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      A seamless trespass: germ cell migration across the seminiferous epithelium during spermatogenesis

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      The Journal of Cell Biology
      Rockefeller University Press|1

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          Abstract

          During spermatogenesis, preleptotene spermatocytes traverse the blood–testis barrier (BTB) in the seminiferous epithelium, which is reminiscent of viral pathogens breaking through the tight junctions of host epithelial cells. The process also closely resembles the migration of leukocytes across endothelial tight junctions to reach inflammation sites. Cell adhesion molecules of the immunoglobulin superfamily (e.g., JAM/CAR/nectin) participate in germ cell migration by conferring transient adhesion between Sertoli and germ cells through homophilic and heterophilic interactions. The same molecules also comprise the junctional complexes at the BTB. Interestingly, JAM/CAR/nectin molecules mediate virus uptake and leukocyte transmigration in strikingly similar manners. It is likely that the strategy used by viruses and leukocytes to break through junctional barriers is used by germ cells to open up the inter–Sertoli cell junctions. In associating these diverse cellular events, we highlight the “guiding” role of JAM/CAR/nectin molecules for germ cell passage. Knowledge on viral invasion and leukocyte transmigration has also shed insights into germ cell movement during spermatogenesis.

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          Isolation of a common receptor for Coxsackie B viruses and adenoviruses 2 and 5.

          A complementary DNA clone has been isolated that encodes a coxsackievirus and adenovirus receptor (CAR). When transfected with CAR complementary DNA, nonpermissive hamster cells became susceptible to coxsackie B virus attachment and infection. Furthermore, consistent with previous studies demonstrating that adenovirus infection depends on attachment of a viral fiber to the target cell, CAR-transfected hamster cells bound adenovirus in a fiber-dependent fashion and showed a 100-fold increase in susceptibility to virus-mediated gene transfer. Identification of CAR as a receptor for these two unrelated and structurally distinct viral pathogens is important for understanding viral pathogenesis and has implications for therapeutic gene delivery with adenovirus vectors.
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            Cellular receptor for poliovirus: molecular cloning, nucleotide sequence, and expression of a new member of the immunoglobulin superfamily.

            Restriction of poliovirus replication to a few sites in the infected primate host appears to be controlled by the expression of viral receptors. To learn more about these binding sites and their role in viral tissue tropism, cDNA clones encoding functional poliovirus receptors were isolated. The predicted amino acid sequence reveals that the human poliovirus receptor is an integral membrane protein with the conserved amino acids and domain structure characteristic of members of the immunoglobulin superfamily. Northern hybridization analysis indicates that poliovirus receptor transcripts are expressed in a wide range of human tissues, in contrast to the limited expression of virus binding sites, which suggests that additional factors or modifications of the receptor protein are required to permit poliovirus attachment.
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              Sertoli-Sertoli and Sertoli-germ cell interactions and their significance in germ cell movement in the seminiferous epithelium during spermatogenesis.

              Spermatogenesis is the process by which a single spermatogonium develops into 256 spermatozoa, one of which will fertilize the ovum. Since the 1950s when the stages of the epithelial cycle were first described, reproductive biologists have been in pursuit of one question: How can a spermatogonium traverse the epithelium, while at the same time differentiating into elongate spermatids that remain attached to the Sertoli cell throughout their development? Although it was generally agreed upon that junction restructuring was involved, at that time the types of junctions present in the testis were not even discerned. Today, it is known that tight, anchoring, and gap junctions are found in the testis. The testis also has two unique anchoring junction types, the ectoplasmic specialization and tubulobulbar complex. However, attention has recently shifted on identifying the regulatory molecules that "open" and "close" junctions, because this information will be useful in elucidating the mechanism of germ cell movement. For instance, cytokines have been shown to induce Sertoli cell tight junction disassembly by shutting down the production of tight junction proteins. Other factors such as proteases, protease inhibitors, GTPases, kinases, and phosphatases also come into play. In this review, we focus on this cellular phenomenon, recapping recent developments in the field.
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                Author and article information

                Journal
                J Cell Biol
                The Journal of Cell Biology
                Rockefeller University Press|1
                0021-9525
                1540-8140
                13 August 2007
                : 178
                : 4
                : 549-556
                Affiliations
                Center for Biomedical Research, Population Council, New York, NY 10065
                Author notes

                Correspondence to C. Yan Cheng: Y-Cheng@ 123456popcbr.rockefeller.edu

                Article
                200704061
                10.1083/jcb.200704061
                2064462
                17698604
                cbc03565-6ba6-4cb4-bd2c-ea414415b1c9
                Copyright © 2007, The Rockefeller University Press
                History
                : 12 April 2007
                : 12 July 2007
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                Cell biology
                Cell biology

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