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Article ; Online: Emergent roles for intercellular adhesion molecule-1 in the restructuring of the blood-testis barrier during spermatogenesis in the mammal.

Mruk, Dolores D

2016 Volume 31, Issue 2, Page(s) 159–166

Abstract: Mammalian spermatogenesis is comprised of a series of molecular, cellular, and morphological events that underscore the movement of developing germ cells across the blood-testis barrier. These events involve the restructuring of tight junctions, basal ... ...

Abstract	Mammalian spermatogenesis is comprised of a series of molecular, cellular, and morphological events that underscore the movement of developing germ cells across the blood-testis barrier. These events involve the restructuring of tight junctions, basal ectoplasmic specializations, gap junctions, and desmosomes, which constitute blood-testis barrier function. Previous studies show that preleptotene/leptotene spermatocytes traverse the blood-testis barrier while transiently trapped within an intermediate compartment, which sequesters primary spermatocytes away from basal and adluminal compartments of the seminiferous epithelium. Preleptotene/leptotene spermatocytes enter the adluminal compartment when stable junctions ahead of spermatocytes disassemble, while new junctions assemble behind them. While there is enormous restructuring of the seminiferous epithelium, the mechanism of germ cell movement is incompletely understood. In this perspective, the significance of intercellular adhesion molecule-1 in the restructuring of the blood-testis barrier during spermatogenesis in the mammal is discussed.
MeSH term(s)	Animals ; Blood-Testis Barrier/metabolism ; Cell Adhesion ; Cell Movement ; Germ Cells/cytology ; Intercellular Adhesion Molecule-1/metabolism ; Male ; Rats ; Seminiferous Epithelium/metabolism ; Sertoli Cells/cytology ; Spermatocytes/cytology ; Spermatogenesis ; Testis/metabolism
Chemical Substances	ICAM1 protein, rat ; Icam1 protein, mouse ; Intercellular Adhesion Molecule-1 (126547-89-5)
Language	English
Publishing date	2016-02
Publishing country	Spain
Document type	Journal Article ; Review
ZDB-ID	83911-5
ISSN	1699-5848 ; 0213-3911
ISSN (online)	1699-5848
ISSN	0213-3911
DOI	10.14670/HH-11-672
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Article: Spermiation: Insights from Studies on the Adjudin Model.

Chen, Haiqi / Jiang, Yu / Mruk, Dolores D / Cheng, C Yan

Advances in experimental medicine and biology

2021 Volume 1288, Page(s) 241–254

Abstract: Spermatogenesis is comprised of a series of cellular events that lead to the generation of haploid sperm. These events include self-renewal of spermatogonial stem cells (SSC), proliferation of spermatogonia by mitosis, differentiation of spermatogonia ... ...

Abstract	Spermatogenesis is comprised of a series of cellular events that lead to the generation of haploid sperm. These events include self-renewal of spermatogonial stem cells (SSC), proliferation of spermatogonia by mitosis, differentiation of spermatogonia and spermatocytes, generation of haploid spermatids via meiosis I/II, and spermiogenesis. Spermiogenesis consists of a series of morphological events in which spermatids are being transported across the apical compartment of the seminiferous epithelium while maturing into spermatozoa, which include condensation of the genetic materials, biogenesis of acrosome, packaging of the mitocondria into the mid-piece, and elongation of the sperm tail. However, the biology of spermiation remains poorly understood. In this review, we provide in-depth analysis based on the use of bioinformatics tools and an animal model that mimics spermiation through treatment of adult rats with adjudin, a non-hormonal male contraceptive known to induce extensive germ cell exfoliation across the seminiferous epithelium, but nost notably elongating/elongated spermatids. These analyses have shed insightful information regaridng the biology of spermiation.
MeSH term(s)	Animals ; Hydrazines ; Indazoles ; Male ; Rats ; Seminiferous Epithelium ; Spermatids ; Spermatogenesis ; Spermatogonia
Chemical Substances	1-(2,4-dichlorobenzyl)indazole-3-carbohydrazide ; Hydrazines ; Indazoles
Language	English
Publishing date	2021-08-28
Publishing country	United States
Document type	Journal Article ; Review
ISSN	2214-8019 ; 0065-2598
ISSN (online)	2214-8019
ISSN	0065-2598
DOI	10.1007/978-3-030-77779-1_12
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Unraveling the Regulation of Cancer/Testis Antigens in Tumorigenesis Through an Analysis of Normal Germ Cell Development in Rodents.

Chen, Haiqi / Jiang, Yu / Mruk, Dolores D / Cheng, C Yan

Advances in experimental medicine and biology

2021 Volume 1288, Page(s) 69–93

Abstract: Cancer/testis (CT) antigens are proteins aberrantly overexpressed in various tumorigenic cells, but they can also be normally expressed in the mammalian germline. Most CT antigens are highly immunogenic and known to be involved in cancer cell ... ...

Abstract	Cancer/testis (CT) antigens are proteins aberrantly overexpressed in various tumorigenic cells, but they can also be normally expressed in the mammalian germline. Most CT antigens are highly immunogenic and known to be involved in cancer cell proliferation and tumor metastasis. A recent genome-wide analysis systematically identified CT antigen expression in 19 cancer types, significantly expanding the repertoire of CT antigens by 5-fold, from over 200 to approximately 1000. However, their function and regulation in tumorigenesis remain poorly understood. The shared functional characteristics between germ cells and cancer cells, if methodically defined, offer a unique gateway to understanding the regulation of CT antigens in cancers by studying gametogenesis. Nonetheless, such studies also provide insightful information on the role of CT antigens in spermatogenesis. Herein, we analyzed publicly available next generation sequencing datasets generated from normal adult testes in rodents, primordial germ cells and cancer samples across a series of published studies and databases. Based on these analyses, we report that a subset of CT antigens belonged to the core fitness gene family. Furthermore, super-enhancers both in normal testes and various cancers controlled specific CT antigens. We found that DNA methylation of CT antigens, such as TEX101 and TAF7L, was inversely correlated with their expression in both normal primordial germ cells and various cancers, which was mediated at least partly by DNA methyltransferase1 (DNMT1). By analyzing data from a testis knockout model, we showed that TAF7L could further influence the expression of additional CT antigens, which also held true in tumors. These findings not only confirmed the previous notion that CT antigens regulate cancer dynamics, but also showed that understanding the regulation of CT antigens during gametogenesis can offer new insights for cancer research.
MeSH term(s)	Animals ; Antigens, Neoplasm/genetics ; Carcinogenesis/genetics ; Germ Cells ; Male ; Rodentia ; Testis
Chemical Substances	Antigens, Neoplasm
Language	English
Publishing date	2021-08-28
Publishing country	United States
Document type	Journal Article
ISSN	2214-8019 ; 0065-2598
ISSN (online)	2214-8019
ISSN	0065-2598
DOI	10.1007/978-3-030-77779-1_4
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Article: Why do we need male contraceptives?

Cheng, C Yan / Mruk, Dolores D

Spermatogenesis

2013 Volume 3, Issue 3, Page(s) e25888

Abstract: A recent article published in Bloomberg ... ...

Abstract	A recent article published in Bloomberg Businessweek
Language	English
Publishing date	2013-07-25
Publishing country	United States
Document type	Journal Article
ZDB-ID	2629571-4
ISSN	2156-5562 ; 2156-5554
ISSN (online)	2156-5562
ISSN	2156-5554
DOI	10.4161/spmg.25888
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Article ; Online: The Src non-receptor tyrosine kinase paradigm: New insights into mammalian Sertoli cell biology.

Chojnacka, Katarzyna / Mruk, Dolores D

Molecular and cellular endocrinology

2015 Volume 415, Page(s) 133–142

Abstract: Src kinases are non-receptor tyrosine kinases that phosphorylate diverse substrates, which control processes such as cell proliferation, differentiation and survival; cell adhesion; and cell motility. c-Src, the prototypical member of this protein family, ...

Abstract	Src kinases are non-receptor tyrosine kinases that phosphorylate diverse substrates, which control processes such as cell proliferation, differentiation and survival; cell adhesion; and cell motility. c-Src, the prototypical member of this protein family, is widely expressed by several organs that include the testis. In the seminiferous epithelium of the adult rat testis, c-Src is highest at the tubule lumen during the release of mature spermatids. Other studies show that testosterone regulates spermatid adhesion to Sertoli cells via c-Src, indicating Src phosphorylates key substrates that prompt the disassembly of Sertoli cell-spermatid junctions. A more recent in vitro study reveals that c-Src participates in the internalization of proteins that constitute the blood-testis barrier, which is present between Sertoli cells, suggesting a similar mechanism of junction disassembly is at play during spermiation. In this review, we discuss recent findings on c-Src, with an emphasis on its role in spermatogenesis in the mammalian testis.
MeSH term(s)	Animals ; Blood-Testis Barrier/metabolism ; Cell Adhesion ; Humans ; Male ; Phosphorylation ; Proto-Oncogene Proteins pp60(c-src)/metabolism ; Seminiferous Epithelium/cytology ; Seminiferous Epithelium/metabolism ; Sertoli Cells/cytology ; Sertoli Cells/metabolism ; Signal Transduction ; Spermatids/cytology ; Spermatids/metabolism ; Spermatogenesis ; Testosterone/metabolism
Chemical Substances	Testosterone (3XMK78S47O) ; Proto-Oncogene Proteins pp60(c-src) (EC 2.7.10.2)
Language	English
Publishing date	2015-11-05
Publishing country	Ireland
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	187438-x
ISSN	1872-8057 ; 0303-7207
ISSN (online)	1872-8057
ISSN	0303-7207
DOI	10.1016/j.mce.2015.08.012
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Article ; Online: The Mammalian Blood-Testis Barrier: Its Biology and Regulation.

Mruk, Dolores D / Cheng, C Yan

Endocrine reviews

2015 Volume 36, Issue 5, Page(s) 564–591

Abstract: Spermatogenesis is the cellular process by which spermatogonia develop into mature spermatids within seminiferous tubules, the functional unit of the mammalian testis, under the structural and nutritional support of Sertoli cells and the precise ... ...

Abstract	Spermatogenesis is the cellular process by which spermatogonia develop into mature spermatids within seminiferous tubules, the functional unit of the mammalian testis, under the structural and nutritional support of Sertoli cells and the precise regulation of endocrine factors. As germ cells develop, they traverse the seminiferous epithelium, a process that involves restructuring of Sertoli-germ cell junctions, as well as Sertoli-Sertoli cell junctions at the blood-testis barrier. The blood-testis barrier, one of the tightest tissue barriers in the mammalian body, divides the seminiferous epithelium into 2 compartments, basal and adluminal. The blood-testis barrier is different from most other tissue barriers in that it is not only comprised of tight junctions. Instead, tight junctions coexist and cofunction with ectoplasmic specializations, desmosomes, and gap junctions to create a unique microenvironment for the completion of meiosis and the subsequent development of spermatids into spermatozoa via spermiogenesis. Studies from the past decade or so have identified the key structural, scaffolding, and signaling proteins of the blood-testis barrier. More recent studies have defined the regulatory mechanisms that underlie blood-testis barrier function. We review here the biology and regulation of the mammalian blood-testis barrier and highlight research areas that should be expanded in future studies.
MeSH term(s)	Animals ; Blood-Testis Barrier/metabolism ; Blood-Testis Barrier/ultrastructure ; Contraceptive Agents, Male ; Humans ; Male ; Spermatogenesis ; Tight Junction Proteins/metabolism
Chemical Substances	Contraceptive Agents, Male ; Tight Junction Proteins
Language	English
Publishing date	2015-09-10
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	603096-8
ISSN	1945-7189 ; 0163-769X
ISSN (online)	1945-7189
ISSN	0163-769X
DOI	10.1210/er.2014-1101
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Article: Lonidamine-ethyl ester-mediated remodelling of the Sertoli cell cytoskeleton induces phosphorylation of plakoglobin and promotes its interaction with α-catenin at the blood-testis barrier.

Mruk, Dolores D / Bonanomi, Michele / Silvestrini, Bruno

Reproduction, fertility, and development

2017 Volume 29, Issue 5, Page(s) 998–1011

Abstract: Several compounds affect male fertility by disrupting the adhesion of germ cells to Sertoli cells, which results in the release of undeveloped germ cells into the seminiferous tubule lumen that are incapable of fertilising the ovum. Indazole carboxylic ... ...

Abstract	Several compounds affect male fertility by disrupting the adhesion of germ cells to Sertoli cells, which results in the release of undeveloped germ cells into the seminiferous tubule lumen that are incapable of fertilising the ovum. Indazole carboxylic acids are one class of compounds exhibiting such effects and they have been investigated as non-hormonal contraceptives for potential human use. The aims of this study were to investigate the effects of lonidamine-ethyl ester, an indazole carboxylic acid, on spermatogenesis and cell junctions, in particular, desmosomes. We found two doses of lonidamine-ethyl ester at 50mg kg
Language	English
Publishing date	2017-04
Publishing country	Australia
Document type	Journal Article
ZDB-ID	1019913-5
ISSN	1448-5990 ; 1031-3613
ISSN (online)	1448-5990
ISSN	1031-3613
DOI	10.1071/RD15378
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Article ; Online: Sphingomyelin synthases and testicular function.

Lee, Nikki Py / Wong, Elissa Wp / Mruk, Dolores D / Cheng, C Yan

Expert review of endocrinology & metabolism

2018 Volume 3, Issue 5, Page(s) 593–601

Abstract: Sphingomyelin synthase (SMS) is a cellular enzyme that catalyzes de novo synthesis of sphingomyelin (SM), which is a vital lipid component of cell membranes. Both members of the SMS family, SMS1 and SMS2, are found in mammalian testes and they are ... ...

Abstract	Sphingomyelin synthase (SMS) is a cellular enzyme that catalyzes de novo synthesis of sphingomyelin (SM), which is a vital lipid component of cell membranes. Both members of the SMS family, SMS1 and SMS2, are found in mammalian testes and they are located in distinctive subcellular compartments, with SMS1 in the Golgi apparatus and SMS2 in the plasma membrane. At present, the precise function of SMS in the testis remains unknown. Recent studies have demonstrated an unique association of SMS2 with spermatids, particularly near developing acrosomes and the junction restructuring site at the apical ectoplasmic specialization (a testis-specific atypical adherens junction type) and Leydig cells in the rat testis. These data illustrate the possible involvement of SMS2 in spermiogenesis and, perhaps, steroidogenesis in male reproductive function. This review summarizes the latest findings on SMS in the field, particularly its role in testicular function.
Language	English
Publishing date	2018-10-05
Publishing country	England
Document type	Journal Article
ISSN	1744-8417
ISSN (online)	1744-8417
DOI	10.1586/17446651.3.5.593
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Article: Lonidamine-ethyl ester-mediated remodelling of the Sertoli cell cytoskeleton induces phosphorylation of plakoglobin and promotes its interaction with Î±-catenin at the bloodâtestis barrier

Mruk, Dolores D / Bruno Silvestrini / Michele Bonanomi

Reproduction, fertility, and development. 2017, v. 29, no. 5

2017

Abstract	Several compounds affect male fertility by disrupting the adhesion of germ cells to Sertoli cells, which results in the release of undeveloped germ cells into the seminiferous tubule lumen that are incapable of fertilising the ovum. Indazole carboxylic acids are one class of compounds exhibiting such effects and they have been investigated as non-hormonal contraceptives for potential human use. The aims of this study were to investigate the effects of lonidamine-ethyl ester, an indazole carboxylic acid, on spermatogenesis and cell junctions, in particular, desmosomes. We found two doses of lonidamine-ethyl ester at 50mg kg-1 to disrupt Sertoliâgerm cell adhesion. By light and fluorescent microscopy, pronounced changes were observed in the distribution of actin microfilaments and intermediate filaments, as well as in the localisation of plakoglobin, a protein with structural and signalling roles at the desmosome and adherens junction at the bloodâtestis barrier. Furthermore, immunoblotting and immunoprecipitation experiments using testis lysates revealed a significant upregulation (P<0.01) of plakoglobin and Tyr-phosphorylated plakoglobin. Co-immunoprecipitation experiments showed an increase in the interaction between plakoglobin and fyn proto-oncogene, an Src family non-receptor tyrosine kinase, after treatment, as well as an increase in the interaction between plakoglobin and Î±-catenin. Taken collectively, these data indicate that a disruption of Sertoli cell and spermatocyteâspermatid adhesion in the seminiferous epithelium by lonidamine-ethyl ester results in the phosphorylation of plakoglobin, thereby promoting its interaction with Î±-catenin at the bloodâtestis barrier.
Keywords	adhesion ; carboxylic acids ; cell adhesion ; contraceptives ; desmosomes ; fluorescence microscopy ; gamma catenin ; humans ; immunoblotting ; intermediate filaments ; male fertility ; microfilaments ; ova ; phosphorylation ; precipitin tests ; proto-oncogenes ; seminiferous epithelium ; Sertoli cells ; spermatogenesis ; tyrosine
Language	English
Size	p. 998-1011.
Publishing place	CSIRO Publishing
Document type	Article
ZDB-ID	1019913-5
ISSN	1448-5990 ; 1031-3613
ISSN (online)	1448-5990
ISSN	1031-3613
DOI	10.1071/RD15378
Database	NAL-Catalogue (AGRICOLA)

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Z 5258: Show issues

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Article: Rat and mouse testicular testin is different from the human tumor suppressor gene TESTIN (Tes): Authors' response to the letter of Dr. S. Kapoor.

Mruk, Dolores D / Cheng, C Yan

Spermatogenesis

2012 Volume 2, Issue 4, Page(s) 305

Language	English
Publishing date	2012-11-28
Publishing country	United States
Document type	Journal Article
ZDB-ID	2629571-4
ISSN	2156-5562 ; 2156-5554
ISSN (online)	2156-5562
ISSN	2156-5554
DOI	10.4161/spmg.22790
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