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      Folliculostellate Cells Are Required for Laminin Release from Gonadotrophs
      in Rat Anterior Pituitary

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          Abstract

          The anterior pituitary gland is organized tissue comprising hormone-producing cells and folliculostellate (FS) cells. FS cells interconnect to form a meshwork, and their cytoplasmic processes are anchored by a basement membrane containing laminin. Recently, we developed a three-dimensional (3D) cell culture that reproduces this FS cell architecture. In this study of the novel function of FS cells, we used transgenic rats that express green fluorescent protein in FS cells for the 3D culture. Anterior pituitary cells were cultured with different proportions of FS cells (0%, 5%, 10%, and 20%). Anterior pituitary cells containing 5–20% FS cells formed round/oval cell aggregates, whereas amorphous cell aggregates were formed in the absence of FS cells. Interestingly, immunohistochemistry showed laminin-immunopositive cells instead of extracellular laminin deposition in FS cell-deficient cell aggregates. Double-immunostaining revealed that these laminin-immunopositive cells were gonadotrophs. Laminin mRNA expression did not differ in relation to the presence or absence of FS cells. When anterior pituitary cells with no FS cells were cultured with FS cell-conditioned medium, the proportion of laminin-immunopositive cells was lower than in control. These results suggest that a humoral factor from FS cells is required for laminin release from gonadotrophs.

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          Most cited references20

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          Laminins.

          Laminins are cell adhesion molecules that comprise a family of glycoproteins found predominantly in basement membranes, which are the thin sheets of extracellular matrix that underlie epithelial and endothelial cells and surround muscle cells, Schwann cells, and fat cells. Many laminins self-assemble to form networks that remain in close association with cells through interactions with cell surface receptors. Laminins are vital for many physiological functions. They are essential for early embryonic development and organogenesis and have crucial functions in several tissues including muscle, nerve, skin, kidney, lung, and the vasculature. A great wealth of data on laminins is available, and an in-depth description is not attempted here. In this review, I will instead provide a snapshot of laminin structure, tissue distribution, and interactions with other matrix molecules and receptors and briefly describe laminin mutations in mice and humans. Several illuminating and timely reviews are cited that can be consulted for references to original articles and more detailed information concerning laminins.
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            Laminin--a glycoprotein from basement membranes.

            We have isolated a large noncollagenous glycoprotein, laminin, from a mouse tumor that produces basement membrane. The protein consists of at least two polypeptide chains (Mr = 220,000 and Mr = 440,000) joined to each other by disulfide bonds. Laminin and type IV collagen are major constituents of the tumor. Laminin is distinctly different from fibronectin, another component of basement membranes, in amino acid composition and immunological reactivity. Pepsin digestion of laminin releases a large, cystine-rich fragment which retains most of the antigenicity of the original protein. Immunological studies using purified antibody against laminin show that it is produced by a variety of cultured cells. In addition, these antibodies react with the basement membranes of normal tissues, suggesting that this protein or an immunologically related protein is a constituent of the basement membranes of these tissues.
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              Bridging structure with function: structural, regulatory, and developmental role of laminins.

              The basement membrane is a highly intricate and organized portion of the extracellular matrix that interfaces with a variety of cell types including epithelial, endothelial, muscle, nerve, and fat cells. The laminin family of glycoproteins is a major constituent of the basement membrane. The 16 known laminin isoforms are formed from combinations of alpha, beta, and gamma chains, with each chain containing specific domains capable of interacting with cellular receptors such as integrins and other extracellular ligands. In addition to its role in the assembly and architectural integrity of the basement membrane, laminins interact with cells to influence proliferation, differentiation, adhesion, and migration, processes activated in normal and pathologic states. In vitro these functions are regulated by the post-translational modifications of the individual laminin chains. In vivo laminin knockout mouse studies have been particularly instructive in defining the function of specific laminins in mammalian development and have also highlighted its role as a key component of the basement membrane. In this review, we will define how laminin structure complements function and explore its role in both normal and pathologic processes.
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                Author and article information

                Journal
                Acta Histochem Cytochem
                Acta Histochem Cytochem
                AHC
                Acta Histochemica et Cytochemica
                JAPAN SOCIETY OF HISTOCHEMISTRY AND CYTOCHEMISTRY
                0044-5991
                1347-5800
                2014
                23 October 2014
                : 47
                : 5
                : 239-245
                Affiliations
                [1 ]Division of Histology and Cell Biology, Department of Anatomy, Jichi Medical University School of Medicine , Tochigi, Japan
                [2 ]Laboratory of Natural History, Jichi Medical University School of Medicine , Tochigi, Japan
                [3 ]Laboratory of Anatomy and Cell Biology, Department of Health Sciences, Kyorin University , Tokyo, Japan
                Author notes
                Correspondence to: Takashi Yashiro, M.D., Ph.D., Department of Anatomy, Jichi Medical University School of Medicine, 3311–1 Yakushiji, Shimotsuke, Tochigi 329–0498, Japan. E-mail: tyashiro@ 123456jichi.ac.jp
                Article
                JST.JSTAGE/ahc/14036 14036
                10.1267/ahc.14036
                4387245
                ba4f9e8c-16eb-4921-beea-b17fb707a73c
                2014 The Japan Society of Histochemistry and Cytochemistry

                This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                : 18 June 2014
                : 26 August 2014
                Categories
                Regular Article

                Clinical chemistry
                laminin,anterior pituitary,folliculostellate cell,gonadotroph,3d cell culture
                Clinical chemistry
                laminin, anterior pituitary, folliculostellate cell, gonadotroph, 3d cell culture

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