A novel epididymal quiescence factor inhibits sperm motility by modulating NOS activity and intracellular NO‐cGMP pathway

Ghosh, Prasanta; Mukherjee, Sandipan; Bhoumik, Arpita; Dungdung, Sandhya Rekha

doi:10.1002/jcp.26275

Cited by 6 publications

(5 citation statements)

References 55 publications

(72 reference statements)

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“…Numerous proteins are identified to be involved in sperm maturation in the epididymis (Myles & Primakoff 1984, Myles et al 1987, Vreeburg et al 1990, Hunnicutt et al 1997, Sipilä et al 2006. Secretory proteins from caput initiate sperm motility (Xu et al 2010) and the proteins from cauda regulate sperm motility (Dungdung & Majumder 2003, Das et al 2010, Ghosh et al 2018 or affect sperm capacitation (Roberts et al 2003, Roberts et al 2006, Ni et al 2009, Krapf et al 2012, Saewu et al 2017. In this study, the sperm hyperactivation indexes (such as VAP, VSL, VCL and ALH) and the level of sperm protein phosphorylation decreased significantly after sperm capacitation of the knockdown GLB1L4 rats was induced by BSA and Ca 2+ .…”

Section: Discussionmentioning

confidence: 99%

Palmitoylated GLB1L4 transfers via exosomes to maintain sperm function in rat epididymis

et al. 2021

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Epididymal specific proteins play a crucial role in sperm maturation. Some of the post-translational modified proteins are transported from the caput to the cauda of the epididymis through exosomes which regulate the function of sperm in cauda epididymis. Rat beta-galactosidase-1-like protein 4 (GLB1L4) expressed specifically in the caput epididymis, localizes on the sperm; however, the regulatory ways in which GLB1L4 protein interacts with sperm to maintain sperm function are unclear. In this study, knockdown of rat GLB1L4 could inhibit in vitro capacitation of sperm in cauda epididymis and reduce the fertility of the male rats by injection of special lentivirus-shRNA into caput epididymis. Moreover, a considerable proportion of GLB1L4 proteins from rat caput epididymis were loaded on exosomes. The exosomes loaded GLB1L4 from in vitro primary rat caput epididymal epithelial cells could bind with spermatozoa in cauda epididymis. Further, the palmitoylation status of cysteine residues at the 12th and 15th sites of the protein molecule could significantly affect cellular localization of GLB1L4 protein. It was identified that most of GLB1L4 was palmitoylated in the presence of exosomes from primary caput epididymal cells and the level of palmitoylated GLB1L4 in the exosomes could be inhibited by 2-bromopalmitate (2-BP). These results suggested that the palmitoylated GLB1L4 from rat caput epididymis could be transported to the cauda epididymis to regulate the sperm function by exosomes.

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Section: Discussionmentioning

confidence: 99%

Palmitoylated GLB1L4 transfers via exosomes to maintain sperm function in rat epididymis

et al. 2021

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“…19,20 In another study, a novel sperm motility-inhibiting protein of 59 kDa was purified from caprine epididymal plasma. 21 In view of the above, in the present study, an attempt was made to isolate and characterize the sperm motility-inhibiting protein(s) of ram CEP. The purification process involved sequential enrichment of the sperm motility-inhibiting activity of ram CEP through hydroxyapatite (HA) gel adsorption followed by anion exchange chromatography.…”

Section: Introductionmentioning

confidence: 99%

“…Purification and characterization of two sperm motility‐inhibiting factors namely motility‐inhibitory factor I and II (MIF‐I and II) of about 100 and 160 kDa, respectively, from goat CEP was reported 19,20 . In another study, a novel sperm motility‐inhibiting protein of 59 kDa was purified from caprine epididymal plasma 21 …”

Section: Introductionmentioning

confidence: 99%

Purification and partial characterization of a sperm motility‐inhibitory protein of ram cauda epididymal plasma

Lal,

Jorasia,

Rathore

et al. 2024

Cell Biochemistry & Function

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Mammalian sperm remain quiescent but fertile for several weeks in cauda epididymis. Although several sperm quiescent factors of epididymal plasma have been identified in goat, pig and cattle; however, little is known in sheep. In the present study, purification and characterization of a novel sperm quiescent protein of ovine cauda epididymal plasma (CEP) was carried out. The sperm quiescent protein was partially purified by hydroxyapatite gel adsorption chromatography followed by DEAE‐sepharose® anion exchange chromatography. In the latter, the sperm quiescent activity was eluted both in 0.05 and 0.2 M potassium phosphate buffer (pH 7.5) fractions having a predominant protein of about 80 and 70 kDa with 87% and 63% homogeneity, respectively. The proteins were designated as motility‐inhibitory factor of sheep I and II (MIFS‐I and II), respectively. Significant (about 60%) inhibition of sperm motility was observed following treatment of cauda epididymal sperm with 6 and 12 µg/mL of partially purified MIFS‐I and II, respectively. Specific activities of the partially purified MIFS‐I and II were 563 and 261 U/mg of protein, while the fold‐purification of the activity were 5119 and 2373, respectively. Both the proteins were heat‐labile and the activity was completely lost following incubation at 100°C for 5 min. Further, the partially purified MIFS‐I (5 µg/mL) caused significant reduction in in vitro sperm capacitation and slight decline in tyrosine phosphorylated p72 and p52 proteins; however the protein was nontoxic to sperm. Mass spectrometric analysis of MIFS‐I revealed significant identity with human semaphorin 3D. Both dot blot and western blot analysis demonstrated cross‐reactivity of MIFS‐I with polyclonal anti‐human SEMA3D antibody. It was concluded that the MIFS‐I of ovine CEP was putative ovine semaphorin 3D protein having potent sperm quiescent and decapacitating activities and it possibly acts through inhibition of protein tyrosine phosphorylation.

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“…The common causes include age, lifestyle changes, inflammation, exposure to chemical pesticides, electromagnetic radiation, and air pollution [ 1 – 3 ]. These factors can lead to abnormal semen coagulation and liquefaction, immune infertility, endocrine disorders, abnormal sperm structure, abnormal chromosomes, and varicocele, thus leading to a decrease in sperm motility [ 4 , 5 ]. However, in addition to these causes, 30–40% of asthenozoospermia cases still remain unexplained and are called idiopathic asthenozoospermia (AST).…”

Section: Introductionmentioning

confidence: 99%

The Activated AMPK/mTORC2 Signaling Pathway Associated with Oxidative Stress in Seminal Plasma Contributes to Idiopathic Asthenozoospermia

Cao

Xia

et al. 2022

Oxidative Medicine and Cellular Longevity

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Asthenozoospermia is a common form of abnormal sperm quality in idiopathic male infertility. While most sperm-mediated causes have been investigated in detail, the significance of seminal plasma has been neglected. Herein, we aimed to investigate the possible pathogenic factors leading to decreased sperm motility based on seminal plasma. Semen was collected from normo- (NOR, n = 70 ), idiopathic oligo- (OLI, n = 57 ), and idiopathic asthenozoospermic (AST, n = 53 ) patients. Using attenuated total reflection-Fourier transform infrared coupled with chemometrics, distinct differences in the biochemical compositions of nucleic acids, protein structure (amides I, II, and III), lipids, and carbohydrates in seminal plasma of AST were observed when compared to NOR and OLI. Compared with NOR and OLI, the levels of peptide aggregation, protein phosphorylation, unsaturated fatty acid, and lipid to protein ratio were significantly increased in AST; however, the level of lipid saturation was significantly decreased in seminal plasma of AST. Compared with NOR, the levels of ROS, MDA, 8-iso-prostaglandin F2α (8-isoPGF2α), and the ratio of phospho-AMPKα/AMPKα1 were significantly increased in AST; however, the levels of SOD, glutathione S-transferase (GSTs), protein carbonyl derivative (PC), and the ratio of phospho-Rictor/Rictor were significantly decreased in seminal plasma of AST. Changes of the AMPK/mTORC2 signaling in the seminal microenvironment possibly induce abnormal glucose and lipid metabolism, which impairs energy production. Oxidative stress potentially damages seminal plasma lipids and proteins, which in turn leads to impaired sperm structure and function. These findings provide evidence that the changes in seminal plasma compositions, oxidative stress, and activation of the AMPK/mTORC2 signaling contribute to the development of asthenozoospermia.

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A novel epididymal quiescence factor inhibits sperm motility by modulating NOS activity and intracellular NO‐cGMP pathway

Cited by 6 publications

References 55 publications

Palmitoylated GLB1L4 transfers via exosomes to maintain sperm function in rat epididymis

Palmitoylated GLB1L4 transfers via exosomes to maintain sperm function in rat epididymis

Purification and partial characterization of a sperm motility‐inhibitory protein of ram cauda epididymal plasma

The Activated AMPK/mTORC2 Signaling Pathway Associated with Oxidative Stress in Seminal Plasma Contributes to Idiopathic Asthenozoospermia

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