Identification of chloride intracellular channel proteins in spermatozoa

Myers, Kimberley; Somanath, Payaningal R.; Berryman, Mark; Vijayaraghavan, Srinivasan

doi:10.1016/j.febslet.2004.04.017

Cited by 20 publications

(9 citation statements)

References 33 publications

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“…This is consistent with an earlier report that Clic4 transcripts increase rapidly in 3T3L1 cells induced to differentiate into adipocytes in vitro [41]. Previous studies had also identified the presence of CLIC4 along with CLIC1 and CLIC5 in bovine spermatozoa [42]. Our probing in mouse testes indicates a predominant expression of CLIC4 in spermatogonia implying an early role for the protein in spermatogenesis.…”

Section: Discussionsupporting

confidence: 93%

Detection of differential fetal and adult expression of chloride intracellular channel 4 (CLIC4) protein by analysis of a green fluorescent protein knock-in mouse line

et al. 2014

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BackgroundChloride Intracellular Channel 4 (CLIC4) is one of seven members in the closely related CLIC protein family. CLIC4 is involved in multiple cellular processes including apoptosis, cellular differentiation, inflammation and endothelial tubulogenesis. Despite over a decade of research, no comprehensive in situ expression analysis of CLIC4 in a living organism has been reported. In order to fulfill this goal, we generated a knock-in mouse to express Green Fluorescent Protein (GFP) from the CLIC4 locus, thus substituting the GFP coding region for CLIC4. We used GFP protein expression to eliminate cross reaction with other CLIC family members.ResultsWe analyzed CLIC4 expression during embryonic development and adult organs. During mid and late gestation, CLIC4 expression is modulated particularly in fetal brain, heart, thymus, liver and kidney as well as in developing brown adipose tissue and stratifying epidermis. In the adult mouse, CLIC4 is highly expressed globally in vascular endothelial cells as well as in liver, lung alveolar septae, pancreatic acini, spermatogonia, renal proximal tubules, cardiomyocytes and thymic epithelial cells. Neural expression included axonal tracks, olfactory bulb, Purkinje cell layer and dentate gyrus. Renal CLIC4 expression was most pronounced in proximal tubules, although altered renal function was not detected in the absence of CLIC4. Myeloid cells and B cells of the spleen are rich in CLIC4 expression as are CD4 and CD8 positive T cells.ConclusionsIn a comprehensive study detailing CLIC4 expression in situ in a mouse model that excludes cross reaction with other family members, we were able to document previously unreported expression for CLIC4 in developing fetus, particularly the brain. In addition, compartmentalized expression of CLIC4 in specific adult tissues and cells provides a focus to explore potential functions of this protein not addressed previously.

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Section: Discussionsupporting

confidence: 93%

Detection of differential fetal and adult expression of chloride intracellular channel 4 (CLIC4) protein by analysis of a green fluorescent protein knock-in mouse line

et al. 2014

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“…The ClC proteins are present in bovine epididymal spermatozoa12 and can bind PP1γ2, a key enzyme involved in regulating sperm maturation and motility. The ClC-3 channels are expressed in healthy human spermatozoa and are involved in sperm volume regulation 6.…”

Section: Discussionmentioning

confidence: 99%

“…Inhibition of transmembrane Cl − transport results in failure of sperm penetration and migration through surrogate cervical mucus 11. ClC channels have been found in the bovine testicular and epididymal spermatozoa,12 and recently in healthy human spermatozoa 6. The ClC proteins can bind to protein phosphatase 1 (PP1γ2), which is required for regulating sperm motility 13.…”

Section: Introductionmentioning

confidence: 99%

Chloride channels are involved in sperm motility and are downregulated in spermatozoa from patients with asthenozoospermia

Liu

Zou

et al. 2017

Asian J Androl

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Human spermatozoa encounter an osmotic decrease from 330 to 290 mOsm l−1 when passing through the female reproductive tract. We aimed to evaluate the role of chloride channels in volume regulation and sperm motility from patients with asthenozoospermia. Spermatozoa were purified using Percoll density gradients. Sperm volume was measured as the forward scatter signal using flow cytometry. Sperm motility was analyzed using computer-aided sperm analysis (CASA). When transferred from an isotonic solution (330 mOsm l−1) to a hypotonic solution (290 mOsm l−1), cell volume was not changed in spermatozoa from normozoospermic men; but increased in those from asthenozoospermic samples. The addition of the chloride channel blockers, 4,4′-diisothiocyanatostilbene-2,2′- isulfonic acid (DIDS) or 5-nitro-2-(3-phenylpropylamino) benzoic acid (NPPB) to the hypotonic solution caused the normal spermatozoa to swell but did not increase the volume of those from the asthenozoospermic semen. DIDS and NPPB decreased sperm motility in both sets of semen samples. The inhibitory effect of NPPB on normal sperm motility was much stronger than on spermatozoa from the asthenozoospermic samples. Both sperm types expressed ClC-3 chloride channels, but the expression levels in the asthenozoospermic samples were much lower, especially in the neck and mid-piece areas. Spermatozoa from men with asthenozoospermia demonstrated lower volume regulating capacity, mobility, and ClC-3 expression levels (especially in the neck) than did normal spermatozoa. Thus, chloride channels play important roles in the regulation of sperm volume and motility and are downregulated in cases of asthenozoospermia.

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“…The sperm motility is a key factor to determine semen quality and its fertilizing capacity (104)(105)(106), which is widely controlled by a variety of factors (107)(108)(109). The phospholipid composition and cholesterol to phospholipid ratio are predominant factors required for the sperm maturation in the epididymis (110).…”

Section: Fertilizationmentioning

confidence: 99%

Zinc α2-Glycoprotein: A Multidisciplinary Protein

Hassan

Waheed

Yadav

et al. 2008

Molecular Cancer Research

216

204

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Zinc A2-glycoprotein (ZAG) is a protein of interest because of its ability to play many important functions in the human body, including fertilization and lipid mobilization. After the discovery of this molecule, during the last 5 decades, various studies have been documented on its structure and functions, but still, it is considered as a protein with an unknown function. Its expression is regulated by glucocorticoids. Due to its high sequence homology with lipid-mobilizing factor and high expression in cancer cachexia, it is considered as a novel adipokine. On the other hand, structural organization and fold is similar to MHC class I antigen-presenting molecule; hence, ZAG may have a role in the expression of the immune response. The function of ZAG under physiologic and cancerous conditions remains mysterious but is considered as a tumor biomarker for various carcinomas. There are several unrelated functions that are attributed to ZAG, such as RNase activity, regulation of melanin production, hindering tumor proliferation, and transport of nephritic by-products. This article deals with the discussion of the major aspects of ZAG from its gene structure to function and metabolism. (Mol Cancer Res 2008;6(6):892 -906)

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Identification of chloride intracellular channel proteins in spermatozoa

Cited by 20 publications

References 33 publications

Detection of differential fetal and adult expression of chloride intracellular channel 4 (CLIC4) protein by analysis of a green fluorescent protein knock-in mouse line

Detection of differential fetal and adult expression of chloride intracellular channel 4 (CLIC4) protein by analysis of a green fluorescent protein knock-in mouse line

Chloride channels are involved in sperm motility and are downregulated in spermatozoa from patients with asthenozoospermia

Zinc α2-Glycoprotein: A Multidisciplinary Protein

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