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Journal articles on the topic 'Bone Morphogenetic Protein 6'

Author: Grafiati

Published: 4 June 2021

Last updated: 11 February 2022

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1

Hong, Jun Hyuk, Geun Taek Lee, Jae Ho Lee, et al. "Effect of bone morphogenetic protein-6 on macrophages." Immunology 128, no. 1pt2 (2009): e442-e450. http://dx.doi.org/10.1111/j.1365-2567.2008.02998.x.

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2

Simic, P., L. Grgurevic, I. Orlic, V. Kufner, R. Spaventi, and S. Vukicevic. "Bone morphogenetic protein-6 (bmp-6) affects bone and glucose via IGF-I." Bone 44 (June 2009): S316. http://dx.doi.org/10.1016/j.bone.2009.03.592.

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3

Kiyoshi, T. A., K. Uchida, and S. Tateyama. "Expression of Bone Morphogenetic Protein-6 and Bone Morphogenetic Protein Receptors in Myoepithelial Cells of Canine Mammary Gland Tumors." Veterinary Pathology 41, no. 2 (2004): 154–63. http://dx.doi.org/10.1354/vp.41-2-154.

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4

Wang, Jesse F., Ming‐Song Lee, Tsung‐Lin Tsai, et al. "Bone Morphogenetic Protein‐6 Attenuates Type 1 Diabetes Mellitus‐Associated Bone Loss." STEM CELLS Translational Medicine 8, no. 6 (2019): 522–34. http://dx.doi.org/10.1002/sctm.18-0150.

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5

Semevolos, Stacy A., Alan J. Nixon, and M. Lisa Strassheim. "Expression of bone morphogenetic protein-6 and -2 and a bone morphogenetic protein antagonist in horses with naturally acquired osteochondrosis." American Journal of Veterinary Research 65, no. 1 (2004): 110–15. http://dx.doi.org/10.2460/ajvr.2004.65.110.

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6

Dendooven, Amélie, Olivia van Oostrom, Dionne M. van der Giezen, et al. "Loss of Endogenous Bone Morphogenetic Protein-6 Aggravates Renal Fibrosis." American Journal of Pathology 178, no. 3 (2011): 1069–79. http://dx.doi.org/10.1016/j.ajpath.2010.12.005.

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7

Noguchi, Taiki, Mayuko Ikeda, Masaru Murakami, et al. "Regulatory expression of bone morphogenetic protein 6 by 2,2′-dipyridyl." Biochimica et Biophysica Acta (BBA) - General Subjects 1864, no. 8 (2020): 129610. http://dx.doi.org/10.1016/j.bbagen.2020.129610.

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8

Plant, Andrea, and Jonathan H. Tobias. "Increased Bone Morphogenetic Protein-6 Expression in Mouse Long Bones After Estrogen Administration." Journal of Bone and Mineral Research 17, no. 5 (2002): 782–90. http://dx.doi.org/10.1359/jbmr.2002.17.5.782.

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9

Sugiura, Koji, and John J. Eppig. "Reduced Fertility in Bone Morphogenetic Protein 6 (Bmp6) Null Female Mice." Biology of Reproduction 81, Suppl_1 (2009): 106. http://dx.doi.org/10.1093/biolreprod/81.s1.106.

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10

He, Yinghua, Ying Cui, Baiying Xu, Jun Gu, Wei Wang, and Xiaoying Luo. "Hypermethylation Leads to Bone Morphogenetic Protein 6 Downregulation in Hepatocellular Carcinoma." PLoS ONE 9, no. 1 (2014): e87994. http://dx.doi.org/10.1371/journal.pone.0087994.

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11

Wang, Yun, Chen-Fu Chang, Marisela Morales, et al. "Bone Morphogenetic Protein-6 Reduces Ischemia-Induced Brain Damage in Rats." Stroke 32, no. 9 (2001): 2170–78. http://dx.doi.org/10.1161/hs0901.095650.

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12

Brkljacic, Jelena, Martina Pauk, Igor Erjavec, et al. "Exogenous heparin binds and inhibits bone morphogenetic protein 6 biological activity." International Orthopaedics 37, no. 3 (2013): 529–41. http://dx.doi.org/10.1007/s00264-012-1714-3.

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13

Ebisawa, T., K. Tada, I. Kitajima, et al. "Characterization of bone morphogenetic protein-6 signaling pathways in osteoblast differentiation." Journal of Cell Science 112, no. 20 (1999): 3519–27. http://dx.doi.org/10.1242/jcs.112.20.3519.

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Bone morphogenetic protein (BMP)-6 is a member of the transforming growth factor (TGF)-(β) superfamily, and is most similar to BMP-5, osteogenic protein (OP)-1/BMP-7, and OP-2/BMP-8. In the present study, we characterized the endogenous BMP-6 signaling pathway during osteoblast differentiation. BMP-6 strongly induced alkaline phosphatase (ALP) activity in cells of osteoblast lineage, including C2C12 cells, MC3T3-E1 cells, and ROB-C26 cells. The profile of binding of BMP-6 to type I and type II receptors was similar to that of OP-1/BMP-7 in C2C12 cells and MC3T3-E1 cells; BMP-6 strongly bound to activin receptor-like kinase (ALK)-2 (also termed ActR-I), together with type II receptors, i.e. BMP type II receptor (BMPR-II) and activin type II receptor (ActR-II). In addition, BMP-6 weakly bound to BMPR-IA (ALK-3), to which BMP-2 also bound. In contrast, binding of BMP-6 to BMPR-IB (ALK-6), and less efficiently to ALK-2 and BMPR-IA, together with BMPR-II was detected in ROB-C26 cells. Intracellular signalling was further studied using C2C12 and MC3T3-E1 cells. Among the receptor-regulated Smads activated by BMP receptors, BMP-6 strongly induced phosphorylation and nuclear accumulation of Smad5, and less efficiently those of Smad1. However, Smad8 was constitutively phosphorylated, and no further phosphorylation or nuclear accumulation of Smad8 by BMP-6 was observed. These findings indicate that in the process of differentiation to osteoblasts, BMP-6 binds to ALK-2 as well as other type I receptors, and transduces signals mainly through Smad5 and possibly through Smad1.

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14

Beckmann, Johannes, Franz Kock, Markus Tingart, Juergen Goetz, Joachim Grifka, and Jens Schaumburger. "Pseudarthrosis in fibrous dysplasia treated with bone morphogenetic protein." Open Medicine 3, no. 3 (2008): 377–79. http://dx.doi.org/10.2478/s11536-008-0028-8.

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AbstractWe present a case of pseudarthrosis in a patient suffering from polyostotic fibrous dysplasia of the right part of the body that was successfully treated with bone morphogenetic protein. Pseudarthrosis occurred after proximal femoral shaft fracture due to a motorcycle accident initially treated by intramedullary nailing. After revision, the patient was treated by pseudarthrosis debridement and grafting of bone morphogenetic protein-7/osteogenic protein-1, resulting in callus formation that allowed indolent full weight-bearing after 6 weeks. The underlying disease as well as the described treatment is discussed.

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15

Kishimoto, K. N., Y. Watanabe, H. Nakamura, and S. Kokubun. "Ectopic bone formation by electroporatic transfer of bone morphogenetic protein-4 gene." Bone 31, no. 2 (2002): 340–47. http://dx.doi.org/10.1016/s8756-3282(02)00825-6.

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16

Dai, Jinlu, Jill Keller, Jian Zhang, Yi Lu, Zhi Yao, and Evan T. Keller. "Bone Morphogenetic Protein-6 Promotes Osteoblastic Prostate Cancer Bone Metastases through a Dual Mechanism." Cancer Research 65, no. 18 (2005): 8274–85. http://dx.doi.org/10.1158/0008-5472.can-05-1891.

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17

Haque, Tasima, Manuela Mandu-Hrit, Frank Rauch, Dominique Lauzier, Maryam Tabrizian, and Reggie C. Hamdy. "Immunohistochemical Localization of Bone Morphogenetic Protein-signaling Smads during Long-bone Distraction Osteogenesis." Journal of Histochemistry & Cytochemistry 54, no. 4 (2006): 407–15. http://dx.doi.org/10.1369/jhc.5a6738.2005.

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In this study we investigated the expression of bone morphogenetic protein (BMP)-signaling Smads in distraction osteogenesis (DO). Osteotomy of the right tibia was performed in 14 skeletally mature white New Zealand male rabbits. Lengthening was started 1 week later at a rate of 0.5 mm/12 hr and was maintained for 3 weeks. Expression of Smad proteins 1, 4, 5, 6, 7, and 8 and Smad ubiquitin regulatory factors (Smurfs) 1 and 2 was evaluated in the distracted zone using immunohistochemistry. Expression of receptor-regulated Smads (R-Smads) 1, 5, and 8 showed a significant increase during the distraction phase, followed by a gradual decrease during the consolidation phase. Smad 4 showed significant expression during both distraction and the beginning of the consolidation phase. Smad 6 and Smad 7 were highly expressed during the consolidation phase. Staining for both Smurfs 1 and 2 was maximal at the end of the distraction period. Staining for all proteins was most intense in chondrocyte and fibroblast-like cells. Expression pattern of R-Smads correlated with our previously reported expression pattern of BMPs 2, 4, and 7 and their receptors. These results therefore suggest a role for the whole BMP signaling pathway including the Smad proteins in DO.

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18

Gazzerro, Elisabetta, and Ernesto Canalis. "Bone morphogenetic proteins and their antagonists." Reviews in Endocrine and Metabolic Disorders 7, no. 1-2 (2006): 51–65. http://dx.doi.org/10.1007/s11154-006-9000-6.

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19

Goutel, Carole, Yasuyuki Kishimoto, Stefan Schulte-Merker, and Frédéric Rosa. "The ventralizing activity of Radar, a maternally expressed bone morphogenetic protein, reveals complex bone morphogenetic protein interactions controlling dorso-ventral patterning in zebrafish." Mechanisms of Development 99, no. 1-2 (2000): 15–27. http://dx.doi.org/10.1016/s0925-4773(00)00470-6.

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20

Wall, N. A., M. Blessing, C. V. Wright, and B. L. Hogan. "Biosynthesis and in vivo localization of the decapentaplegic-Vg-related protein, DVR-6 (bone morphogenetic protein-6)." Journal of Cell Biology 120, no. 2 (1993): 493–502. http://dx.doi.org/10.1083/jcb.120.2.493.

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DVR-6 (BMP-6 or Vgr-1) is a member of the TGF-beta superfamily of polypeptide signaling molecules. In situ hybridization studies have previously shown that DVR-6 RNA is expressed in a variety of cell types in the mouse embryo, but no information has been available on protein localization and biosynthesis. We have produced a polyclonal antibody to the proregion of DVR-6 and used it to localize the protein in whole mount and sectioned embryonic, newborn, and adult mouse tissues. DVR-6 protein is expressed in the mouse nervous system beginning at 9.5 days postcoitum (d.p.c.) and continues through adulthood. A variety of epithelial tissues also produce DVR-6 protein, including the suprabasal layer of the skin, bronchiolar epithelium, and the cornea. Additionally, a stably transfected cell line, BMGE+H/D6c4, is used to study the biosynthesis of DVR-6 protein and evidence is presented for translational regulation of DVR-6 expression.

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21

U., Ripamonti. "Craniofacial bone regeneration by osteogenic protein-1 (hOP-1/BMP-7) and related bone morphogenetic proteins." International Journal of Oral and Maxillofacial Surgery 26 (January 1997): 25. http://dx.doi.org/10.1016/s0901-5027(97)80921-6.

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22

Kusafuka, Kimihide, Akira Yamaguchi, Teruo Kayano, and Tamiko Takemura. "Immunohistochemical localization of the bone morphogenetic protein‐6 in salivary pleomorphic adenomas." Pathology International 49, no. 12 (1999): 1023–27. http://dx.doi.org/10.1046/j.1440-1827.1999.00991.x.

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23

Thomas, BG, and FC Hamdy. "Bone morphogenetic protein-6: potential mediator of osteoblastic metastases in prostate cancer." Prostate Cancer and Prostatic Diseases 3, no. 4 (2000): 283–85. http://dx.doi.org/10.1038/sj.pcan.4500482.

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24

Kleven, Mark D., Caroline A. Enns, and An-Sheng Zhang. "Bone Morphogenetic Protein-6 Mutations Take Their Place in Iron Overload Diseases." Gastroenterology 150, no. 3 (2016): 556–59. http://dx.doi.org/10.1053/j.gastro.2016.01.016.

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25

Daibata, Masanori, Yuiko Nemoto, Kentaro Bandobashi, et al. "Promoter Hypermethylation of the Bone Morphogenetic Protein-6 Gene in Malignant Lymphoma." Clinical Cancer Research 13, no. 12 (2007): 3528–35. http://dx.doi.org/10.1158/1078-0432.ccr-06-2766.

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26

Pauk, Martina, Tatjana Bordukalo-Niksic, Jelena Brkljacic, et al. "A novel role of bone morphogenetic protein 6 (BMP6) in glucose homeostasis." Acta Diabetologica 56, no. 3 (2018): 365–71. http://dx.doi.org/10.1007/s00592-018-1265-1.

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27

Du, Jun, Yanjuan Zhu, Xiangyu Chen, et al. "Protective effect of bone morphogenetic protein-6 on neurons from H2O2 injury." Brain Research 1163 (August 2007): 10–20. http://dx.doi.org/10.1016/j.brainres.2007.06.002.

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28

Irie, Atsushi, Hiroko Habuchi, Koji Kimata, and Yutaka Sanai. "Heparan sulfate is required for bone morphogenetic protein-7 signaling." Biochemical and Biophysical Research Communications 308, no. 4 (2003): 858–65. http://dx.doi.org/10.1016/s0006-291x(03)01500-6.

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29

Bunakase, Takano, Kenta Ariga, Shimpei Miyamoto, et al. "Distribution of genes for bone morphogenetic protein—4, —6, growth differentiation factor—5, and bone morphogenetic protein receptors in the process of experimental spondylosis in mice." Journal of Neurosurgery: Spine 94, no. 1 (2001): 68–75. http://dx.doi.org/10.3171/spi.2001.94.1.0068.

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Object. Because little is known about the molecular mechanisms underlying the process of spondylosis, the authors examined the extent of genetic localization of several members of bone morphogenetic protein (BMP) and BMP receptors in chondrogenesis during the process of inducing spondylosis in their previously established experimental mice model. Methods. Experimental spondylosis was induced in 5-week-old ICR mice. The cervical spine was harvested chronologically, and histological sections were prepared. Messenger RNA for BMP-4, growth and differentiation (GDF)—5, BMP-6, and BMP receptors (ALK-3, -6, and BMP-RII) was localized in the tissue sections by in situ hybridization. In the early stage, BMP-4—derived mRNA was localized mainly in cells in the anterior margin of the cervical discs, together with ALK-6 and BMP-RII mRNA. No GDF-5 and BMP-6 mRNA was detected at this stage. In the late stage, cells positive for BMP-4 decreased, whereas GDF-5 and BMP-6 mRNA were localized in cells undergoing chondrogenesis. The ALK-3 mRNA began to appear in this stage, as did ALK-6 and BMP-RII. Conclusions. The localization of transcripts for BMP-4, -6, and GDF-5 as well as BMP receptors shown during the present experimental model indicate the possible involvement of molecular signaling by these BMPs in the chondrogenic progress in spondylosis.

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30

Steinbicker, Andrea U., Chetana Sachidanandan, Ashley J. Vonner, et al. "Inhibition of bone morphogenetic protein signaling attenuates anemia associated with inflammation." Blood 117, no. 18 (2011): 4915–23. http://dx.doi.org/10.1182/blood-2010-10-313064.

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Abstract Anemia of inflammation develops in settings of chronic inflammatory, infectious, or neoplastic disease. In this highly prevalent form of anemia, inflammatory cytokines, including IL-6, stimulate hepatic expression of hepcidin, which negatively regulates iron bioavailability by inactivating ferroportin. Hepcidin is transcriptionally regulated by IL-6 and bone morphogenetic protein (BMP) signaling. We hypothesized that inhibiting BMP signaling can reduce hepcidin expression and ameliorate hypoferremia and anemia associated with inflammation. In human hepatoma cells, IL-6–induced hepcidin expression, an effect that was inhibited by treatment with a BMP type I receptor inhibitor, LDN-193189, or BMP ligand antagonists noggin and ALK3-Fc. In zebrafish, the induction of hepcidin expression by transgenic expression of IL-6 was also reduced by LDN-193189. In mice, treatment with IL-6 or turpentine increased hepcidin expression and reduced serum iron, effects that were inhibited by LDN-193189 or ALK3-Fc. Chronic turpentine treatment led to microcytic anemia, which was prevented by concurrent administration of LDN-193189 or attenuated when LDN-193189 was administered after anemia was established. Our studies support the concept that BMP and IL-6 act together to regulate iron homeostasis and suggest that inhibition of BMP signaling may be an effective strategy for the treatment of anemia of inflammation.

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31

Wutzl, A., W. Brozek, I. Lernbass, et al. "Bone morphogenetic proteins 5 and 6 stimulate osteoclast generation." International Journal of Oral and Maxillofacial Surgery 34 (January 2005): 122. http://dx.doi.org/10.1016/s0901-5027(05)81359-1.

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32

Wutzl, Arno, Wolfgang Brozek, Isolde Lernbass, et al. "Bone morphogenetic proteins 5 and 6 stimulate osteoclast generation." Journal of Biomedical Materials Research Part A 77A, no. 1 (2006): 75–83. http://dx.doi.org/10.1002/jbm.a.30615.

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33

Araújo, Valdevane Rocha, Isabel Bezerra Lima-Verde, Khessler Patrícia Olazia Name, et al. "Bone Morphogenetic Protein-6 (BMP-6) induces atresia in goat primordial follicles cultured in vitro." Pesquisa Veterinária Brasileira 30, no. 9 (2010): 770–81. http://dx.doi.org/10.1590/s0100-736x2010000900010.

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This study investigated the effects of bone morphogenetic protein 6 (BMP-6) on in vitro primordial follicle development in goats. Samples of goat ovarian cortex were cultured in vitro for 1 or 7 days in Minimum Essential Medium (control medium) supplemented with different concentrations of BMP-6. Follicle survival, activation and growth were evaluated through histology and transmission electron microscopy (TEM). After 7 days of culture, histological analysis demonstrated that BMP-6 enhanced the percentages of atretic primordial follicles when compared to fresh control (day 0). Nevertheless, BMP-6 increased follicular and oocyte diameter during both culture periods. As the culture period progressed from day 1 to day 7, a significant increase in follicle diameter was observed with 1 or 50ng/ml BMP-6. However, on the contrary to that observed with the control medium TEM revealed that follicles cultured for up to 7 days with 1 or 50ng/ml BMP-6 had evident signs of atresia. In conclusion, this study demonstrated that BMP-6 negatively affects the survival and ultrastructure of goat primordial follicles.

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34

Lind, M., E. F. Eriksen, and C. Bünger. "Bone morphogenetic protein-2 but not bone morphogenetic protein-4 and -6 stimulates chemotactic migration of human osteoblasts, human marrow osteoblasts, and U2-OS cells." Bone 18, no. 1 (1996): 53–57. http://dx.doi.org/10.1016/8756-3282(95)00423-8.

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35

Makanga, Martine, Céline Dewachter, Hidekazu Maruyama, et al. "Downregulated bone morphogenetic protein signaling in nitrofen-induced congenital diaphragmatic hernia." Pediatric Surgery International 29, no. 8 (2013): 823–34. http://dx.doi.org/10.1007/s00383-013-3340-6.

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36

Munir, Arooj, Anne Døskeland, Steven J. Avery, et al. "Efficacy of copolymer scaffolds delivering human demineralised dentine matrix for bone regeneration." Journal of Tissue Engineering 10 (January 2019): 204173141985270. http://dx.doi.org/10.1177/2041731419852703.

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Poly(L-lactide-co-ε-caprolactone) scaffolds were functionalised by 10 or 20 µg/mL of human demineralised dentine matrix. Release kinetics up to 21 days and their osteogenic potential on human bone marrow stromal cells after 7 and 21 days were studied. A total of 390 proteins were identified by mass spectrometry. Bone regeneration proteins showed initial burst of release. Human bone marrow stromal cells were cultured on scaffolds physisorbed with 20 µg/mL and cultured in basal medium (DDM group) or physisorbed and cultured in osteogenic medium or cultured on non-functionalised scaffolds in osteogenic medium. The human bone marrow stromal cells proliferated less in demineralised dentine matrix group and activated ERK/1/2 after both time points. Cells on DDM group showed highest expression of IL-6 and IL-8 at 7 days and expressed higher collagen type 1 alpha 2, SPP1 and bone morphogenetic protein-2 until 21 days. Extracellular protein revealed higher collagen type 1 and bone morphogenetic protein-2 at 21 days in demineralised dentine matrix group. Cells on DDM group showed signs of mineralisation. The functionalised scaffolds were able to stimulate osteogenic differentiation of human bone marrow stromal cells.

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37

Fujimori, Youichi, Takashi Nakamura, Shinichiro Ijiri, Kazuya Shimizu, and Takao Yamamuro. "Heterotopic bone formation induced by bone morphogenetic protein in mice with collagen-induced arthritis." Biochemical and Biophysical Research Communications 186, no. 3 (1992): 1362–67. http://dx.doi.org/10.1016/s0006-291x(05)81556-6.

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38

Mehler, Mark F., Peter C. Mabie, Damin Zhang, and John A. Kessler. "Bone morphogenetic proteins in the nervous system." Trends in Neurosciences 20, no. 7 (1997): 309–17. http://dx.doi.org/10.1016/s0166-2236(96)01046-6.

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39

Paralkar, V. M., L. Grgurevic, P. Simic, et al. "A novel role of bone morphogenetic protein-6 (BMP-6) as an endocrine regulator of bone and glucose homeostasis." Bone 47 (June 2010): S57. http://dx.doi.org/10.1016/j.bone.2010.04.107.

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40

Kejner, Alexandra E., M. Benjamin Burch, Larissa Sweeny, and Eben L. Rosenthal. "Bone morphogenetic protein 6 expression in oral cavity squamous cell cancer is associated with bone invasion." Laryngoscope 123, no. 12 (2013): 3061–65. http://dx.doi.org/10.1002/lary.24267.

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41

Grgurevic, L., I. Erjavec, G. Bicanic, et al. "Human Bone Morphogenetic Protein-1-3 (BMP-1-3) and BMP-6 synergistically influence bone healing." Bone 44 (June 2009): S309—S310. http://dx.doi.org/10.1016/j.bone.2009.03.575.

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42

Hjertner, Öyvind, Henrik Hjorth-Hansen, Magne Börset, Carina Seidel, Anders Waage, and Anders Sundan. "Bone morphogenetic protein-4 inhibits proliferation and induces apoptosis of multiple myeloma cells." Blood 97, no. 2 (2001): 516–22. http://dx.doi.org/10.1182/blood.v97.2.516.

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Abstract Bone morphogenetic proteins (BMPs) can be isolated from organic bone matrix and are able to initiate de novo cartilage and bone formation. Here it is shown that BMP-4 inhibited DNA synthesis in a dose-dependent manner in 3 IL-6–dependent multiple myeloma (MM) cell lines (OH-2, IH-1, and ANBL-6). In contrast, no effect on DNA synthesis was observed in 3 IL-6–independent MM cell lines (JJN-3, U266, and RPMI 8226). BMP-4 induced cell cycle growth arrest in the G0/G1 phase in OH-2 and ANBL-6 cells but not in IH-1 cells. BMP-4 induced apoptosis in OH-2 and IH-1 cells, but not significantly in ANBL-6 cells. Furthermore, BMP-4 induced apoptosis in freshly isolated MM cells from 4 of 13 patients. In the OH-2 and ANBL-6 cell lines and in a patient sample, immunoblotting showed that BMP-4 down-regulated IL-6–induced tyrosine phosphorylation of Stat3, suggesting a mechanism for the apparent antagonism between IL-6 and BMP-4. BMP-4 or analogues may be attractive therapeutic agents in MM because of possible beneficial effects on both tumor burden and bone disease.

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43

Kim, Airie, Tomas Ganz, and Seth Rivera. "THE ROLE OF BONE MORPHOGENETIC PROTEIN 6 IN THE ANEMIA OF LUNG CANCER." Chest 136, no. 4 (2009): 20S. http://dx.doi.org/10.1016/s0012-3692(16)47768-8.

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44

Zhang, Ming, Qing Wang, Wei Yuan, et al. "Epigenetic regulation of bone morphogenetic protein-6 gene expression in breast cancer cells." Journal of Steroid Biochemistry and Molecular Biology 105, no. 1-5 (2007): 91–97. http://dx.doi.org/10.1016/j.jsbmb.2007.01.002.

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45

Cabanas-Danés, Jordi, Ellie Landman, Jurriaan Huskens, Marcel Karperien, and Pascal Jonkheijm. "Hydrolytically Labile Linkers Regulate Release and Activity of Human Bone Morphogenetic Protein-6." Langmuir 34, no. 31 (2018): 9298–306. http://dx.doi.org/10.1021/acs.langmuir.8b00853.

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46

Joo, Young Bin, So-Young Bang, Tae-Hwan Kim, et al. "Bone Morphogenetic Protein 6 Polymorphisms Are Associated with Radiographic Progression in Ankylosing Spondylitis." PLoS ONE 9, no. 8 (2014): e104966. http://dx.doi.org/10.1371/journal.pone.0104966.

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47

Ratliff, Timothy L. "Bone Morphogenetic Protein (BMP)-6 Signaling and BMP Antagonist Noggin in Prostate Cancer." Journal of Urology 173, no. 5 (2005): 1825. http://dx.doi.org/10.1016/s0022-5347(05)60734-3.

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48

Tamada, Hiroshi, Riko Kitazawa, Kazuo Gohji, and Sohei Kitazawa. "Epigenetic Regulation of Human Bone Morphogenetic Protein 6 Gene Expression in Prostate Cancer." Journal of Bone and Mineral Research 16, no. 3 (2001): 487–96. http://dx.doi.org/10.1359/jbmr.2001.16.3.487.

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49

Banach, Joanna, Wojciech Gilewski, Artur Słomka, et al. "Bone morphogenetic protein 6-a possible new player in pathophysiology of heart failure." Clinical and Experimental Pharmacology and Physiology 43, no. 12 (2016): 1247–50. http://dx.doi.org/10.1111/1440-1681.12665.

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50

Feng, Qi, Mary C. Migas, Abdul Waheed, Robert S. Britton, and Robert E. Fleming. "Ferritin upregulates hepatic expression of bone morphogenetic protein 6 and hepcidin in mice." American Journal of Physiology-Gastrointestinal and Liver Physiology 302, no. 12 (2012): G1397—G1404. http://dx.doi.org/10.1152/ajpgi.00020.2012.

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Abstract:

Hepcidin is a hepatocellular hormone that inhibits the release of iron from certain cell populations, including enterocytes and reticuloendothelial cells. The regulation of hepcidin ( HAMP) gene expression by iron status is mediated in part by the signaling molecule bone morphogenetic protein 6 (BMP6). We took advantage of the low iron status of juvenile mice to characterize the regulation of Bmp6 and Hamp1 expression by iron administered in three forms: 1) ferri-transferrin (Fe-Tf), 2) ferric ammonium citrate (FAC), and 3) liver ferritin. Each of these forms of iron enters cells by distinct mechanisms and chemical forms. Iron was parenterally administered to 10-day-old mice, and hepatic expression of Bmp6 and Hamp1 mRNAs was measured 6 h later. We observed that hepatic Bmp6 expression increased in response to ferritin but was unchanged by Fe-Tf or FAC. Hepatic Hamp1 expression likewise increased in response to ferritin and Fe-Tf but was decreased by FAC. Exogenous ferritin increased Bmp6 and Hamp1 expression in older mice as well. Removing iron from ferritin markedly decreased its effect on Bmp6 expression. Exogenously administered ferritin and the derived iron localized in the liver primarily to sinusoidal lining cells. Moreover, expression of Bmp6 mRNA in isolated adult rodent liver cells was much higher in sinusoidal lining cells than hepatocytes (endothelial >> stellate > Kupffer). We conclude that exogenous iron-containing ferritin upregulates hepatic Bmp6 expression, and we speculate that liver ferritin contributes to regulation of Bmp6 and, thus, Hamp1 genes.

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