C-type natriuretic peptide regulates blood–testis barrier dynamics in adult rat testes

Xia, Weiliang; Mruk, Dolores D.; Cheng, C. Yan

doi:10.1073/pnas.0610100104

Cited by 55 publications

(51 citation statements)

References 54 publications

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“…Upon gonadotrophin stimulation, it is proposed that tight junction proteins would relocate to the cell membrane, providing a mechanism conducive to a rapid reorganisation of functional tight junctions and re-initiation of spermatogenesis. The recycling of membrane-bound versus intracellular TJ proteins has recently been implicated in TJ regulation elsewhere (Sarkar et al 2008, Xia et al 2007. Our data demonstrates that such testicular tight junction protein recycling after gonadotrophin suppression occurs for claudin-11, occludin and Sertoli cell JAM-A, but not claudin-3 or GC JAM-A.…”

Section: Discussionmentioning

confidence: 50%

Regulation of testicular tight junctions by gonadotrophins in the adult Djungarian hamster in vivo

Tarulli¹,

Meachem²,

Schlatt³

et al. 2008

Reproduction

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This study aimed to assess the effect of gonadotrophin suppression and FSH replacement on testicular tight junction dynamics and blood-testis barrier (BTB) organisation in vivo, utilising the seasonal breeding Djungarian hamster. Confocal immunohistology was used to assess the cellular organisation of tight junction proteins and real-time PCR to quantify tight junction mRNA. The effect of tight junction protein organisation on the BTB permeability was also investigated using a biotin-linked tracer. Tight junction protein (claudin-3, junctional adhesion molecule (JAM)-A and occludin) localisation was present but disorganised after gonadotrophin suppression, while mRNA levels (claudin-11, claudin-3 and occludin) were significantly (two-to threefold) increased. By contrast, both protein localisation and mRNA levels for the adaptor protein zona occludens-1 decreased after gonadotrophin suppression. FSH replacement induced a rapid reorganisation of tight junction protein localisation. The functionality of the BTB (as inferred by biotin tracer permeation) was found to be strongly associated with the organisation and localisation of claudin-11. Surprisingly, JAM-A was also recognised on spermatogonia, suggesting an additional novel role for this protein in trans-epithelial migration of germ cells across the BTB. It is concluded that gonadotrophin regulation of tight junction proteins forming the BTB occurs primarily at the level of protein organisation and not gene transcription in this species, and that immunolocalisation of the organised tight junction protein claudin-11 correlates with BTB functionality.

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Section: Discussionmentioning

confidence: 50%

Regulation of testicular tight junctions by gonadotrophins in the adult Djungarian hamster in vivo

Tarulli¹,

Meachem²,

Schlatt³

et al. 2008

Reproduction

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“…Germ cell movement across the seminiferous epithelium during spermatogenesis is associated with extensive junction restructuring [4][5][6][7][8], including dynamic changes in the BTB [2,9,10,[35][36][37]. As shown in Figs.…”

Section: Discussionmentioning

confidence: 99%

“…Recent advances in biochemistry and molecular biology have shifted attention to understanding some of the key events that regulate spermatogenesis, such as opening and closing of the BTB to permit timely passage of primary spermatocytes across the BTB [4][5][6][7][8][35][36][37]. Though the results of recent findings in this area also suggest that the BTB in the seminiferous epithelium must "open" to accommodate migration of primary spermatocytes from the basal compartment to the adluminal compartment, the BTB probably maintains its integrity to protect haploid germ cells against the autoimmune system.…”

Section: Discussionmentioning

confidence: 99%

“…The BTB is a dynamic structure that undergoes cycles of "opening" and "closing" during the epithelial cycle to facilitate germ cell migration, yet its integrity must not be compromised in order to maintain the microenvironment behind it. On the other hand, recent advances concerning the molecular architecture of the BTB have shifted attention to understanding some of the key events that regulate spermatogenesis, such as opening and closing of the BTB to permit timely passage of primary spermatocytes across the it [4][5][6][7][8][35][36][37]. The results of recent research in this area also suggest that the BTB in the seminiferous epithelium must "open" to accommodate migration of primary spermatocytes from the basal compartment to the adluminal compartment.…”

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confidence: 98%

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Continual Maintenance of the Blood-Testis Barrier During Spermatogenesis: The Intermediate Compartment Theory Revisited

Yazama

2008

Journal of Reproduction and Development

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Abstract. Tight junctions occur between the lateral processes of neighboring Sertoli cells that divide the seminiferous epithelium into two compartments: basal and adluminal compartments. These tight junctions constitute the bloodtestis barrier (BTB). The established theory that the BTB must open when spermatocytes translocate from the basal compartment to the adluminal compartment is marked by one contradiction, that is, normal spermatogenesis occurs in the testis because the BTB is expected to constantly seclude the adluminal compartment from the basal compartment in order to protect haploid germ cells from the autoimmune system. Subsequently, another concept was proposed in which two BTBs divide the seminiferous epithelium into three compartments: basal, intermediate and adluminal compartments. It has been suggested that the transition from the basal region to the adluminal region without the BTB open occurs through the agency of a short-lived intermediate compartment embodying some primary spermatocytes. In contrast, the results of recent findings in the molecular architecture of the BTB suggest that the BTB in the seminiferous epithelium must "open". In this paper, I re-examine the BTBs of boar and experimental cryptorchid mouse testes by transmission electron microscope (TEM). TEM analysis showed that an atypical basal compartment existed in the thin seminiferous epithelium of 14-day post-cryptorchid mice testes. In developmental boar testes, ectoplasmic specialization (ES) of the seminiferous epithelium showed dynamic behavior. The intermediate compartment was clearly observed between the basal and adluminal compartments of the mature boar seminiferous epithelium. ESs were observed between Sertoli cells and spermatids at all developmental stages, including early, late and mature. Furthermore, ESs were situated on the apical surface of the seminiferous epithelium. From these results, I propose that the BTB is continually maintained during spermatogenesis and suggest a model of ES circulation in the seminiferous epithelium. Key words: Blood-testis barrier, Cryptorchidism, Ectoplasmic specialization, Testis, Transmission electron microscope (TEM) (J. Reprod. Dev. 54: [299][300][301][302][303][304][305] 2008) ost epithelia have tight junctions between their cells, just below their free surfaces. The seminiferous epithelium is exceptional in having tight junctions nearer the base of the epithelium. These tight junctions occur between the lateral processes of neighboring Sertoli cells that arch over the intervening spermatogonia. They divide the seminiferous epithelium into two compartments: a basal compartment containing spermatogonia and an adluminal compartment containing the later stage of germ cell differentiation. These tight junctions constitute the blood-testis barrier (BTB), and the BTB must open to accommodate elevation of the spermatocyte. This theory was established by Dym and Fawcett in 1970 [1]. The BTB is a dynamic structure that undergoes cycles of "opening" and "closing" during the epitheli...

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“…These findings have helped establish the major functions of CNP as being either paracrine or autocrine in nature, rather than endocrine. In keeping with its limited range of action, CNP expression is normally confined to those tissues and organs in which it exerts a regulatory role, principally the brain and pituitary [82], cardiovascular system [11,23,38,69,98], endochondral bone [102], and the male [100] and female [95,103] reproductive systems. CNP transcript and/or protein have also been identified in a number of tissues and organs where its functional role has yet to be defined [9,76,77,94].…”

Section: C-type Natriuretic Peptidementioning

confidence: 99%

Regulation of C-type natriuretic peptide expression

2011

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a b s t r a c t C-type natriuretic peptide (CNP) is a member of the small family of natriuretic peptides that also includes atrial natriuretic peptide (ANP) and brain, or B-type natriuretic peptide (BNP). Unlike them, it performs its major functions in an autocrine or paracrine manner. Those functions, mediated through binding to the membrane guanylyl cyclase natriuretic peptide receptor B (NPR-B), or by signaling through the non-enzyme natriuretic peptide receptor C (NPR-C), include the regulation of endochondral ossification, reproduction, nervous system development, and the maintenance of cardiovascular health. To date, the regulation of CNP gene expression has not received the attention that has been paid to regulation of the ANP and BNP genes. CNP expression in vitro is regulated by TGF-␤ and receptor tyrosine kinase growth factors in a cell/tissue-specific and sometimes species-specific manner. Expression of CNP in vivo is altered in diseased organs and tissues, including atherosclerotic vessels, and the myocardium of failing hearts. Analysis of the human CNP gene has led to the identification of a number of regulatory sites in the proximal promoter, including a GC-rich region approximately 50 base pairs downstream of the Tata box, and shown to be a binding site for several putative regulatory proteins, including transforming growth factor clone 22 domain 1 (TSC22D1) and a serine threonine kinase (STK16). The purpose of this review is to summarize the current literature on the regulation of CNP expression, emphasizing in particular the putative regulatory elements in the CNP gene and the potential DNA-binding proteins that associate with them.Published by Elsevier Inc.

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C-type natriuretic peptide regulates blood–testis barrier dynamics in adult rat testes

Cited by 55 publications

References 54 publications

Regulation of testicular tight junctions by gonadotrophins in the adult Djungarian hamster in vivo

Regulation of testicular tight junctions by gonadotrophins in the adult Djungarian hamster in vivo

Continual Maintenance of the Blood-Testis Barrier During Spermatogenesis: The Intermediate Compartment Theory Revisited

Regulation of C-type natriuretic peptide expression

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