<i>In Vivo</i> and <i>In Vitro</i> Sperm Interaction with Oviductal Epithelial Cells of Llama

Apichela, Silvana Andrea; Jiménez-Díaz, MA; Roldán‐Olarte, Mariela; Valz-Gianinet, JN; Miceli, Dora C.

doi:10.1111/j.1439-0531.2008.01125.x

Cited by 16 publications

(20 citation statements)

References 30 publications

(71 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…1995b; Apichela et al. 2009). Strategies underlying sperm binding have been considered, especially in terms of preovulatory sperm storage and suppression of full membranous maturation (Hunter 2011).…”

Section: Discussionmentioning

confidence: 99%

Sperm storage and spermatozoa interaction with epithelial cells in oviduct of Chinese soft‐shelled turtle, Pelodiscus sinensis

Chen

Zhang

Yuan

et al. 2015

Ecology and Evolution

View full text Add to dashboard Cite

Spermatozoa are known to be stored within the female genital tract after mating in various species to optimize timing of reproductive events such as copulation, fertilization, and ovulation. The mechanism supporting long-term sperm storage is still unclear in turtles. The aim of this study was to investigate the interaction between the spermatozoa and oviduct in Chinese soft-shelled turtle by light and electron microscopy to reveal the potential cytological mechanism of long-term sperm storage. Spermatozoa were stored in isthmus, uterine, and vagina of the oviduct throughout the year, indicating long-term sperm storage in vivo. Sperm heads were always embedded among the cilia and even intercalated into the apical hollowness of the ciliated cells in the oviduct mucosal epithelium. The stored spermatozoa could also gather in the gland conduit. There was no lysosome distribution around the hollowness of the ciliated cell, suggesting that the ciliated cells of the oviduct can support the spermatozoa instead of phagocytosing them in the oviduct. Immune cells were sparse in the epithelium and lamina propria of oviduct, although few were found inside the blood vessel of mucosa, which may be an indication of immune tolerance during sperm storage in the oviduct of the soft-shelled turtle. These characteristics developed in the turtle benefited spermatozoa survival for a long time as extraneous cells in the oviduct of this species. These findings would help to improve the understanding of reproductive regularity and develop strategies of species conservation in the turtle. The Chinese soft-shelled turtle may be a potential model for uncovering the mechanism behind the sperm storage phenomenon.

show abstract

Section: Discussionmentioning

confidence: 99%

Sperm storage and spermatozoa interaction with epithelial cells in oviduct of Chinese soft‐shelled turtle, Pelodiscus sinensis

Chen

Zhang

Yuan

et al. 2015

Ecology and Evolution

View full text Add to dashboard Cite

show abstract

“…Sperm are held in the reservoir by being bound to oviductal epithelium. In vitro, binding to the oviductal epithelium has been shown to prolong the motile lifespan of sperm of several species [6,[8][9][10][11][12]. Release of sperm from the reservoir is gradual, which helps to reduce the risk of polyspermy [13,14].…”

Section: Introductionmentioning

confidence: 99%

Alterations to the Bull Sperm Surface Proteins That Bind Sperm to Oviductal Epithelium1

Hung

Suárez

2012

Biology of Reproduction

View full text Add to dashboard Cite

Three Binder of SPerm proteins (BSP1, BSP3, BSP5) are secreted by bovine seminal vesicles into seminal plasma and adsorbed onto sperm. When sperm inseminated into the female reach the oviduct, the BSP proteins bind them to its epithelial lining, forming a sperm storage reservoir. Previously, we reported that binding of capacitated sperm to oviductal epithelium in vitro is lower than that of uncapacitated sperm and we proposed that reduced binding was due to loss of BSP proteins during capacitation. Because of differences in amino acid sequences, we predicted that each BSP would respond differently to capacitating conditions. To test whether all three BSP proteins were lost from sperm during capacitation and whether the kinetics of loss differed among the three BSP proteins, ejaculated bull sperm were incubated under various capacitating conditions, and then the amounts of BSP proteins remaining on the sperm were assayed by Western blotting. Capacitation was assayed by analysis of protein tyrosine phosphorylation. While loss of BSP1 was not detected, most of the BSP5 was lost from sperm during incubation in TALP medium, even without addition of the capacitation enhancers heparin and dbcAMP-IBMX. Surprisingly, a smaller molecular mass was detected by anti-BSP3 antibodies in extracts of incubated sperm. Its identity was confirmed as BSP3 by mass spectrometry, indicating that BSP3 undergoes modification on the sperm surface. These changes in the composition of BSP proteins on sperm could play a role in releasing sperm from the storage reservoir by modifying sperm interactions with the oviductal epithelium.

show abstract

“…We previously demonstrated that the llama sperm reservoir is formed at the utero-tubal junction by means of a lectin-like molecule that mediates sperm recognition of N-acetylgalactosamine (GalNAc) and galactose in the female oviduct (Apichela et al, 2010). Under normal conditions, sperm remain attached to the llama utero-tubal junction at least 28 hr after mating (Apichela, Jiménez-Díaz, Roldán-Olarte, Valz-Gianinet, & Miceli, 2009); surgical removal of the bulbourethral glands diminished such sperm attachment (Apichela et al, 2014). The current study sought to isolate and identify the GalNAc-binding lectins present on llama sperm, and to test the hypothesis that they are provided by seminal plasma.…”

Section: Introductionmentioning

confidence: 99%

SL15: A seminal plasma‐derived lectin from the sperm of llama (Lama glama)

Zampini

Sequeira

Argañaraz

et al. 2017

Molecular Reproduction Devel

View full text Add to dashboard Cite

The oviductal sperm reservoir of South American camelids is formed when sperm bind to N-acetylgalactosamine (GalNAc) on the surface of oviductal epithelium. The aim of this study was to characterize the GalNAc-binding proteins on llama sperm, and to establish their origin. Sperm-adsorbed proteins were extracted with 0.5 M KCl in Hepes-balanced salts. Sperm-adsorbed and seminal plasma proteins were then subjected to ligand blotting for their GalNAc affinity, and the labeled bands were identified by mass spectrometry. Three proteins were identified in seminal plasma versus only one in the sperm-adsorbed population; SL15, a seminal lectin, was common to both. SL15 is a homologue of Zymogen granule protein 16, homolog B-like, which belongs to the Jacalin-related lectin family. This lectin is likely presented to sperm via seminal plasma since epididymal sperm are not capable of binding GalNAc, whereas ejaculated sperm does, and its transcript was enriched predominantly in the prostate and bulbourethral glands. This is the first report of a seminal lectin in South American camelids that originates in the male reproductive tract, and is probably involved in sperm reservoir formation.

show abstract

In Vivo and In Vitro Sperm Interaction with Oviductal Epithelial Cells of Llama

Cited by 16 publications

References 30 publications

Sperm storage and spermatozoa interaction with epithelial cells in oviduct of Chinese soft‐shelled turtle, Pelodiscus sinensis

Sperm storage and spermatozoa interaction with epithelial cells in oviduct of Chinese soft‐shelled turtle, Pelodiscus sinensis

Alterations to the Bull Sperm Surface Proteins That Bind Sperm to Oviductal Epithelium1

SL15: A seminal plasma‐derived lectin from the sperm of llama (Lama glama)

Contact Info

Product

Resources

About