Direct evidence for the secretion of lactoferrin and its binding to sperm in the porcine epididymis

Jin, Yin‐Zhe; Bannai, Shiro; Dacheux, Françoise; Dacheux, Jean‐Louis; Okamura, Nobuyuki

doi:10.1002/(sici)1098-2795(199708)47:4<490::aid-mrd16>3.0.co;2-#

Cited by 47 publications

(9 citation statements)

References 36 publications

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“…Ion chelators in seminal plasma, such as lactoferrin (LF), also protect sperm against effects of lipid peroxidation ( Ochsendorf, 1999 ). Lactoferrin sequesters ionic iron ( Nozaki et al ., 2003 ) and adsorption to sperm during epididymal transit ( Jin et al ., 1997 ) and ejaculation ( Thaler et al ., 1990 ). In stallions, LF represents 41.2% of all proteins secreted by the epididymis (Fouchecourt et al ., 2000) and high concentrations of LF in horse and dog seminal plasma relate to total number of sperm ( Kikuchi et al ., 2003a , b ).…”

Section: Seminal Plasma Proteinsmentioning

confidence: 99%

Seminal plasma proteins and metabolites: effects on sperm function and potential as fertility markers

Moura¹,

Memili²,

Portela³

et al. 2018

Anim Reprod

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Molecular components of sperm and in the media surrounding them influence male fertility. In this regard, seminal plasma proteins and metabolites modulate various reproductive events, including sperm motility and capacitation, cell protection, acrosome reaction, fertilization and embryonic development. Empirical associations between seminal proteins and metabolites and fertility indicate that these molecules are potential molecular markers of male reproductive status in cattle and other species.

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Section: Seminal Plasma Proteinsmentioning

confidence: 99%

Seminal plasma proteins and metabolites: effects on sperm function and potential as fertility markers

Moura¹,

Memili²,

Portela³

et al. 2018

Anim Reprod

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“…A wide variety of proteins including antimicrobial proteins released into the lumen of epididymis bind sperm and are thought to play an important role in epididymal immunity in addition to their role in sperm maturation [15]. Examples of antimicrobial proteins reported in the male reproductive tract include human cationic antimicrobial protein (hCAP18, a cathelicidin) [16], defensins [17-20], the epididymal β-defensin member Bin1b [21], cystatins [22,23], lactoferrin [24] seminalplasmin [25] and seminogelin-derived peptides [26]. Earlier we identified and characterized the sperm binding epididymal proteins of the HE2 family [27], which show homology to the antimicrobial β-defensins.…”

Section: Introductionmentioning

confidence: 99%

Untitled

Yenugu

Hamil

French

et al. 2004

Reprod Biol Endocrinol

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“…Several epididymal AMPs and proteins, including β-defensins, lactoferrin, EPPIN, lysozyme and lysozyme-like protein 6, SPAG11 isoforms and others, have dual functions. In addition to their antimicrobial roles, they bind to spermatozoa and affect their function, including fertilizing ability, in both rodent models and humans ( Jin et al , 1997 ; Yenugu et al , 2004 ; Zhou et al , 2004 ; Wei et al , 2013 ; Huang et al , 2017 ). Similarly, cathelicidin, CRES, CRES2 and CRES3 bind to epididymal spermatozoa for reasons not yet known ( Malm et al , 2000 ; Cornwall, unpublished observations).…”

Section: Discussionmentioning

confidence: 99%

“…For example, the rodent and human epididymal epithelium secretes multiple β-defensins, SPAG11 (HE2) and its isoforms, cathelicidin (hCAP18, mouse CAMP) and other AMPs into the lumen ( Malm et al , 2000 ; Yenugu et al , 2003 ; Hall et al , 2007 ; Yenugu and Narmadha, 2010 ). The epididymis also secretes several antimicrobial proteins including the secretory leukoprotease inhibitor (SLPI), lactoferrin, lysozyme, epididymal protease inhibitor (EPPIN), lipocalin-2 and others ( Jin et al , 1997 ; Hall et al , 2002 ; Yenugu et al , 2004 ; Jenssen and Hancock, 2009 ; Silva et al , 2012 ). Despite their critical roles in protecting the germline, mechanisms by which the epididymal AMPs and proteins defend against pathogens remain poorly understood.…”

Section: Introductionmentioning

confidence: 99%

Host defense functions of the epididymal amyloid matrix

Myers

Hastert

2022

Molecular Human Reproduction

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The epididymal lumen is an immunologically distinct environment. It maintains tolerance for the naturally antigenic spermatozoa to allow their maturation into functional cells while simultaneously defending against pathogens that can ascend the male tract and cause infertility. We previously demonstrated that a nonpathological amyloid matrix that includes several CRES (cystatin-related epididymal spermatogenic) subgroup family members is distributed throughout the mouse epididymal lumen but its function was unknown. Here we reveal a role for the epididymal amyloid matrix in host defense and demonstrate that the cystatin-related epididymal spermatogenic (CRES) amyloids and CD-1 mouse epididymal amyloid matrix exhibit potent antimicrobial activity against bacterial strains that commonly cause epididymal infections in men. We show the CRES and epididymal amyloids use several defense mechanisms including bacterial trapping, disruption of bacterial membranes, and promotion of unique bacterial ghost-like structures. Remarkably, these antimicrobial actions varied depending on the bacterial strain indicating CRES amyloids and the epididymal amyloids elicit strain-specific host defense responses. We also demonstrate that the CRES monomer and immature assemblies of the epididymal amyloid transitioned into advanced structures in the presence of bacteria, suggesting their amyloid-forming/shape-shifting properties allows for a rapid reaction to a pathogen and provides an inherent plasticity in their host defense response. Together, our studies reveal new mechanistic insight into how the male reproductive tract defends against pathogens. Future studies using a mouse model for human epididymitis are needed to establish the epididymal amyloid responses to pathogens in vivo. Broadly, our studies provide an example of why nature has maintained the amyloid fold throughout evolution.

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Direct evidence for the secretion of lactoferrin and its binding to sperm in the porcine epididymis

Cited by 47 publications

References 36 publications

Seminal plasma proteins and metabolites: effects on sperm function and potential as fertility markers

Seminal plasma proteins and metabolites: effects on sperm function and potential as fertility markers

Untitled

Host defense functions of the epididymal amyloid matrix

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