Collagen Synthesis by Rat Anterior Pituitary Cells In Vivo and In Vitro.

Kaidzu, Sachiko; Noda, Takahiro; Tane, Nobuhiro; Yashiro, Takashi

doi:10.1267/ahc.33.81

Cited by 11 publications

(15 citation statements)

References 25 publications

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“…Our group has identified various collagen types (type I, III, IV, and VI collagens) in rat anterior pituitary gland (Kaidzu et al 2000). These collagens are distributed around endocrine cells and capillaries and support tissue structure.…”

Section: Introductionmentioning

confidence: 99%

Folliculostellate cell interacts with pericyte via TGFβ2 in rat anterior pituitary

Tsukada¹,

Azuma²,

Horiguchi³

et al. 2016

Journal of Endocrinology

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The anterior pituitary gland comprises five types of endocrine cells plus non-endocrine cells including folliculostellate cells, endothelial cells, and capillary mural cells (pericytes). In addition to being controlled by the hypothalamic-pituitary-target organ axis, the functions of these cells are likely regulated by local cell and extracellular matrix (ECM) interactions. However, these complex interactions are not fully understood. We investigated folliculostellate cell-mediated cell-to-cell interaction. Using S100β-GFP transgenic rats, which express GFP in folliculostellate cells, we designed a three-dimensional cell culture to examine the effects of folliculostellate cells. Interestingly, removal of folliculostellate cells reduced collagen synthesis (Col1a1 and Col3a1). Because pericytes are important collagen-producing cells in the gland, we stained for desmin (a pericyte marker). Removal of folliculostellate cells resulted in fewer desmin-positive pericytes and less desmin mRNA. We then attempted to identify the factor mediating folliculostellate cell-pericyte interaction. RT-PCR and in situ hybridization revealed that the important profibrotic factor transforming growth factor beta-2 (TGFβ2) was specifically expressed in folliculostellate cells and that TGFβ receptor II was expressed in pericytes, endothelial cells, and parenchymal cells. Immunocytochemistry showed that TGFβ2 induced SMAD2 nuclear translocation in pericytes. TGFβ2 increased collagen synthesis in a dose-dependent manner. This action was completely blocked by TGFβ receptor I inhibitor (SB431542). Diminished collagen synthesis in folliculostellate cell-deficient cell aggregates was partially recovered by TGFβ2. TGFβ2-mediated folliculostellate cell-pericyte interaction appears to be essential for collagen synthesis in rat anterior pituitary. This finding sheds new light on local cell-ECM interactions in the gland. 159-170 229:2 FS cell interacts with pericyte via TGFβ2t tsukada and others

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Section: Introductionmentioning

confidence: 99%

Folliculostellate cell interacts with pericyte via TGFβ2 in rat anterior pituitary

Tsukada¹,

Azuma²,

Horiguchi³

et al. 2016

Journal of Endocrinology

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“…These cell aggregations form cell cords or clusters surrounded by different types of extracellular matrices (ECM) that provide the mechanical integrity, rigidity, and elasticity that are essential for these cells to perform their respective roles (Soji & Herbert 1989, Kaidzu et al 2000, Paez-Pereda et al 2005. FS cells have a star-like appearance and form a pseudolumen at the central portion of FS cell clusters (Soji & Herbert 1989).…”

Section: Introductionmentioning

confidence: 99%

Caveolin 3-mediated integrin β1 signaling is required for the proliferation of folliculostellate cells in rat anterior pituitary gland under the influence of extracellular matrix

Horiguchi¹,

Fujiwara²,

Ilmiawati³

et al. 2011

Journal of Endocrinology

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Folliculostellate (FS) cells in the anterior pituitary gland are believed to have multifunctional properties. Using transgenic rats that express green fluorescent protein (GFP) specifically in FS cells in the anterior pituitary gland (S100b-GFP rats), we recently revealed that FS cells in primary culture exhibited marked proliferation in the presence of laminin, an extracellular matrix (ECM) component of the basement membrane. In a process referred to as matricrine action, FS cells receive ECM as a signal through their receptors, which results in morphological and functional changes. In this study, we investigated matricrine signaling in FS cells and observed that the proliferation of FS cells is mediated by integrin b1, which is involved in various signaling pathways for cell migration and proliferation in response to ECM. Then, we analyzed downstream events of the integrin b1 signaling pathway in the proliferation of FS cells and identified caveolin 3 as a potential candidate molecule. Caveolin 3 is a membrane protein that binds cholesterol and a number of signaling molecules that interact with integrin b1. Using specific small interfering RNA of caveolin 3, the proliferation of FS cells was inhibited. Furthermore, caveolin 3 drove activation of the mitogen-activated protein kinase (MAPK) signaling cascades, which resulted in upregulation of cyclin D1 in FS cells. These findings suggest that matricrine signaling in the proliferation of FS cells was transduced by a caveolin 3-mediated integrin b1 signaling pathway and subsequent activation of the MAPK pathway.

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“…6). The production of various ECM proteins, such as laminin, fibronectin, and collagen, by hormone-producing cells in the anterior pituitary has been reported [9,23]. The observations depicted in Figure 6 may be due to the process described as follows: as the anterior pituitary cells form clusters and the ECM is gradually discharged from the cells, integrin including α5 subunit is synthesized, bound to the ECM, and eventually stabilized in the cell membrane.…”

Section: Discussionmentioning

confidence: 92%

“…Observation of the clusters by electron microscope indicated the presence of cell junctions only among folliculo-stellate cells, but not among hormone-producing cells; this was the same feature seen in tissue observation. In addition, it has been reported that the extracellular matrix was produced and secreted by the hormone-producing cells in primary culture [9].…”

Section: Introductionmentioning

confidence: 99%

An In Vivo and In Vitro Immunohistochemical Study of Integrin Alpha Subunit Localization in the Rat Anterior Pituitary

Kikuchi

Sunaga

Yatabe

et al. 2005

Acta Histochem. Cytochem

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Different types of integrin alpha subunit were investigated immunohistochemically to determine the relationship between the cell adhesion molecule and the local morphology of the rat anterior pituitary using anterior pituitary tissues and primary cultured cells. Alpha 3 subunit was shown to be the main integrin subunit in the anterior pituitary. In vitro, immunoreactions of 3 subunit appeared mainly surrounding cell clusters. The distribution roughly overlapped with immunoreaction of laminin, while it was also observed where expression of laminin was negative. When dispersed cells were primary cultured for 2, 3 or 5 days, immunoreaction of 3 subunit was clearly detected in the vicinity of cell membrane throughout the period; while that of 5 subunit was not observed on day 2, it was observed as dots in cytoplasm on day 3 and more distinctly as lines in the vicinity of the cell membrane on day 5. Alpha 5 subunit was not detectable in vivo. These results indicate the possibility that integrin 3 subunit not only binds the cells to the basement membrane but also to other extracellular matrix or directly to adjacent cells in the anterior pituitary. In addition, integrin 5 subunit may supplement the function of 3 subunit under certain conditions.

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Collagen Synthesis by Rat Anterior Pituitary Cells In Vivo and In Vitro.

Cited by 11 publications

References 25 publications

Folliculostellate cell interacts with pericyte via TGFβ2 in rat anterior pituitary

Folliculostellate cell interacts with pericyte via TGFβ2 in rat anterior pituitary

Caveolin 3-mediated integrin β1 signaling is required for the proliferation of folliculostellate cells in rat anterior pituitary gland under the influence of extracellular matrix

An In Vivo and In Vitro Immunohistochemical Study of Integrin Alpha Subunit Localization in the Rat Anterior Pituitary

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