Tachykinins and neurokinin receptors in bone marrow functions: neural-hematopoietic link

References

• Patel N, Castillo M, Rameshwar P. An in vitro method to study the effects of hematopoietic regulators during immune and blood cell development. Biol Proced Online. 2007;(9):56–64.
   Google Scholar
• Metcalf D. Hematopoietic cytokines. Blood. 2008;111(2):485–491.
   PubMed Web of Science ®Google Scholar
• Van Hagen PM, Krenning EP, Kwekkeboom DJ, et al. Somatostatin and the immune and haematopoetic system: a review. Eur J Clin Invest. 1994;24(2):91–99.
   Web of Science ®Google Scholar
• Maestroni GJM. Adrenergic regulation of haematopoiesis. Pharmacol Res. 1995;32(5):249–252.
   Web of Science ®Google Scholar
• Greco SJ, Corcoran KE, Cho CJ, Rameshwar P Tachykinins in the emerging immune system: relevance to bone marrow homeostasis and maintenance of hematopoietic stem cells. FrontBiosci. 2004;(9):1782–1793.
   Google Scholar
• Rameshwar P, Poddar A, Gascón P. Hematopoietic regulation mediated by interactions among the neurokinins and cytokines. Leuk Lymphoma. 1997;28(1–2):1–10.
   PubMed Web of Science ®Google Scholar
• Pinto FM, Almeida TA, Hernández M, Devillier P, Advenier C, Candenas, ML. mRNA expression of tachykinins and tachykinin receptors in different human tissues. Eur J Pharmacol. 2004;494 (2–3):233–239.
   Web of Science ®Google Scholar
• Von Euler US, Gaddum JH. An unidentified depressor substance in certain tissue extracts. J Physiol (Lond). 1931;72(1):74–87.
   Google Scholar
• Chang MM, Leeman SE, Niall HD. Amino acid sequence of substance P. Nature. 1971;232(29):86–87.
   Web of Science ®Google Scholar
• Kimura S, Okada M, Sugita Y, Kanazawa I, Munekata E. Novel Neuropeptides, Neurokinin α and β, Isolated from Porcine Spinal Cord. Proc Jpn Acad. 1983;(59):101–104.
   Google Scholar
• Kangawa K, Minamino N, Fukuda A, Matsuo H. Neuromedin K: a novel mammalian tachykinin identified in porcine spinal cord. Biochem Biophys Res Commun. 1983;114(2):533–540.
   Web of Science ®Google Scholar
• Nawa H, Doteuchi M, Igano K, Inouye K, Nakanishi S. Substance K: a novel mammalian tachykinin that differs from substance P in its pharmacological profile. Life Sci. 1984;34(12):1153–1160.
   Web of Science ®Google Scholar
• Liu K, Castillo MD, Murthy RG, Patel N, Rameshwar P. Tachykinins and hematopoiesis. Clin Chim Acta. 2007;385(1–2):28–34.
   PubMed Web of Science ®Google Scholar
• Page NM. Hemokinins and endokinins. Cell Mol Life Sci. 2004;61(13):1652–1663.
   Web of Science ®Google Scholar
• Almeida TA, Rojo J, Nieto PM, Pinto FM, et al. Tachykinins and tachykinin receptors: structure and activity relationships. Curr Med Chem. 2004;11(15):2045–2081.
   PubMed Web of Science ®Google Scholar
• MacDonald MR, McCourt DW, Krause JE. Posttranslational processing of alpha-, beta-, and gamma-preprotachykinins. Cell-free translation and early posttranslational processing events. J Biol Chem. 1988;263(29):15176–15183.
   Web of Science ®Google Scholar
• Eipper BA, Stoffers DA, Mains RE. The biosynthesis of neuropeptides: peptide alpha-amidation. Annu Rev Neurosci. 1992;(15):57–85.
   Google Scholar
• Joshi DD, Dang A, Yadav P, et al. Negative feedback on the effects of stem cell factor on hematopoiesis is partly mediated through neutral endopeptidase activity on substance P: a combined functional and proteomic study. Blood. 2001;98(9):2697–2706.
   Web of Science ®Google Scholar
• Klassert TE, Pinto F, Hernández M, et al. Differential expression of neurokinin B and hemokinin-1 in human immune cells. J Neuroimmunol. 2008;196(1–2):27–34.
   Web of Science ®Google Scholar
• Zhang Y, Berger A, Milne CD, Paige CJ. Tachykinins in the immune system. Curr Drug Targets. 2006;7(8):1011–1020.
   PubMed Web of Science ®Google Scholar
• Chavolla-Calderón M, Bayer MK, Fontán JJ. Bone marrow transplantation reveals an essential synergy between neuronal and hemopoietic cell neurokinin production in pulmonary inflammation. J Clin Invest. 2003;111(7):973–980.
   Web of Science ®Google Scholar
• Page NM, Bell NJ, Gardiner S, et al. Characterization of the endokinins: human tachykinins with cardiovascular activity. Proc Natl Acad Sci USA. 2003;100(10):6245–6250.
   Web of Science ®Google Scholar
• Ho WZ, Douglas SD. Substance P and neurokinin-1 receptor modulation of HIV J Neuroimmunol. 2004;157(1–2):48–55.
   Web of Science ®Google Scholar
• Nowicki M, Ostalska-Nowicka D, Kondraciuk B, Miskowiak B. The significance of substance P in physiological and malignant haematopoiesis. J Clin Pathol. 2007;60(7):749–755.
   PubMed Web of Science ®Google Scholar
• Sudakov SK, Medvedeva OF, Rusakova IV, Terebilina NN, Goldberg SR. Differences in genetic predisposition to high anxiety in two inbred rat strains: role of substance P, diazepam binding inhibitor fragment and neuropeptide Y Psychopharmacol. 2001 ;154(4):327–335.
   Web of Science ®Google Scholar
• Stockmeier CA, Shi X, Konick L, et al. Neurokinin-1 receptors are decreased in major depressive disorder. Neuroreport. 2002;13(9):1223–1227.
   Web of Science ®Google Scholar
• Rioux L, Joyce JN. Substance P receptors are differentially affected in Parkinson’s and Alzheimer’s disease. J Neural Transm Park Dis Dement Sect. 1993;6(3):199–210.
   Google Scholar
• Vink R, Nimmo AJ, Cernak I. An overview of new and novel pharmacotherapies for use in traumatic brain injury. Clin Exp Pharmacol Physiol. 2001;28(11):919–921.
   Web of Science ®Google Scholar
• Stumm R, Culmsee C, Schafer MK, Krieglstein J, Weihe E. Adaptive plasticity in tachykinin and tachykinin receptor expression after focal cerebral ischemia is differentially linked to gabaergic and glutamatergic cerebrocortical circuits and cerebrovenular endothelium. J Neurosci. 2001;21(3):798–811.
   Web of Science ®Google Scholar
• Liu H, Sankar R, Shin DH, Mazarati AM, Wasterlain CG. Patterns of status epilepticus-induced substance P expression during development. Neuroscience. 2000;101(2):297–304.
   Web of Science ®Google Scholar
• Gerard NP, Bao L, Xiao-Ping H, Gerard C. Molecular aspects of the tachykinin receptors. Regul Pept. 1993;43(1–2):21–35.
   Google Scholar
• Attwood TK. A compendium of specific motifs for diagnosing GPCR subtypes. Trends Pharmacol Sci. 2001;22(6):162–165.
   Google Scholar
• Maggi CA. The mammalian tachykinin receptors. General Pharmacol. 1995;26(5):911–944.
   Google Scholar
• Pennefather JN, Lecci A, Candenas ML, Patak E, Pinto FM, Maggi CA. Tachykinins and tachykinin receptors: a growing family. Life Sci. 2004;74(12):1445–1463.
   PubMed Web of Science ®Google Scholar
• Ramkissoon SH, Patel HJ, Taborga M, Rameshwar P. G protein-coupled receptors in haematopoietic disruption. Expert Opin Biol Ther. 2006;6(2):109–120.
   PubMed Web of Science ®Google Scholar
• Fong TM, Anderson SA, Yu H, Huang RRC, Strader CD. Differential activation of intracellular effector by two isoforms of human neurokinin-1 receptor. Mol Pharmacol 1992;41(1):24–30.
   PubMed Web of Science ®Google Scholar
• Lai JP, Lai S, Tuluc F, et al. Differences in the length of the carboxyl terminus mediate functional properties of neurokinin-1 receptor. Proc Natl Acad Sci U SA. 2008;105(34):12605–12610.
   PubMed Web of Science ®Google Scholar
• Tuluc F, Lai JP, Kilpatrick LE, Evans DL, Douglas SD. Neurokinin 1 receptor isoforms and the control of innate immunity. Trends Immunol. 2009;30(6):271–276.
   PubMed Web of Science ®Google Scholar
• Douglas SD, Lai JP, Tuluc F, Schwartz L, Kilpatrick LE. Neurokinin-1 receptor expression and function in human macrophages and brain: Perspective on the role in HIV neuropathogenesis. Ann NY Acad Sci. 2008;1144(1):90–96.
   Google Scholar
• Grant AD, Akhtar R, Gerard NP, Brain SD. Neurokinin B induces oedema formation in mouse lung via tachykinin receptor-independent mechanisms. J Physiol. 2002;543(3):1007–1114.
   Web of Science ®Google Scholar
• Bandari PS, Qian J, Oh HS, et al. Crosstalk between neurokinin receptors is relevant to hematopoietic regulation: cloning and characterization of neurokinin-2 promoter. J Neuroimmunol. 2003;138(1–2):65–75.
   Web of Science ®Google Scholar
• Quartara L, Maggi CA.The tac hykinin NK1 receptor Part I: ligands and mechanisms of cellular activation. Neuropeptides. 1997;31(6):537–563.
   PubMed Web of Science ®Google Scholar
• Valant C, Maillet E, Bourguignon JJ, et al. Allosteric functional switch of neurokinin A-mediated signaling at the neurokinin NK2 receptor: structural exploration. J Med Chem. 2009;52(19):5999–6011.
   Web of Science ®Google Scholar
• Palanche T, Ilien B, Zoffmann S, et al. The neurokinin A receptor activates calcium and cAMP responses through distinct conformational states. J Biol Chem. 2001;276(37):34853–34861.
   Web of Science ®Google Scholar
• Williams R, Zou X, Hoyle GW. Tachykinin-1 receptor stimulates proin flammatory gene expression in lung epithelial cells through activation of NF-kappaB via a G(q)-dependent pathway. Am J Physiol Lung Cell Mol Physiol. 2007;292(2):430–437.
   PubMed Web of Science ®Google Scholar
• Krause JE, Bu JY, Takeda Y, et al. Structure, expression and second messenger-mediated regulation of the human and rat substance P receptors and their genes. Regul Pept. 1993;46(1–2):59–66.
   Google Scholar
• Janelsins BM, Mathers AR, Tkacheva OA, et al. Proinflammatory tachykinins that signal through the neurokinin 1 receptor promote survival of dendritic cells and potent cellular immunity. Blood. 2009;113(13):3017–3026.
   Web of Science ®Google Scholar
• Corcoran KE, Rameshwar P. Nuclear factor-kappaB accounts for the repressor effects of high stromal cell-derived factor-1alpha levels on Tac1 expression in nontumorigenic breast cells. Mol Cancer Res. 2007a;5(4):373–381.
   Google Scholar
• Jorgensen R, Holliday ND, Hansen JL, et al. Characterization of G-protein coupled receptor kinase interaction with the neurokinin-1 receptor using bioluminescence resonance energy transfer. Mol Pharmacol. 2008;73(2):349–358.
   Web of Science ®Google Scholar
• Luttrell LM, Lefkowitz RJ. The role of beta-arrestins in the termination and transduction of G-protein-coupled receptor signals. J Cell Sci. 2002;115(Pt 3):455–465.
   PubMed Web of Science ®Google Scholar
• Bennett VJ, Perrine SA, Simmons MA. Neurokinin-1 receptor re sensitization precedes receptor recycling. J Pharmacol Exp Ther 2005;313(3):1347–1354.
   Web of Science ®Google Scholar
• Cottrell GS, Padilla B, Pikios S, et al. Ubiquitin-dependent down-regulation of the neurokinin-1 receptor. J Biol Chem. 2006;281(38):27773–27783.
   Web of Science ®Google Scholar
• Vauquelin G, Van Liefde I. G protein-coupled receptors: a count of 1001 conformations. Fundam Clin Pharmacol. 2005;19(1):45–56.
   PubMed Web of Science ®Google Scholar
• Hastrup H, Schwartz TW. Septide and neurokinin A are high affinity ligands on the NK-1 receptor: evidence from homologous versus heterologous binding analysis. FEBS Lett. 1996;399(3):264–266.
   Web of Science ®Google Scholar
• Rameshwar P, Ganea D, Gascon P. In vitro stimulatory effect of substance P on hematopoiesis. Blood. 1993;81(2):391–398.
   PubMed Web of Science ®Google Scholar
• Rameshwar P, Gascon P. Induction of negative hematopoietic regulators by neurokinin-A in bone marrow stroma. Blood. 1996;88(1):98–106.
   Web of Science ®Google Scholar
• Simmons PJ, Levesque JP, Zannettino AC. Adhesion molecules in haemopoiesis. Baillieres Clin Haematol. 1997;10(3):485–505.
   PubMedGoogle Scholar
• Zon LI. Developmental biology of hematopoiesis. Blood. 1995;86(8):2876–2891.
   Web of Science ®Google Scholar
• Kondo M, Wagers AJ, Manz MG, et al. Biology of hematopoietic stem cells and progenitors: implications for clinical application. Annu Rev Immunol. 2003;(21):759–806.
   Google Scholar
• Martinez-Agosto JA, Mikkola HK, Hartenstein V, Banerjee U. The hematopoietic stem cell and its niche: a comparative view. Genes Dev. 2007;21(23):3044–3060.
   PubMed Web of Science ®Google Scholar
• Naveiras O, Nardi V, Wenzel PL, Hauschka PV, Fahey F, Daley GQ. Bone-marrow adipocytes as negative regulators of the haematopoietic microenvironment. Nature. 2009;460(7252):259–263.
   PubMed Web of Science ®Google Scholar
• Sugimura R, Li L. Shifting in balance between osteogenesis and adipogenesis substantially influences hematopoiesis. J Mol Cell Biol. 2010;2(2):61–62.
   Web of Science ®Google Scholar
• Bianco P, Robey PG, Simmons PJ. Mesenchymal stem cells: revisiting history, concepts, and assays. Cell Stem Cell. 2008;2(4):313–319.
   PubMed Web of Science ®Google Scholar
• Rodríguez JP, Astudillo P, Ríos S, Pino AM. Involvement of adipogenic potential of human bone marrow mesenchymal stem cells (MSCs) in osteoporosis. Curr Stem Cell Res Ther. 2008;3(3):208–218.
   Web of Science ®Google Scholar
• Corcoran KE, Trzaska KA, Fernandes H, et al. Mesenchymal stem cells in early entry of breast cancer into bone marrow. PLoS One. 2008;3(6): e2563.
   PubMed Web of Science ®Google Scholar
• Matsuoka S, Tsuji K, Hisakawa H, et al. Generation of definitive hematopoietic stem cells from murine early yolk sac and paraaortic splanchnopleures by aorta-gonad-mesonephros region-derived stromal cells. Blood. 2001;98(1):6–12.
   Web of Science ®Google Scholar
• Ogawa M. Differentiation and proliferation of hematopoietic stem cells. Blood. 1993;81(11):2844–2853.
   PubMed Web of Science ®Google Scholar
• Muller-Sieburg CE, Deryugina E. The stromal cells’ guide to the stem cell universe. Stem Cells. 1995;13(5):477–486.
   Web of Science ®Google Scholar
• Meunch MD, Schneider JG, Moore MAS. Interaction amongst colony stimulating factors, IL-1b, IL-6 and kit-ligand in the regulation of primitive murine hematopoietic cells. Exp Hematol. 1992;20(3):339–349.
   Web of Science ®Google Scholar
• Grebien F, Kerenyi MA, Kovacic B, et al. Stat5 activation enables erythropoiesis in the absence of EpoR and Jak2. Blood. 2008;111(9):4511–4522.
   PubMed Web of Science ®Google Scholar
• North TE, de Bruijn MF, Stacy T, et al. Runx1 expression marks long-term repopulating hematopoietic stem cells in the midgestation mouse embryo. Immunity. 2002;16(5):661–672.
   Web of Science ®Google Scholar
• Lapidot T, Dar A, Kollet O. How do stem cells find their way home? Blood. 2005;106(6):1901–1910.
   PubMed Web of Science ®Google Scholar
• Corcoran KE, Patel N, Rameshwar P. Stromal derived growth factor-1alpha: another mediator in neural-emerging immune system through Tac 1 expression in bone marrow stromal cells. J Immunol. 2007;178(4):2075–2082.
   Web of Science ®Google Scholar
• Tabarowski Z, Gibson-Berry K, Felten SY. Noradrenergic and peptidergic innervation of the mouse femur bone marrow. Acta Histochem. 1996;98(4):453–457.
   PubMed Web of Science ®Google Scholar
• Zhang Y, Paige CJ. T-cell developmental blockage by tachykinins antagonists and the role of hemokinin 1 in T lymphopoiesis. Blood. 2003;102(6):2165–2172.
   Web of Science ®Google Scholar
• Tsuda T, Wong D, Dolovich J, Bienenstock J, Marshall J, Denbury JA. Synergistic effects of nerve growth factor and granulocyte-macrophage colony-stimulating factor on human basophilic cell differentiation. Blood. 1991;77(5):971–979.
   Web of Science ®Google Scholar
• Tordjman R, Lepelletier Y, Lemarchandel V et al. A neuronal receptor, neuropilin-1, is essential for the initiation of the primary immune response. Nature Immunol. 2002;3(5):477–482.
   PubMed Web of Science ®Google Scholar
• Bischoff SC, Dahinden CA. Effect of nerve growth factor on the release of inflammatory mediators by mature human basophils. Blood. 1992;79(10):2662–2669.
   Web of Science ®Google Scholar
• Murthy RG, Greco SJ, Taborga M, Patel N, Rameshwar P. Tac1 regulation by RNA-binding protein and miRNA in bone marrow stroma: Implication for hematopoietic activity. Brain Behav Immun. 2008;22(4):442–450.
   Web of Science ®Google Scholar
• Corcoran KE, Malhotra A, Molina CA, Rameshwar P. Stromal-derived factor-1alpha induces a non-canonical pathway to activate the endocrine-linked Tac1 gene in non-tumorigenic breast cells. J Mol Endocrinol. 2008;40(3):113–123.
   Web of Science ®Google Scholar
• Singh D, Joshi DD, Hameed M, et al. Increased expression of preprotachykinin-I and neurokinin receptors in human breast cancer cells: implications for bone marrow metastasis. Proc Natl Acad Sci USA. 2000;97(1):388–393.
   PubMed Web of Science ®Google Scholar
• Kang HS, Trzaska KA, Corcoran K, Chang VT, Rameshwar P. Neurokinin receptors: relevance to the emerging immune system. Arch Immunol Ther Exp (Warsz). 2004;52(5):338–347.
   Web of Science ®Google Scholar
• Perez LE, Alpdogan O, Shieh JH, et al. Increased plasma levels of stromal-derived factor-1 (SDF-1/CXCL12) enhance human thrombopoiesis and mobilize human colony-forming cells (CFC) in NOD/SCID mice. Exp Hematol. 2004;32(3):300–307.
   Web of Science ®Google Scholar
• Hattori K, Heissig B, Rafii S. The regulation of hematopoietic stem cell and progenitor mobilization by chemokine SDF-1. Leuk Lymphoma. 2003;44(4):575–582.
   PubMed Web of Science ®Google Scholar
• Lapteva N, Yang AG, Sanders DE, Strube RW, Chen SY. CXCR4 knockdown by small interfering RNA abrogates breast tumor growth in vivo. Cancer Gene Ther. 2005;12(1):84–89.
   Web of Science ®Google Scholar
• Reddy BY, Greco SJ, Patel PS, Trzaska KA, Rameshwar P. RE-1-silencing transcription factor shows tumor-suppressor functions and negatively regulates the oncogenic TAC1 in breast cancer cells. Proc Natl Acad Sci U S A. 2009;106(11):4408–4413.
   Web of Science ®Google Scholar
• Rameshwar P, Ganea D, Gascon P. Induction of IL-3 and granulocyte-macrophage colony-stimulating factor by substance P in bone marrow cells is partially mediated through the release of IL-I and IL-6. J Immunol. 1994;152(8):4044–4054.
   Web of Science ®Google Scholar
• Rameshwar P, Joshi DD, Yadav P, et al. Mimicry between neurokinin-1 and fibronectin may explain the transport and stability of increased substance P-immunoreactivity in patients with bone marrow fibrosis. Blood. 2001;97(10):3025–3031.
   Web of Science ®Google Scholar
• Fras C, Kravetz P, Mody DR, Heggeness MH. Substance P-containing nerves within the human vertebral body: an immunohistochemical study of the basiverterbral nerve. Spine J. 2003;3(1):63–67.
   Google Scholar
• Goto T, Tanaka T. Tachykinins and tachykinin receptors in the bone. Microsc Res Tech. 2002;(58):91–97.
   Google Scholar
• Rameshwar P, Gascon P. Neural regulation of hematopoiesis by the tachykinins. Mol Biol Hemat. 1996;(5):463–470.
   Google Scholar
• Zhang Y, Lu L, Furlonger C, et al. Hemokinin is a hematopoietic specific tachykinin that regulates B lymphopoiesis. Nat Immunol. 2000;1(5):392–397.
   Web of Science ®Google Scholar
• Rameshwar P, Gascon P, Ganea D. Stimulation of IL-2 production in murine lymphocytes by substance P and related tachykinins. J Immunol. 1993;151(5):2484–2496.
   Web of Science ®Google Scholar
• Rameshwar P. Substance P: a regulatory neuropeptide for hematopoiesis and immune functions. Clin Immunol Immunopathol. 1997;85(2):129–133.
   Google Scholar
• Lotz M, Vaughan JH, Carson DA. Effect of neuropeptides on production of inflammatory cytokines by human monocytes. Science. 1988;241(4870):1218–1221.
   PubMed Web of Science ®Google Scholar
• Laurenzi MA, Persson MAA, Dalsgaard CJ, Haegerstrand A. The neuropeptide substance P stimulates production of interleukin I in human blood monocytes: Activated cells are preferentially influenced by the neuropeptide. Scand J Immunol 1990;31(4):529–533.
   Web of Science ®Google Scholar
• Cozens PJ, Rowe FM. Substance P is a potent inducer of TNF and IL-1 secretion by macrophages. A potent role for TNF in the pathogenesis of asthma. Immunobiology. 1987;175:7–15.
   Web of Science ®Google Scholar
• Kimball ES, Persico FJ, Vaught JL. Substance P, neurokinin A, and neurokinin B induce generation of IL-I-like activity in P388D1 cells. Possible relevance to arthritic disease. J Immunol. 1988;141(10):3564–3569.
   Web of Science ®Google Scholar
• Wagner F, Fink R, Hart R, Dancygier H. Substance P enhances interferon-Y production by human peripheral blood mononuclear cells. Regul Pept. 1987;19(5–6):355–364.
   Google Scholar
• Rameshwar P, Gascon P, Ganea D. Immunoregulatory effects of neuropeptides Stimulation of interleukin-2 production by Substance P. J Neuroimmunol. 1992;37(1–2):65–74.
   Web of Science ®Google Scholar
• Ansel JC, Brown JR, Payan DG, Brown MA. Substance P selectively activates TNF-a gene expression in murine mast cells. J Immunol. 1993;150(10):4478–4485.
   Web of Science ®Google Scholar
• Rameshwar P, Gascon P. Substance P (SP) mediates production of stem cell factor and interleukin-1 in bone marrow stroma: Potential autoregulatory role for these cytokines in SP receptor expression and induction. Blood. 1995;86(2):482–490.
   PubMed Web of Science ®Google Scholar
• Vishalakumar S, Patel H, Moharita AL, Harrison JS, Rameshwar P. The anti-proliferative effect of neurokinin-A on hematopoietic progenitor cells is partly mediated by p53 activating the 5 ’ flanking region of neurokinin-2 receptor. Cell Signal. 2006;18(4):422–432.
   Web of Science ®Google Scholar
• Ricardo M, Trzaska KA, Rameshwar P. Neurokinin-A inhibits cell cycle activators in K562 cells and activates Smad 4 through a non-canonical pathway: a novel method in neural-hematopoietic axis. J Neuroimmunol. 2008;204(1–2):85–91.
   Web of Science ®Google Scholar
• Bandari PS, Qian J, Yehia G, et al. Differences in the expression of neurokinin receptor in neural and bone marrow mesenchymal cells: implications for neuronal expansion from bone marrow cells. Neuropeptides. 2001;36(1):13–21.
   Web of Science ®Google Scholar
• Simeonidis S, Castagliuolo I, Pan A, et al. Regulation of the NK-1 receptor gene expression in human macrophage cells via an NF-kB site on its promoter. Proc Natl Acad Sci US A. 2003;100(5):2957–2962.
   Web of Science ®Google Scholar
• Vazquez-Prado J, Casas-Gonzalez P, Garcia-Sainz JA. G protein-c oupled receptor cross-talk: pivotal roles of protein phosphorylation and protein-protein interactions. Cell Signal. 2003;15(6):549–557.
   Web of Science ®Google Scholar
• Yoshikawa T, Kanazawa H. Functional crosstalk between ß2-adrenoreceptor and muscarinic acetylcholine receptor: implications for gene-gene interactions and bronchodilatory responses in patients with asthma and COPD. Curr Pharmacogen Pers Med. 2008;6(4):302–319.
   Google Scholar
• Sun J, Ramnath RD, Tamizhselvi R, Bhatia M. Role of protein kinase C and phosphoinositide 3-kinase-Akt in substance P-induced proinflammatory pathways in mouse macrophages. FASEB J. 2009;23(4):997–1010.
   PubMed Web of Science ®Google Scholar
• Sassone-Corsi P. Transcription factors responsive to cAMP Annu Rev Cell Dev Biol. 1995;(11):355–377.
   Google Scholar
• Barnes PJ. Receptor heterodimerization: a new level of cross-talk. J Clin Invest. 2006;116(5):1210–1212.
   PubMed Web of Science ®Google Scholar
• Greco SJ, Smirnov SV, Murthy RG, Rameshwar P. Synergy between the RE-1 silencer of transcription and NFkappaB in the repression of the neurotransmitter gene TAC1 in human mesenchymal stem cells. J Biol Chem. 2007;282(41):30039–30050.
   Web of Science ®Google Scholar
• Rameshwar P Gascon P Bandari PS, Joshi DD, Fernandes A, Dang A. Structural similarity between the bone marrow extracellular matrix protein and neurokinin 1 could be the limiting factor in the hematopoietic effects of substance P. Can J Pharmacol Physiol. 2002;80(5):475–481.
   Web of Science ®Google Scholar