Coxsackie and adenovirus receptor (CAR) is a product of Sertoli and germ cells in rat testes which is localized at the Sertoli–Sertoli and Sertoli–germ cell interface

Wang, Claire Q.F.; Mruk, Dolores D.; Lee, Will M.; Cheng, C. Yan

doi:10.1016/j.yexcr.2007.01.017

Cited by 67 publications

(64 citation statements)

References 56 publications

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“…2A). It is worth noting that previous studies have shown all of these proteins to localize to the Sertoli cell barrier/BTB (Cheng and Mruk, 2012;Cyr et al, 1999;Hellani et al, 2000;Mruk and Cheng, 2004;Su et al, 2010a;Wang et al, 2007;Wong et al, 2004). To validate that ICAM-1 was indeed a constituent protein of the BTB, Sertoli cells (previously cultured for 4 days and having a functional barrier that mimicked the BTB in vivo) were fluorescently immunostained and analyzed by confocal microscopy (Fig.…”

Section: Icam-1 Is An Integral Component Of the Btbmentioning

confidence: 98%

Intercellular adhesion molecule-1 is a regulator of blood–testis barrier function

Xiao

Cheng

Mruk

2012

Journal of Cell Science

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SummaryThe mechanism underlying the movement of preleptotene/leptotene spermatocytes across the blood-testis barrier (BTB) during spermatogenesis is not well understood largely owing to the fact that the BTB, unlike most other blood-tissue barriers, is composed of several co-existing and co-functioning junction types. In the present study, we show that intercellular adhesion molecule-1 [ICAM-1, a Sertoli and germ cell adhesion protein having five immunoglobulin (Ig)-like domains, in addition to transmembrane and cytoplasmic domains] is a regulator of BTB integrity. Initial experiments showed ICAM-1 to co-immunoprecipitate and co-localize with tight junction and basal ectoplasmic specialization proteins such as occludin and N-cadherin, which contribute to BTB function. More importantly, overexpression of ICAM-1 in Sertoli cells in vitro enhanced barrier function when monitored by transepithelial electrical resistance measurements, illustrating that ICAM-1-mediated adhesion can promote BTB integrity. On the other hand, overexpression of a truncated form of ICAM-1 that consisted only of the five Ig-like domains (sICAM-1; this form of ICAM-1 is known to be secreted) elicited an opposite effect when Sertoli cell barrier function was found to be perturbed in vitro; in this case, sICAM-1 overexpression resulted in the downregulation of several BTB constituent proteins, which was probably mediated by Pyk2/p-Pyk2-Y402 and c-Src/pSrc-Y530. These findings were expanded to the in vivo level when BTB function was found to be disrupted following sICAM-1 overexpression. These data illustrate the existence of a unique mechanism in the mammalian testis where ICAM-1 can either positively or negatively regulate BTB function.

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Section: Icam-1 Is An Integral Component Of the Btbmentioning

confidence: 98%

Intercellular adhesion molecule-1 is a regulator of blood–testis barrier function

Xiao

Cheng

Mruk

2012

Journal of Cell Science

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“…In recent years, some of the proteins that are known to be confined to cell-matrix interface at the focal contact (also known as focal adhesion complex, an actin-based cell-matrix anchoring junction type) to facilitate cell movement were found to be components of the apical ES, such as FAK, ILK (integrin-linked kinase) and vinculin. [16][17][18] Additionally, gap junction proteins (e.g., connexin 43,19 ) and tight junction proteins (e.g., JAM-C, junctional adhesion molecule-C also known as JAM-1), 20 coxsackie and adenovirus receptor (CAR), 21,22 are also found to be integrated components of the apical ES, making it a hybrid anchoring junction type. 4,8,15,23 However, a detailed analysis on the components of the integrin-based cell adhesion protein complex which regulate signaling function at the apical at 2 d (Fig.…”

Section: Resultsmentioning

confidence: 99%

The β1-integrin-p-FAK-p130Cas-DOCK180-RhoA-vinculin is a novel regulatory protein complex at the apical ectoplasmic specialization in adult rat testes

et al. 2011

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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%

“…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: 99%

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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Coxsackie and adenovirus receptor (CAR) is a product of Sertoli and germ cells in rat testes which is localized at the Sertoli–Sertoli and Sertoli–germ cell interface

Cited by 67 publications

References 56 publications

Intercellular adhesion molecule-1 is a regulator of blood–testis barrier function

Intercellular adhesion molecule-1 is a regulator of blood–testis barrier function

The β1-integrin-p-FAK-p130Cas-DOCK180-RhoA-vinculin is a novel regulatory protein complex at the apical ectoplasmic specialization in adult rat testes

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

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