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

Horiguchi, Kotaro; Fujiwara, Ken; Ilmiawati, Cimi; Kikuchi, Motoshi; Tsukada, Takehiro; Kouki, Tom; Yashiro, Takashi

doi:10.1530/joe-11-0103

Cited by 21 publications

(13 citation statements)

References 30 publications

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“…3A and B). Cells were treated with 100 mM MMP-9 synthetic inhibitor or an equal volume of vehicle (DMSO; control group) from 0 to 72 h. In the control group, the behavior of FS cells was similar to that reported previously (Horiguchi et al 2010(Horiguchi et al , 2011a inhibitor, FS cells did not fully flatten but did extend their cytoplasmic processes. In addition, although the motility of these cells was comparable to that of the control group, they only established sparse cellular interconnections by 72 h of culture ( Fig.…”

Section: Effect Of Mmp-9 Inhibitor On Fs Cells In Primary Culturesupporting

confidence: 63%

“…Previously, we discovered that FS cells formed networks in the presence of laminin, a process mediated through integrin b1 signaling (Horiguchi et al 2011a). Veeravalli et al (2010) showed that MMP-9 silencing downregulates the a-subunit and b-subunit of integrin in vitro.…”

Section: Discussionmentioning

confidence: 99%

“…In a series of experiments that investigated the influence on FS cells of laminin -an ECM component of the basement membrane -we found that FS cells exhibited a motile phenotype and enhanced proliferation and that they established numerous interconnections, which closely resembled their cellular arrangement in vivo (Horiguchi et al 2010(Horiguchi et al , 2011a. The high motility of FS cells on laminin suggested that, to migrate on the ECM, they must express matrix-degrading enzymes.…”

Section: Introductionmentioning

confidence: 99%

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Matrix metalloproteinase-9 expression in folliculostellate cells of rat anterior pituitary gland

Ilmiawati¹,

Horiguchi²,

Fujiwara³

et al. 2011

Journal of Endocrinology

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Folliculostellate (FS) cells of the anterior pituitary gland express a variety of regulatory molecules. Using transgenic rats that express green fluorescent protein specifically in FS cells, we recently demonstrated that FS cells in vitro showed marked changes in motility, proliferation, and that formation of cellular interconnections in the presence of laminin, a component of the extracellular matrix, closely resembled those observed in vivo. These findings suggested that FS cells express matrix metalloproteinase-9 (MMP-9), which assists their function on laminin. In the present study, we investigate MMP-9 expression in rat anterior pituitary gland and examine its role in motility and proliferation of FS cells on laminin. Immunohistochemistry, RT-PCR, immunoblotting, and gelatin zymography were performed to assess MMP-9 expression in the anterior pituitary gland and cultured FS cells. Real-time RT-PCR was used to quantify MMP-9 expression in cultured FS cells under different conditions and treatments. MMP-9 expression was inhibited by pharmacological inhibitor or downregulated by siRNA and time-lapse images were acquired. A 5-bromo-2 0 -deoxyuridine assay was performed to analyze the proliferation of FS cells. Our results showed that MMP-9 was expressed in FS cells, that this expression was upregulated by laminin, and that laminin induced MMP-9 secretion by FS cells. MMP-9 inhibition and downregulation did not impair FS motility; however, it did impair the capacity of FS cells to form interconnections and it significantly inhibited proliferation of FS cells on laminin. We conclude that MMP-9 is necessary in FS cell interconnection and proliferation in the presence of laminin.

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Section: Effect Of Mmp-9 Inhibitor On Fs Cells In Primary Culturesupporting

confidence: 63%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Matrix metalloproteinase-9 expression in folliculostellate cells of rat anterior pituitary gland

Ilmiawati¹,

Horiguchi²,

Fujiwara³

et al. 2011

Journal of Endocrinology

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“…In addition to their role in caveolae, Cav proteins also function in other subcellular locations of the cell such as the focal adhesion complex (10,11). As has been identified in cell types other than CM, Cav and integrin function may be cooperatively regulated (12)(13)(14)(15)(16). Various human Cav3 mutations result in loss of Cav3 function, and are associated with both hypertrophic and dilated cardiomyopathies, as well as a range of neuromuscular diseases (17)(18)(19).…”

mentioning

confidence: 99%

Caveolin modulates integrin function and mechanical activation in the cardiomyocyte

Israeli-Rosenberg

Chen

et al. 2014

FASEB j.

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β1 integrins (β1) transduce mechanical signals in many cells, including cardiac myocytes (CM). Given their close localization, as well as their role in mechanotransduction and signaling, we hypothesized that caveolin (Cav) proteins might regulate integrins in the CM. β1 localization, complex formation, activation state, and signaling were analyzed using wild-type, Cav3 knockout, and Cav3 CM-specific transgenic heart and myocyte samples. Studies were performed under basal and mechanically loaded conditions. We found that: (1) β1 and Cav3 colocalize in CM and coimmunoprecipitate from CM protein lysates; (2) β1 is detected in a subset of caveolae; (3) loss of Cav3 caused reduction of β1D integrin isoform and active β1 integrin from the buoyant domains in the heart; (4) increased expression of myocyte Cav3 correlates with increased active β1 integrin in adult CM; (5) in vivo pressure overload of the wild-type heart results in increased activated integrin in buoyant membrane domains along with increased association between active integrin and Cav3; and (6) Cav3-deficient myocytes have perturbed basal and stretch mediated signaling responses. Thus, Cav3 protein can modify integrin function and mechanotransduction in the CM and intact heart.

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“…For example, RVD depends on cation influx following membrane tension during hyposmotic cell swelling as shown in astrocytes and kidney cells (Hua et al, 2010). The influx of Ca 2+ in turn triggers a series of cellular signaling events, such as activation mitogen-activated protein kinases (MAPKs) including c-Jun NH2-terminal kinase, p38 MAPK and extracellular signal-regulated protein kinase 1/2 (Horiguchi et al, 2011; Shi et al, 2011). The last kinase is known to activate TRP channels (Ebner et al, 2006; Dine et al, 2014).…”

Section: Cellular Volumementioning

confidence: 99%

Interactions of the Mechanosensitive Channels with Extracellular Matrix, Integrins, and Cytoskeletal Network in Osmosensation

Jiao

Cui

Wang

et al. 2017

Front. Mol. Neurosci.

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Life is maintained in a sea water-like internal environment. The homeostasis of this environment is dependent on osmosensory system translation of hydromineral information into osmotic regulatory machinery at system, tissue and cell levels. In the osmosensation, hydromineral information can be converted into cellular reactions through osmoreceptors, which changes thirst and drinking, secretion of antidiuretic vasopressin (VP), reabsorption of water and salt in the kidneys at systemic level as well as cellular metabolic activity and survival status at tissue level. The key feature of osmosensation is the activation of mechanoreceptors or mechanosensors, particularly transient receptor potential vallinoid (TRPV) and canonical (TRPC) family channels, which increases cytosolic Ca2+ levels, activates osmosensory cells including VP neurons and triggers a series of secondary reactions. TRPV channels are sensitive to both hyperosmotic and hyposmotic stimuli while TRPC channels are more sensitive to hyposmotic challenge in neurons. The activation of TRP channels relies on changes in cell volume, membrane stretch and cytoskeletal reorganization as well as hydration status of extracellular matrix (ECM) and activity of integrins. Different families of TRP channels could be activated differently in response to hyperosmotic and hyposmotic stimuli in different spatiotemporal orders, leading to differential reactions of osmosensory cells. Together, they constitute the osmosensory machinery. The activation of this osmoreceptor complex is also associated with the activity of other osmolarity-regulating organelles, such as water channel protein aquaporins, Na-K-2Cl cotransporters, volume-sensitive anion channels, sodium pump and purinergic receptors in addition to intercellular interactions, typically astrocytic neuronal interactions. In this article, we review our current understandings of the composition of osmoreceptors and the processes of osmosensation.

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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

Cited by 21 publications

References 30 publications

Matrix metalloproteinase-9 expression in folliculostellate cells of rat anterior pituitary gland

Matrix metalloproteinase-9 expression in folliculostellate cells of rat anterior pituitary gland

Caveolin modulates integrin function and mechanical activation in the cardiomyocyte

Interactions of the Mechanosensitive Channels with Extracellular Matrix, Integrins, and Cytoskeletal Network in Osmosensation

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