Panax ginseng induces anterograde transport of pigment organelles in Xenopus melanophores

Eriksson, Thérèse; Svensson, Samuel; Lundström, Ingemar; Persson, Karin; Andersson, Tobias; Andersson, Rolf G. G.

doi:10.1016/j.jep.2008.05.024

Cited by 3 publications

(3 citation statements)

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“…In adult animals, coat color is dependent on melanin produced by melanocytes at the base of hair follicles. In studying signal transduction of hair follicle, researchers have mainly focused on the melanocortin receptor 1/protein kinase A (MC1R/PKA) signaling pathways (Våge et al, 2014; Dorshorst et al, 2015), Wnt/β-catenin signaling pathways (Enshell-Seijffersa et al, 2010), mitogen-activated protein kinase signaling pathways (Eriksson et al, 2008; Feng et al, 2014), and other signaling pathways, which are involved the growth and development stages of hair follicles and control the proliferation and differentiation of the hair follicle epithelial cells (Tian and Fan, 2006). Recently, some subunits of G protein-couple signaling pathway have been found to regulate and control coat color formation by mutation (Van Raamsdonk et al, 2004; 2009).…”

Section: Introductionmentioning

confidence: 99%

Expression and Distribution of the Guanine Nucleotide-binding Protein Subunit Alpha-s in Mice Skin Tissues and Its Association with White and Black Coat Colors

Yin

Zhao

Wang

et al. 2016

Asian Australas. J. Anim. Sci

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Guanine nucleotide-binding protein subunit alpha-s (Gnαs) is a small subunit of the G protein-couple signaling pathway, which is involved in the formation of coat color. The expression level and distribution of Gnαs were detected by quantitative real-time-polymerase chain reaction (qPCR), western blot, and immunohistochemistry to investigate the underlying mechanisms of coat color in white and black skin tissues of mice. qPCR and western blot results suggested that Gnαs was expressed at significantly higher levels in black mice compared with that of white mice, and transcripts and protein possessed the same expression in both colors. Immunohistochemistry demonstrated Gnαs staining in the root sheath and dermal papilla in hair follicle of mice skins. The results indicated that the Gnαs gene was expressed in both white and black skin tissues, and the expression level of Gnαs in the two types of color was different. Therefore, Gnαs may be involved in the coat color formation in mice.

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Section: Introductionmentioning

confidence: 99%

Expression and Distribution of the Guanine Nucleotide-binding Protein Subunit Alpha-s in Mice Skin Tissues and Its Association with White and Black Coat Colors

Yin

Zhao

Wang

et al. 2016

Asian Australas. J. Anim. Sci

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“…Ginsenosides have been used and reported as the representative ingredients in most ginseng-related biochemical studies [1]. Since the content of ginsenoside within ginseng is low, ginsenoside isolation from ginseng is complicated, and as a result pure ginsenosides are expensive, thus we and others have used crude ginseng total saponin fraction (CGSF) that has been prepared from butanol extraction of ginseng root to explain various in vitro and in vivo physiological or pharmacological actions of ginseng [4][5][6][7][8][9][10].…”

Section: Introductionmentioning

confidence: 99%

Novel Glycolipoproteins from Ginseng

Pyo¹,

Choi²,

Hwang³

et al. 2011

Journal of Ginseng Research

116

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Ginseng has been used as a general tonic agent to invigorate human body. In the present study, we isolated novel glycolipoproteins from ginseng that activate Ca 2+ -activated Cl -channel (CaCC) in Xenopus oocytes and transiently increase intracellular free Ca 2+ concentration ([Ca 2+ ] i ) in mouse Ehrlich ascites tumor cells. We named the active ingredients as gintonin. Gintonin exists in at least six different forms. The native molecular weight of gintonin is about 67 kDa but its apparent molecular weight is about 13 kDa, indicating that gintonin might be a pentamer. Gintonin is rich in hydrophobic amino acids. Its main carbohydrates are glucose and glucosamine. Its lipid components are linoleic, palmitic, oleic, and stearic acids. Gintonin actions were blocked by U73122, a phospholipase C inhibitor, 2-aminoethxydiphenyl borate, an inositol 1,4,5-trisphosphate receptor antagonist, or bis (o-aminophenoxy) ethane-N,N,N0,N0-tetracetic acid acetoxymethyl ester, a membrane permeable Ca 2+ chelator. In the present study, we for the fi rst time isolated novel gintonin and showed the signaling pathways on gintonin-mediated CaCC activations and transient increase of [Ca 2+ ] i . Since [Ca 2+ ] i as a second messenger plays a pivotal role in the regulation of diverse Ca 2+ -dependent intracellular signal pathways, gintonin-mediated regulations of [Ca 2+ ] i might contribute to biological actions of ginseng.

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“…Fish and amphibians 46 make use of the prototypical cAMP-PKA-dependent regulatory pathway to consciously 47 control the deployment of these three different types of motors ( Fig. 1A and B) (8)(9)(10)(11). 48 When external cues lead to an increase of intracellular PKA activity, melanosomes 49 disperse throughout the cell on the actin network ( Fig.…”

Section: Introductionmentioning

confidence: 99%

How to navigate the myosin-V motor through the actin network

Spieler¹,

Oberhofer²,

Zimmermann

et al. 2020

Preprint

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1Myosin-V (MyoV) is a ubiquitous motor protein that transports an astonishingly diverse 2 set of cargos on the actin network in eukaryotes. Phosphorylation-dependent 3 processes often regulate MyoV-mediated cargo transport, molecular details of which 4 remain largely unknown. We previously showed that phosphorylation regulates MyoV's 5 switching from microtubules onto actin filaments, not its motor activity. Regulation of 6 switching at reconstituted microtubule-actin-crossings in fact sufficed to recapitulate 7 the MyoVa-driven redistribution of pigment-organelles in amphibian melanophores. 8 However, in those cells, MyoVa also encounter many actin-actin crossings. Here, we 9 show that isolated MyoVa motors switch with equal probabilities at reconstituted actin-10 actin-crossings. Under the control of its adaptor-protein melanophilin (Mlph), however, 11 the motor differentiates between the actin filaments at crossing points in a 12 phosphorylation-regulated manner. Whereas phosphorylation of Mlph forced about 13 ~2/3 of MyoVa to ignore the intersections, dephosphorylation completely reversed this 14 behavior and forced ~2/3 to switch. We show that the filament-binding domain (FBD) 15 of Mlph controls this switching behavior. This property evolved in amphibians, but not 16 in the early vertebrate zebrafish. By protein engineering, we demonstrate that changes 17 of a few residues are sufficient to impart actin-binding capability onto the zebrafish 18 Mlph. We thus unmask the molecular beginnings of dual filament binding in Mlph that 19 allow it to control the switching behavior of MyoVa at cytoskeletal crossings. We 20 therefore propose a direct link between intracellular phosphorylation activity and the 21 adaptor-protein, not to regulate MyoVa activity, but to navigate the motor through the 22 entire cytoskeletal maze for correct positioning of cargo. 23Significance statement 25 In virtually all eukaryotic cells, numerous myosin motors have to navigate through an 26 elaborate actin network for timely transport of intracellular cargo. Here, we unmask an 27 unintuitive regulation of the myosin-Va motor that is involved in pigment organelle 28 transport. We demonstrate that myosin-Va differentiates between the same actin 29 filaments and displays regulated switching at reconstituted actin-actin crossings, an 30 unexpected behavior that has been predicted from previous theoretical work. We trace 31 this regulation back to the adaptor protein of the myosin-Va motor and show that this 32 regulation was present in amphibian but had not evolved in the early vertebrate 33 zebrafish. Notably, we demonstrate that the evolution of actin-binding capability is 34 achieved by changing a few residues in the adaptor protein.

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Panax ginseng induces anterograde transport of pigment organelles in Xenopus melanophores

Cited by 3 publications

References 40 publications

Expression and Distribution of the Guanine Nucleotide-binding Protein Subunit Alpha-s in Mice Skin Tissues and Its Association with White and Black Coat Colors

Expression and Distribution of the Guanine Nucleotide-binding Protein Subunit Alpha-s in Mice Skin Tissues and Its Association with White and Black Coat Colors

Novel Glycolipoproteins from Ginseng

How to navigate the myosin-V motor through the actin network

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