47
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: not found

      Folliculostellate cells in pituitary pars distalis of male viscacha: immunohistochemical, morphometric and ultrastructural study

      review-article

      Read this article at

      ScienceOpenPublisherPMC
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          Folliculostellate cells (FSC) have been reported in pituitary of several mammalian species. FSC morphology and secreted substances have been instrumental to the understanding of their function. The purpose of this work was to perform an immunohistochemical, morphometric and ultrastructural study of the pituitary pars distalis FSC in adult male viscacha and to analyze their relation with hormone secreting cells. Immunohistochemistry and image analysis were carried out in different sectors of the gland, from the middle (sector 1) to the glandular periphery (sector 5). Transmission electron microscopy with lanthanum as electrodense tracer was used. FSC formed follicles with PAS-positive colloid inside. They expressed S-100 protein mainly in both nucleus and cytoplasm. FSC were stellate-like in shape and exhibited short cytoplasmic processes that contacted with blood vessels and endocrine cells. In addition, some follicular colloids were immunostained with anti-S-100 protein. A few FSC were immunostained with anti-glial fibrillary acidic protein (GFAP) and anti-vimentin. The morphometric parameters analyzed (percentages of S-100-positive total, cellular and colloidal areas) increased from sector 1 to sector 3 and then decreased to sector 5. Hormone secreting cells, mainly lactotrophs, gonadotrophs and corticotrophs were associated with FSC and follicles. The ultrastructural study demonstrated that FSC developed junctional complexes and desmosomes between their lateral membranes. Lanthanum freely penetrated the spaces between granulated cells and FSC, but did not penetrate into the follicular lumen. In conclusion: 1) the differential expression of S-100 protein, GFAP and vimentin may indicate different physiological stages of FSC; 2) the expression of these proteins suggests a neuroectodermic origin of these cells; 3) FSC spatial distribution, association with endocrine cells, and the generation of an intercellular communication network suggest that FSC are involved in the pituitary pars distalis paracrine regulation of the viscacha.

          Related collections

          Most cited references53

          • Record: found
          • Abstract: found
          • Article: not found

          Calcium-dependent and -independent interactions of the S100 protein family.

          The S100 proteins comprise at least 25 members, forming the largest group of EF-hand signalling proteins in humans. Although the proteins are expressed in many tissues, each S100 protein has generally been shown to have a preference for expression in one particular tissue or cell type. Three-dimensional structures of several S100 family members have shown that the proteins assume a dimeric structure consisting of two EF-hand motifs per monomer. Calcium binding to these S100 proteins, with the exception of S100A10, results in an approx. 40 degrees alteration in the position of helix III, exposing a broad hydrophobic surface that enables the S100 proteins to interact with a variety of target proteins. More than 90 potential target proteins have been documented for the S100 proteins, including the cytoskeletal proteins tubulin, glial fibrillary acidic protein and F-actin, which have been identified mostly from in vitro experiments. In the last 5 years, efforts have concentrated on quantifying the protein interactions of the S100 proteins, identifying in vivo protein partners and understanding the molecular specificity for target protein interactions. Furthermore, the S100 proteins are the only EF-hand proteins that are known to form both homo- and hetero-dimers, and efforts are underway to determine the stabilities of these complexes and structural rationales for their formation and potential differences in their biological roles. This review highlights both the calcium-dependent and -independent interactions of the S100 proteins, with a focus on the structures of the complexes, differences and similarities in the strengths of the interactions, and preferences for homo- compared with hetero-dimeric S100 protein assembly.
            Bookmark
            • Record: found
            • Abstract: not found
            • Article: not found

            HEXAGONAL ARRAY OF SUBUNITS IN INTERCELLULAR JUNCTIONS OF THE MOUSE HEART AND LIVER

              Bookmark
              • Record: found
              • Abstract: not found
              • Article: not found

              A MODIFIED PROCEDURE FOR LEAD STAINING OF THIN SECTIONS

                Bookmark

                Author and article information

                Journal
                Eur J Histochem
                EJH
                EJH
                European Journal of Histochemistry : EJH
                PAGEPress Publications (Pavia, Italy )
                1121-760X
                2038-8306
                20 March 2010
                20 March 2010
                : 54
                : 1
                : e1
                Affiliations
                Cátedra de Histología y Embriología, Facultad de Química, Bioquímica y Farmacia, Universidad Nacional de San Luis, Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), San Luis, Argentina
                Author notes
                Correspondence: Fabian Mohamed, Cátedra de Histología y Embriología, Facultad de Química, Bioquímica y Farmacia, Universidad Nacional de San Luis, Avenida Ejército de los Andes 950 - 2° piso. CP 5700, San Luis, Argentina. E-mail: fhmo@ 123456unsl.edu.ar
                Article
                ejh.2010.e1
                10.4081/ejh.2010.e1
                3167288
                20353904
                5009bd8a-d650-4b86-9874-d1aed1446907
                ©Copyright M. Acosta et al., 2010

                This work is licensed under a Creative Commons Attribution 3.0 License (by-nc 3.0).

                Licensee PAGEPress, Italy

                History
                : 28 July 2009
                : 24 November 2009
                Categories
                Original Paper

                Clinical chemistry
                pituitary,distribution,lagostomus,folliculostellate cells,ultrastructure.,immunohistochemistry

                Comments

                Comment on this article