Purification and Characterization of an FSH Releasing Protein from Porcine Ovarian Follicular Fluid

Vale, Wylie; Rivier, J.; Vaughan, Joan; McClintock, Richard A.; Corrigan, A; Woo, Wilson; Karr, David; Spiess, Joachim

doi:10.1097/00006254-198702000-00014

Cited by 219 publications

(285 citation statements)

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“…Activins and inhibins were first identified as important regulators of pituitary follicle-stimulating hormone release. (14)(15)(16)(17) Subsequent studies have demonstrated that activins are expressed in diverse tissues and play important roles in embryology, wound healing, and tissue homeostasis. (18)(19)(20)(21)(22) Activins signal by binding either the activin receptor type IIA (ActRIIA) or the activin receptor type IIB, which recruits the type I receptor, activin-like kinase 4 (Alk4), leading to phosphorylation of cytoplasmic Smads 2/3.…”

Section: J Jbmrmentioning

confidence: 99%

Inhibiting activin-A signaling stimulates bone formation and prevents cancer-induced bone destruction in vivo

Chantry

Heath

Mulivor

et al. 2010

Journal of Bone and Mineral Research

135

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Cancers that grow in bone, such as myeloma and breast cancer metastases, cause devastating osteolytic bone destruction. These cancers hijack bone remodeling by stimulating osteoclastic bone resorption and suppressing bone formation. Currently, treatment is targeted primarily at blocking bone resorption, but this approach has achieved only limited success. Stimulating osteoblastic bone formation to promote repair is a novel alternative approach. We show that a soluble activin receptor type IIA fusion protein (ActRIIA.muFc) stimulates osteoblastogenesis ( p < .01), promotes bone formation ( p < .01) and increases bone mass in vivo ( p < .001). We show that the development of osteolytic bone lesions in mice bearing murine myeloma cells is caused by both increased resorption ( p < .05) and suppression of bone formation ( p < .01). ActRIIA.muFc treatment stimulates osteoblastogenesis ( p < .01), prevents myeloma-induced suppression of bone formation ( p < .05), blocks the development of osteolytic bone lesions ( p < .05), and increases survival ( p < .05). We also show, in a murine model of breast cancer bone metastasis, that ActRIIA.muFc again prevents bone destruction ( p < .001) and inhibits bone metastases ( p < .05). These findings show that stimulating osteoblastic bone formation with ActRIIA.muFc blocks the formation of osteolytic bone lesions and bone metastases in models of myeloma and breast cancer and paves the way for new approaches to treating this debilitating aspect of cancer. ß

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Section: J Jbmrmentioning

confidence: 99%

Inhibiting activin-A signaling stimulates bone formation and prevents cancer-induced bone destruction in vivo

Chantry

Heath

Mulivor

et al. 2010

Journal of Bone and Mineral Research

135

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“…Activin is a multifunctional member of TGF- superfamily (15)(16)(17). Homo-or hetero-dimerization of two inhibin  subunits (A and B) form three types of activins, activin A (AA), activin B (BB) and activin AB (AB).…”

Section: Discussionmentioning

confidence: 99%

Direct Effects of Activin A on the Activation of Mouse Macrophage RAW264.7 Cells

Wang

Yang

et al. 2009

Cell Mol Immunol

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Macrophages play critical roles in innate immune and acquired immune via secreting pro-inflammatory mediators, phagocytosing microorganisms and presenting antigens. Activin A, a member of transforming growth factor  (TGF-) superfamily, is produced by macrophages and microglia cells. In this study, we reported a direct effect of activin A as a pro-inflammatory factor on mouse macrophage cell line RAW264.7 cells. Our data revealed that activin A could not only increase IL-1 and IL-6 production from RAW264.7 cells, but also promote pinocytic and phagocytic activities of RAW264.7 cells. In addition, activin A obviously up-regulated MHC II expression on the surface of RAW264.7 cells, whereas did not influence MHC I expression. Activin A also enhanced CD80 expression, which is a marker of activated macrophages, but did not influence RAW264.7 cell proliferation. These data suggest that activin A may regulate primary macrophage-mediated innate and acquired immune response via promoting the activation of rest macrophages. Cellular & Molecular Immunology. 2009;6(2):129-133.

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“…Activin (Ling et al, 1986;Vale et al, 1986) and transforming growth factor -p (TGF-P; Derynck et al, 1985) are members of a large growth factor superfam-0 1993 WILEY-LISS, INC. ily that includes Mullerian inhibiting substance (MIS; Cate et al, 1986), inhibin (Mason et al, 1985), bone morphogenetic proteins (Wozney et al, 19881, Drosophila decapentaplegic complex (Padgett et al, 1987), and Xenopus Vg-1 (Weeks and Melton, 1987). These proteins exist as latent dimeric precursors that undergo proteolytic processing to release homologous carboxyterminal fragments (Pepinsky et al, 1988).…”

Section: Introductionmentioning

confidence: 99%

Developmental expression of four novel serine/threonine kinase receptors homologous to the activin/transforming growth factor‐β type II receptor family

Gustafson

Hirobe

et al. 1993

Developmental Dynamics

164

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Serinekhreonine kinase transmembrane proteins are a new family of growth factor signal transducers that includes several isoforms of the activin type I1 receptor and the type I1 receptor for transforming growth factor-p. In an effort to clone the receptor for Mullerian inhibiting substance, a member of the transforming growth factor-p superfamily, oligonucleotide primers designed from conserved regions of these receptors' kinase domains were used for PCR amplification of fetal rat urogenital ridge cDNA. We isolated four novel receptors in this manner (designated Rl-R4), each of which has structural features of the previously cloned kinases, including a small extracellular ligand-binding domain, a single hydrophobic transmembrane domain, and an intracellular serinekhreonine kinase domain. In addition, each has characteristic kinase subdomains and conserved serinekhreonine kinase sequences found in this family. Northern analysis revealed mRNA expression of R1-R4 in several tissues, including fetal urogenital ridge, testis, and ovary, as well as brain and lung. In situ hybridization further localized R1 to mesenchyme of the 14.5 to 15-day fetal rat Mullerian duct and to oocytes of preantral and antral follicles, sites that are consistent with the predicted localization of Mullerian inhibiting substance receptor. In addition, R2 localized specifically to seminiferous tubules of the postnatal testis. These newest members of the activin and transforming growth factor-p type I1 receptor family should help define the molecular mechanisms by which this ligand superfamily affects cell growth and differentiation via membrane phosphorylation.

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Purification and Characterization of an FSH Releasing Protein from Porcine Ovarian Follicular Fluid

Cited by 219 publications

References 0 publications

Inhibiting activin-A signaling stimulates bone formation and prevents cancer-induced bone destruction in vivo

Inhibiting activin-A signaling stimulates bone formation and prevents cancer-induced bone destruction in vivo

Direct Effects of Activin A on the Activation of Mouse Macrophage RAW264.7 Cells

Developmental expression of four novel serine/threonine kinase receptors homologous to the activin/transforming growth factor‐β type II receptor family

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