of the spermatozoa, and these essential tasks are achieved by the acquisition of additional cytoskeletal structures, namely the outer dense fibers and fibrous sheath, surrounding the sperm axoneme (26,28).…”

mentioning

confidence: 99%

Spermatocyte/Spermatid-specific Thioredoxin-3, a Novel Golgi Apparatus-associated Thioredoxin, Is a Specific Marker of Aberrant Spermatogenesis

Jiménez

Wei

Rawe

et al. 2004

Journal of Biological Chemistry

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Mammalian germ cells are endowed with a complete set of thioredoxins (Trx), a class of redox proteins located in specific structures of the spermatid and sperm tail. We report here the characterization, under normal and pathological conditions, of a novel thioredoxin with a germ line-restricted expression pattern, named spermatocyte/spermatid-specific thioredoxin-3 (SPTRX-3). The human SPTRX-3 gene maps at 9q32, only 50 kb downstream from the TRX-1 gene from which it probably originated as genomic duplication. Therefore, human SPTRX-3 protein comprises a unique thioredoxin domain displaying high homology with the ubiquitously expressed TRX-1. Among the tissues investigated, Sptrx-3 mRNA is found exclusively in the male germ cells at pachytene spermatocyte and round spermatid stages. Light and electron microscopy show SPTRX-3 protein to be predominately located in the Golgi apparatus of pachytene spermatocytes and round and elongated spermatids, with a transient localization in the developing acrosome of round spermatids. In addition, increased levels of SPTRX-3, possibly caused by overexpression, are observed in morphologically abnormal human spermatozoa from infertile men. In addition, SPTRX-3 is identified as a novel postobstruction autoantigen. In this report, we propose that SPTRX-3 can be used as a specific marker for diverse sperm and testis pathologies. SPTRX-3 is the first thioredoxin specific to the Golgi apparatus, and its function within this organelle might be related to the post-translational modification of proteins required for germ cell-specific functions, such as acrosomal biogenesis.

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Mammalian Sperm Acrosome: Formation, Contents, and Function

Cited by 215 publications

References 85 publications

Elevation of transcription factor Islet-1 levels in vivo increases β-cell function but not β-cell mass

Elevation of transcription factor Islet-1 levels in vivo increases β-cell function but not β-cell mass

The mechanism of sperm–oocyte fusion in mammals

Spermatocyte/Spermatid-specific Thioredoxin-3, a Novel Golgi Apparatus-associated Thioredoxin, Is a Specific Marker of Aberrant Spermatogenesis

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