메뉴 건너뛰기




Volumn 19, Issue 1, 2014, Pages 59-71

The biology of zinc transport in mammary epithelial cells: Implications for mammary gland development, lactation, and involution

Author keywords

Involution; Lactation; Mammary development; TRPML1; Zinc; Zinc transporter

Indexed keywords

GELATINASE A; GELATINASE B; INTERSTITIAL COLLAGENASE; MATRIX METALLOPROTEINASE; MITOGEN ACTIVATED PROTEIN KINASE; TISSUE INHIBITOR OF METALLOPROTEINASE; TRANSCRIPTION FACTOR; TRANSIENT RECEPTOR POTENTIAL CHANNEL; TRANSIENT RECEPTOR POTENTIAL MUCOLIPIN 1; UNCLASSIFIED DRUG; ZINC; ZINC FINGER PROTEIN; ZINC TRANSPORTER;

EID: 84896493072     PISSN: 10833021     EISSN: 15737039     Source Type: Journal    
DOI: 10.1007/s10911-013-9314-4     Document Type: Article
Times cited : (43)

References (115)
  • 1
    • 33747040785 scopus 로고    scopus 로고
    • Hormonal and local control of mammary branching morphogenesis
    • 1:CAS:528:DC%2BD28Xpsl2jurc%3D 2580831 16916375
    • Sternlicht MD, Kouros-Mehr H, Lu P, et al. Hormonal and local control of mammary branching morphogenesis. Differentiation. 2006;74(7):365-81.
    • (2006) Differentiation , vol.74 , Issue.7 , pp. 365-381
    • Sternlicht, M.D.1    Kouros-Mehr, H.2    Lu, P.3
  • 2
    • 0027394031 scopus 로고
    • The biochemical basis of zinc physiology
    • 1:CAS:528:DyaK3sXhvVyhtrY%3D 8419966
    • Vallee BL, Falchuk KH. The biochemical basis of zinc physiology. Physiol Rev. 1993;73(1):79-118.
    • (1993) Physiol Rev , vol.73 , Issue.1 , pp. 79-118
    • Vallee, B.L.1    Falchuk, K.H.2
  • 3
    • 0024472714 scopus 로고
    • Specificity and timing of the Zn2+ requirement for DNA synthesis by 3 T3 cells
    • 1:CAS:528:DyaK3cXhvFaitA%3D%3D 2806401
    • Chesters JK, Petrie L, Vint H. Specificity and timing of the Zn2+ requirement for DNA synthesis by 3 T3 cells. Exp Cell Res. 1989;184(2):499-508.
    • (1989) Exp Cell Res , vol.184 , Issue.2 , pp. 499-508
    • Chesters, J.K.1    Petrie, L.2    Vint, H.3
  • 4
    • 0025924809 scopus 로고
    • Nature of the Zn2+ requirement for DNA synthesis by 3 T3 cells
    • 1:CAS:528:DyaK3MXpvFSksw%3D%3D 1988298
    • Chesters JK, Boyne R. Nature of the Zn2+ requirement for DNA synthesis by 3 T3 cells. Exp Cell Res. 1991;192(2):631-4.
    • (1991) Exp Cell Res , vol.192 , Issue.2 , pp. 631-634
    • Chesters, J.K.1    Boyne, R.2
  • 5
    • 44349145050 scopus 로고    scopus 로고
    • Down regulation by a low-zinc diet in gene expression of rat prostatic thymidylate synthase and thymidine kinase
    • Ishikawa Y, Kudo H, Suzuki S, et al. Down regulation by a low-zinc diet in gene expression of rat prostatic thymidylate synthase and thymidine kinase. Nutr Metab (Lond). 2008;5:12.
    • (2008) Nutr Metab (Lond) , vol.5 , pp. 12
    • Ishikawa, Y.1    Kudo, H.2    Suzuki, S.3
  • 6
    • 0032907983 scopus 로고    scopus 로고
    • Inhibition of insulin-like growth factor-I mitogenic action by zinc chelation is associated with a decreased mitogen-activated protein kinase activation in RAT-1 fibroblasts
    • 1:CAS:528:DyaK1MXis1aru78%3D 10338149
    • Lefebvre D, Boney CM, Ketelslegers JM, et al. Inhibition of insulin-like growth factor-I mitogenic action by zinc chelation is associated with a decreased mitogen-activated protein kinase activation in RAT-1 fibroblasts. FEBS Lett. 1999;449(2-3):284-8.
    • (1999) FEBS Lett , vol.449 , Issue.2-3 , pp. 284-288
    • Lefebvre, D.1    Boney, C.M.2    Ketelslegers, J.M.3
  • 7
    • 43849104102 scopus 로고    scopus 로고
    • Roles of zinc and zinc signaling in immunity: Zinc as an intracellular signaling molecule
    • 1:CAS:528:DC%2BD1cXhtVajsrfF 18501770
    • Hirano T, Murakami M, Fukada T, et al. Roles of zinc and zinc signaling in immunity: zinc as an intracellular signaling molecule. Adv Immunol. 2008;97:149-76.
    • (2008) Adv Immunol , vol.97 , pp. 149-176
    • Hirano, T.1    Murakami, M.2    Fukada, T.3
  • 8
    • 85027956266 scopus 로고    scopus 로고
    • Cell apoptosis induced by zinc deficiency in osteoblastic MC3T3-E1 cells via a mitochondrial-mediated pathway
    • 1:CAS:528:DC%2BC3MXhs1Oqsr3L 21997737
    • Guo B, Yang M, Liang D, et al. Cell apoptosis induced by zinc deficiency in osteoblastic MC3T3-E1 cells via a mitochondrial-mediated pathway. Mol Cell Biochem. 2012;361(1-2):209-16.
    • (2012) Mol Cell Biochem , vol.361 , Issue.1-2 , pp. 209-216
    • Guo, B.1    Yang, M.2    Liang, D.3
  • 9
    • 0033369167 scopus 로고    scopus 로고
    • Cloning, expression, and vesicular localization of zinc transporter Dri 27/ZnT4 in intestinal tissue and cells
    • 1:CAS:528:DC%2BD3cXhs1yhuw%3D%3D 10600821
    • Murgia C, Vespignani I, Cerase J, et al. Cloning, expression, and vesicular localization of zinc transporter Dri 27/ZnT4 in intestinal tissue and cells. Am J Physiol. 1999;277(6 Pt 1):G1231-9.
    • (1999) Am J Physiol , vol.277 , Issue.6 PART 1 , pp. 1231-1239
    • Murgia, C.1    Vespignani, I.2    Cerase, J.3
  • 10
    • 84875129764 scopus 로고    scopus 로고
    • The SLC39 family of zinc transporters
    • 1:CAS:528:DC%2BC3sXksVyku7Y%3D 23506894
    • Jeong J, Eide DJ. The SLC39 family of zinc transporters. Mol Aspects Med. 2013;34(2-3):612-9.
    • (2013) Mol Aspects Med , vol.34 , Issue.2-3 , pp. 612-619
    • Jeong, J.1    Eide, D.J.2
  • 11
    • 0034051667 scopus 로고    scopus 로고
    • Functional expression of the human hZIP2 zinc transporter
    • 1:CAS:528:DC%2BD3cXhsFKktr0%3D 10681536
    • Gaither LA, Eide DJ. Functional expression of the human hZIP2 zinc transporter. J Biol Chem. 2000;275(8):5560-4.
    • (2000) J Biol Chem , vol.275 , Issue.8 , pp. 5560-5564
    • Gaither, L.A.1    Eide, D.J.2
  • 12
    • 0035933885 scopus 로고    scopus 로고
    • The human ZIP1 transporter mediates zinc uptake in human K562 erythroleukemia cells
    • 1:CAS:528:DC%2BD3MXkvVanurY%3D 11301334
    • Gaither LA, Eide DJ. The human ZIP1 transporter mediates zinc uptake in human K562 erythroleukemia cells. J Biol Chem. 2001;276(25):22258-64.
    • (2001) J Biol Chem , vol.276 , Issue.25 , pp. 22258-22264
    • Gaither, L.A.1    Eide, D.J.2
  • 13
    • 67650540770 scopus 로고    scopus 로고
    • Identification of the Zn2+ binding site and mode of operation of a mammalian Zn2+ transporter
    • 1:CAS:528:DC%2BD1MXnsVWksLw%3D 2719407 19366695
    • Ohana E, Hoch E, Keasar C, et al. Identification of the Zn2+ binding site and mode of operation of a mammalian Zn2+ transporter. J Biol Chem. 2009;284(26):17677-86.
    • (2009) J Biol Chem , vol.284 , Issue.26 , pp. 17677-17686
    • Ohana, E.1    Hoch, E.2    Keasar, C.3
  • 14
    • 84896488355 scopus 로고    scopus 로고
    • Contribution of calcium-conducting channels to the transport of zinc ions
    • Bouron A, Oberwinkler J. Contribution of calcium-conducting channels to the transport of zinc ions. Pflugers Arch 2013.
    • (2013) Pflugers Arch
    • Bouron, A.1    Oberwinkler, J.2
  • 15
    • 79955052958 scopus 로고    scopus 로고
    • Role of TRP channels in the regulation of the endosomal pathway
    • 1:CAS:528:DC%2BC3MXjsVKjtrg%3D
    • Abe K, Puertollano R. Role of TRP channels in the regulation of the endosomal pathway. Physiology (Bethesda). 2011;26(1):14-22.
    • (2011) Physiology (Bethesda) , vol.26 , Issue.1 , pp. 14-22
    • Abe, K.1    Puertollano, R.2
  • 16
    • 33751223540 scopus 로고    scopus 로고
    • Zinc-buffering capacity of a eukaryotic cell at physiological pZn
    • 1:CAS:528:DC%2BD28Xht1entLnE 16924557
    • Krezel A, Maret W. Zinc-buffering capacity of a eukaryotic cell at physiological pZn. J Biol Inorg Chem. 2006;11(8):1049-62.
    • (2006) J Biol Inorg Chem , vol.11 , Issue.8 , pp. 1049-1062
    • Krezel, A.1    Maret, W.2
  • 17
    • 77952566927 scopus 로고    scopus 로고
    • Cytosolic zinc buffering and muffling: Their role in intracellular zinc homeostasis
    • 1:CAS:528:DC%2BC3cXnt1Kitr4%3D 21069178
    • Colvin RA, Holmes WR, Fontaine CP, et al. Cytosolic zinc buffering and muffling: their role in intracellular zinc homeostasis. Metallomics. 2010;2(5):306-17.
    • (2010) Metallomics , vol.2 , Issue.5 , pp. 306-317
    • Colvin, R.A.1    Holmes, W.R.2    Fontaine, C.P.3
  • 18
    • 42049101604 scopus 로고    scopus 로고
    • Metallothionein redox biology in the cytoprotective and cytotoxic functions of zinc
    • 1:CAS:528:DC%2BD1cXkvFCqtbo%3D 18171607
    • Maret W. Metallothionein redox biology in the cytoprotective and cytotoxic functions of zinc. Exp Gerontol. 2008;43(5):363-9.
    • (2008) Exp Gerontol , vol.43 , Issue.5 , pp. 363-369
    • Maret, W.1
  • 19
    • 84861113372 scopus 로고    scopus 로고
    • Marginal maternal zinc deficiency in lactating mice reduces secretory capacity and alters milk composition
    • 1:CAS:528:DC%2BC38XkvFals7o%3D 3301987 22357740
    • Dempsey C, McCormick NH, Croxford TP, et al. Marginal maternal zinc deficiency in lactating mice reduces secretory capacity and alters milk composition. J Nutr. 2012;142(4):655-60.
    • (2012) J Nutr , vol.142 , Issue.4 , pp. 655-660
    • Dempsey, C.1    McCormick, N.H.2    Croxford, T.P.3
  • 20
    • 72149086674 scopus 로고    scopus 로고
    • Zip6-attenuation promotes epithelial-to-mesenchymal transition in ductal breast tumor (T47D) cells
    • 1:CAS:528:DC%2BD1MXhs1WgtbvJ 19852955
    • Lopez V, Kelleher SL. Zip6-attenuation promotes epithelial-to-mesenchymal transition in ductal breast tumor (T47D) cells. Exp Cell Res. 2010;316(3):366-75.
    • (2010) Exp Cell Res , vol.316 , Issue.3 , pp. 366-375
    • Lopez, V.1    Kelleher, S.L.2
  • 21
    • 84884804010 scopus 로고    scopus 로고
    • A Mechanism for Epithelial-Mesenchymal Transition and Anoikis Resistance in Breast Cancer Triggered by Zinc Channel ZIP6 and Signal Transducer and Activator of Transcription 3 (STAT3)
    • Hogstrand C, Kille P, Ackland ML, et al. A Mechanism for Epithelial-Mesenchymal Transition and Anoikis Resistance in Breast Cancer Triggered by Zinc Channel ZIP6 and Signal Transducer and Activator of Transcription 3 (STAT3). Biochem J 2013.
    • (2013) Biochem J
    • Hogstrand, C.1    Kille, P.2    Ackland, M.L.3
  • 22
    • 84855724443 scopus 로고    scopus 로고
    • Mapping the zinc-transporting system in mammary cells: Molecular analysis reveals a phenotype-dependent zinc-transporting network during lactation
    • 1:CAS:528:DC%2BC38XlvVGnsA%3D%3D 3207005 21702047
    • Kelleher SL, Velasquez V, Croxford TP, et al. Mapping the zinc-transporting system in mammary cells: Molecular analysis reveals a phenotype-dependent zinc-transporting network during lactation. J Cell Physiol. 2012;227(4):1761-70.
    • (2012) J Cell Physiol , vol.227 , Issue.4 , pp. 1761-1770
    • Kelleher, S.L.1    Velasquez, V.2    Croxford, T.P.3
  • 23
    • 0030724951 scopus 로고    scopus 로고
    • A novel gene involved in zinc transport is deficient in the lethal milk mouse
    • 1:CAS:528:DyaK2sXntVSnsbY%3D 9354792
    • Huang L, Gitschier J. A novel gene involved in zinc transport is deficient in the lethal milk mouse. Nat Genet. 1997;17(3):292-7.
    • (1997) Nat Genet , vol.17 , Issue.3 , pp. 292-297
    • Huang, L.1    Gitschier, J.2
  • 24
    • 33845969541 scopus 로고    scopus 로고
    • Identification of a mutation in SLC30A2 (ZnT-2) in women with low milk zinc concentration that results in transient neonatal zinc deficiency
    • 1:CAS:528:DC%2BD28Xhtlagsb%2FK 17065149
    • Chowanadisai W, Lönnerdal B, Kelleher SL. Identification of a mutation in SLC30A2 (ZnT-2) in women with low milk zinc concentration that results in transient neonatal zinc deficiency. J Biol Chem. 2006;281(51):39699- 707.
    • (2006) J Biol Chem , vol.281 , Issue.51 , pp. 39699-39707
    • Chowanadisai, W.1    Lönnerdal, B.2    Kelleher, S.L.3
  • 25
    • 33845316798 scopus 로고    scopus 로고
    • Secretion and fluid transport mechanisms in the mammary gland: Comparisons with the exocrine pancreas and the salivary gland
    • 17136613
    • McManaman JL, Reyland ME, Thrower EC. Secretion and fluid transport mechanisms in the mammary gland: comparisons with the exocrine pancreas and the salivary gland. J Mammary Gland Biol Neoplasia. 2006;11(3-4):249-68.
    • (2006) J Mammary Gland Biol Neoplasia , vol.11 , Issue.3-4 , pp. 249-268
    • McManaman, J.L.1    Reyland, M.E.2    Thrower, E.C.3
  • 26
    • 0027408422 scopus 로고
    • Transport of casein submicelles and formation of secretion granules in the Golgi apparatus of epithelial cells of the lactating mammary gland of the rat
    • 1:CAS:528:DyaK3sXhvVygtL0%3D 8430906
    • Clermont Y, Xia L, Rambourg A, et al. Transport of casein submicelles and formation of secretion granules in the Golgi apparatus of epithelial cells of the lactating mammary gland of the rat. Anat Rec. 1993;235(3):363-73.
    • (1993) Anat Rec , vol.235 , Issue.3 , pp. 363-373
    • Clermont, Y.1    Xia, L.2    Rambourg, A.3
  • 27
    • 0020035325 scopus 로고
    • Metabolic energy and cytoskeletal requirements for synthesis and secretion by acini from rat mammary gland-II. Intracellular transport and secretion of protein and lactose
    • 1:CAS:528:DyaL38XitFCru74%3D 7067894
    • Smith JJ, Nickerson SC, Keenan TW. Metabolic energy and cytoskeletal requirements for synthesis and secretion by acini from rat mammary gland-II. Intracellular transport and secretion of protein and lactose. Int J Biochem. 1982;14(2):99-109.
    • (1982) Int J Biochem , vol.14 , Issue.2 , pp. 99-109
    • Smith, J.J.1    Nickerson, S.C.2    Keenan, T.W.3
  • 28
    • 79952362077 scopus 로고    scopus 로고
    • Characterisation of the potential SNARE proteins relevant to milk product release by mouse mammary epithelial cells
    • 1:CAS:528:DC%2BC3MXjtFersbk%3D 21354649
    • Chat S, Layani S, Mahaut C, et al. Characterisation of the potential SNARE proteins relevant to milk product release by mouse mammary epithelial cells. Eur J Cell Biol. 2011;90(5):401-13.
    • (2011) Eur J Cell Biol , vol.90 , Issue.5 , pp. 401-413
    • Chat, S.1    Layani, S.2    Mahaut, C.3
  • 29
    • 70450227327 scopus 로고    scopus 로고
    • Mammary gland secretion: Hormonal coordination of endocytosis and exocytosis
    • 1:CAS:528:DC%2BD1MXhs1Sjt7%2FN 22443558
    • Truchet S, Ollivier-Bousquet M. Mammary gland secretion: hormonal coordination of endocytosis and exocytosis. Animal. 2009;3(12):1733-42.
    • (2009) Animal , vol.3 , Issue.12 , pp. 1733-1742
    • Truchet, S.1    Ollivier-Bousquet, M.2
  • 30
    • 58149277429 scopus 로고    scopus 로고
    • Calcium transport by mammary secretory cells: Mechanisms underlying transepithelial movement
    • 1:CAS:528:DC%2BD1cXhtlOgsLvO 18458827
    • Shennan DB. Calcium transport by mammary secretory cells: mechanisms underlying transepithelial movement. Cell Mol Biol Lett. 2008;13(4):514-25.
    • (2008) Cell Mol Biol Lett , vol.13 , Issue.4 , pp. 514-525
    • Shennan, D.B.1
  • 31
    • 0242661897 scopus 로고    scopus 로고
    • Zn transporter levels and localization change throughout lactation in rat mammary gland and are regulated by Zn in mammary cells
    • 1:CAS:528:DC%2BD3sXovFKhu7g%3D 14608047
    • Kelleher SL, Lonnerdal B. Zn transporter levels and localization change throughout lactation in rat mammary gland and are regulated by Zn in mammary cells. J Nutr. 2003;133(11):3378-85.
    • (2003) J Nutr , vol.133 , Issue.11 , pp. 3378-3385
    • Kelleher, S.L.1    Lonnerdal, B.2
  • 32
    • 17644396710 scopus 로고    scopus 로고
    • Zip3 plays a major role in zinc uptake into mammary epithelial cells and is regulated by prolactin
    • 1:CAS:528:DC%2BD2MXktlSgtbo%3D 15634741
    • Kelleher SL, Lonnerdal B. Zip3 plays a major role in zinc uptake into mammary epithelial cells and is regulated by prolactin. Am J Physiol Cell Physiol. 2005;288(5):C1042-7.
    • (2005) Am J Physiol Cell Physiol , vol.288 , Issue.5 , pp. 1042-1047
    • Kelleher, S.L.1    Lonnerdal, B.2
  • 33
    • 68849093297 scopus 로고    scopus 로고
    • Prolactin regulates ZNT2 expression through the JAK2/STAT5 signaling pathway in mammary cells
    • 1:CAS:528:DC%2BD1MXhtVahsbjM 2724096 19494234
    • Qian L, Lopez V, Seo YA, et al. Prolactin regulates ZNT2 expression through the JAK2/STAT5 signaling pathway in mammary cells. Am J Physiol Cell Physiol. 2009;297(2):C369-77.
    • (2009) Am J Physiol Cell Physiol , vol.297 , Issue.2 , pp. 369-377
    • Qian, L.1    Lopez, V.2    Seo, Y.A.3
  • 34
    • 84864523128 scopus 로고    scopus 로고
    • ZnT4 provides zinc to zinc-dependent proteins in the trans-Golgi network critical for cell function and Zn export in mammary epithelial cells
    • 1:CAS:528:DC%2BC38XhtlSlu7zP 3423030 22621784
    • McCormick NH, Kelleher SL. ZnT4 provides zinc to zinc-dependent proteins in the trans-Golgi network critical for cell function and Zn export in mammary epithelial cells. Am J Physiol Cell Physiol. 2012;303(3):C291-7.
    • (2012) Am J Physiol Cell Physiol , vol.303 , Issue.3 , pp. 291-297
    • McCormick, N.H.1    Kelleher, S.L.2
  • 35
    • 84865445532 scopus 로고    scopus 로고
    • A dominant negative heterozygous G87R mutation in the zinc transporter, ZnT-2 (SLC30A2), results in transient neonatal zinc deficiency
    • 1:CAS:528:DC%2BC38Xht1Cgtr7L 3436150 22733820
    • Lasry I, Seo YA, Ityel H, et al. A dominant negative heterozygous G87R mutation in the zinc transporter, ZnT-2 (SLC30A2), results in transient neonatal zinc deficiency. J Biol Chem. 2012;287(35):29348-61.
    • (2012) J Biol Chem , vol.287 , Issue.35 , pp. 29348-29361
    • Lasry, I.1    Seo, Y.A.2    Ityel, H.3
  • 36
    • 12844265345 scopus 로고    scopus 로고
    • Zinc transporters, ZnT5 and ZnT7, are required for the activation of alkaline phosphatases, zinc-requiring enzymes that are glycosylphosphatidylinositol-anchored to the cytoplasmic membrane
    • 1:CAS:528:DC%2BD2cXhtFGgu7fJ 15525635
    • Suzuki T, Ishihara K, Migaki H, et al. Zinc transporters, ZnT5 and ZnT7, are required for the activation of alkaline phosphatases, zinc-requiring enzymes that are glycosylphosphatidylinositol-anchored to the cytoplasmic membrane. J Biol Chem. 2005;280(1):637-43.
    • (2005) J Biol Chem , vol.280 , Issue.1 , pp. 637-643
    • Suzuki, T.1    Ishihara, K.2    Migaki, H.3
  • 37
    • 84869205439 scopus 로고    scopus 로고
    • 2+ in multiple cellular locations
    • 1:CAS:528:DC%2BC38XhvVShs7jE 3500285 23173058
    • 2+ in multiple cellular locations. PLoS ONE. 2012;7(11):e49371.
    • (2012) PLoS ONE , vol.7 , Issue.11 , pp. 49371
    • Miranda, J.G.1    Weaver, A.L.2    Qin, Y.3
  • 39
    • 84867812919 scopus 로고    scopus 로고
    • New sensors for quantitative measurement of mitochondrial Zn(2+)
    • 1:CAS:528:DC%2BC38XhtFWiu7vP 3477250 22850482
    • Park JG, Qin Y, Galati DF, et al. New sensors for quantitative measurement of mitochondrial Zn(2+). ACS Chem Biol. 2012;7(10):1636-40.
    • (2012) ACS Chem Biol , vol.7 , Issue.10 , pp. 1636-1640
    • Park, J.G.1    Qin, Y.2    Galati, D.F.3
  • 40
    • 79956297378 scopus 로고    scopus 로고
    • Measuring steady-state and dynamic endoplasmic reticulum and Golgi Zn2+ with genetically encoded sensors
    • 1:CAS:528:DC%2BC3MXmtFSrsrg%3D 3088641 21502528
    • Qin Y, Dittmer PJ, Park JG, et al. Measuring steady-state and dynamic endoplasmic reticulum and Golgi Zn2+ with genetically encoded sensors. Proc Natl Acad Sci U S A. 2011;108(18):7351-6.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , Issue.18 , pp. 7351-7356
    • Qin, Y.1    Dittmer, P.J.2    Park, J.G.3
  • 41
    • 56749177293 scopus 로고    scopus 로고
    • Organelle-specific zinc detection using zinpyr-labeled fusion proteins in live cells
    • 1:CAS:528:DC%2BD1cXhtlWqurvJ 2645946 18973293
    • Tomat E, Nolan EM, Jaworski J, et al. Organelle-specific zinc detection using zinpyr-labeled fusion proteins in live cells. J Am Chem Soc. 2008;130(47):15776-7.
    • (2008) J Am Chem Soc , vol.130 , Issue.47 , pp. 15776-15777
    • Tomat, E.1    Nolan, E.M.2    Jaworski, J.3
  • 42
    • 79957660884 scopus 로고    scopus 로고
    • A histidine-rich motif mediates mitochondrial localization of ZnT2 to modulate mitochondrial function
    • 1:CAS:528:DC%2BC3MXot1Cgu78%3D 3118624 21289295
    • Seo YA, Lopez V, Kelleher SL. A histidine-rich motif mediates mitochondrial localization of ZnT2 to modulate mitochondrial function. Am J Physiol Cell Physiol. 2011;300(6):C1479-89.
    • (2011) Am J Physiol Cell Physiol , vol.300 , Issue.6 , pp. 1479-1489
    • Seo, Y.A.1    Lopez, V.2    Kelleher, S.L.3
  • 43
    • 0029866646 scopus 로고    scopus 로고
    • The galvanization of biology: A growing appreciation for the roles of zinc
    • 1:CAS:528:DyaK28Xht1GksLk%3D 8599083
    • Berg JM, Shi Y. The galvanization of biology: a growing appreciation for the roles of zinc. Science. 1996;271(5252):1081-5.
    • (1996) Science , vol.271 , Issue.5252 , pp. 1081-1085
    • Berg, J.M.1    Shi, Y.2
  • 44
    • 0034602175 scopus 로고    scopus 로고
    • The transcription factor MTF-1 mediates metal regulation of the mouse ZnT1 gene
    • 1:CAS:528:DC%2BD3cXotFWlurw%3D 10952993
    • Langmade SJ, Ravindra R, Daniels PJ, et al. The transcription factor MTF-1 mediates metal regulation of the mouse ZnT1 gene. J Biol Chem. 2000;275(44):34803-9.
    • (2000) J Biol Chem , vol.275 , Issue.44 , pp. 34803-34809
    • Langmade, S.J.1    Ravindra, R.2    Daniels, P.J.3
  • 45
    • 77649239656 scopus 로고    scopus 로고
    • STAT5-glucocorticoid receptor interaction and MTF-1 regulate the expression of ZnT2 (Slc30a2) in pancreatic acinar cells
    • 1:CAS:528:DC%2BC3cXis1Cltrw%3D 2840329 20133611
    • Guo L, Lichten LA, Ryu MS, et al. STAT5-glucocorticoid receptor interaction and MTF-1 regulate the expression of ZnT2 (Slc30a2) in pancreatic acinar cells. Proc Natl Acad Sci U S A. 2010;107(7):2818-23.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , Issue.7 , pp. 2818-2823
    • Guo, L.1    Lichten, L.A.2    Ryu, M.S.3
  • 46
    • 0024222446 scopus 로고
    • A zinc-responsive factor interacts with a metal-regulated enhancer element (MRE) of the mouse metallothionein-I gene
    • 1:CAS:528:DyaL1MXhvFegsw%3D%3D 454951 3208749
    • Westin G, Schaffner W. A zinc-responsive factor interacts with a metal-regulated enhancer element (MRE) of the mouse metallothionein-I gene. EMBO J. 1988;7(12):3763-70.
    • (1988) EMBO J , vol.7 , Issue.12 , pp. 3763-3770
    • Westin, G.1    Schaffner, W.2
  • 47
    • 33748930954 scopus 로고    scopus 로고
    • Role of metal-responsive transcription factor-1 (MTF-1) in EGF-dependent DNA synthesis in primary hepatocytes
    • 1:CAS:528:DC%2BD28XhtVSktL3N 16619271
    • Kimura T, Itoh N, Sone T, et al. Role of metal-responsive transcription factor-1 (MTF-1) in EGF-dependent DNA synthesis in primary hepatocytes. J Cell Biochem. 2006;99(2):485-94.
    • (2006) J Cell Biochem , vol.99 , Issue.2 , pp. 485-494
    • Kimura, T.1    Itoh, N.2    Sone, T.3
  • 48
    • 0030006984 scopus 로고    scopus 로고
    • Extracellular zinc ions induces mitogen-activated protein kinase activity and protein tyrosine phosphorylation in bombesin-sensitive Swiss 3T3 fibroblasts
    • 1:CAS:528:DyaK28Xit1Kltr8%3D 8644999
    • Hansson A. Extracellular zinc ions induces mitogen-activated protein kinase activity and protein tyrosine phosphorylation in bombesin-sensitive Swiss 3T3 fibroblasts. Arch Biochem Biophys. 1996;328(2):233-8.
    • (1996) Arch Biochem Biophys , vol.328 , Issue.2 , pp. 233-238
    • Hansson, A.1
  • 49
    • 0022545229 scopus 로고
    • The complete primary structure of protein kinase C-The major phorbol ester receptor
    • 1:CAS:528:DyaL28XmtF2qt7c%3D 3755547
    • Parker PJ, Coussens L, Totty N, et al. The complete primary structure of protein kinase C-The major phorbol ester receptor. Science. 1986;233(4766):853- 9.
    • (1986) Science , vol.233 , Issue.4766 , pp. 853-859
    • Parker, P.J.1    Coussens, L.2    Totty, N.3
  • 50
    • 0023944916 scopus 로고
    • Zinc can increase the activity of protein kinase C and contributes to its binding to plasma membranes in T lymphocytes
    • 1:CAS:528:DyaL1cXit1Shsr4%3D 3258866
    • Csermely P, Szamel M, Resch K, et al. Zinc can increase the activity of protein kinase C and contributes to its binding to plasma membranes in T lymphocytes. J Biol Chem. 1988;263(14):6487-90.
    • (1988) J Biol Chem , vol.263 , Issue.14 , pp. 6487-6490
    • Csermely, P.1    Szamel, M.2    Resch, K.3
  • 51
    • 77956214419 scopus 로고    scopus 로고
    • X-ray fluorescence microscopy reveals accumulation and secretion of discrete intracellular zinc pools in the lactating mouse mammary gland
    • 2884036 20552032
    • McCormick N, Velasquez V, Finney L, et al. X-ray fluorescence microscopy reveals accumulation and secretion of discrete intracellular zinc pools in the lactating mouse mammary gland. PLoS ONE. 2010;5(6):e11078.
    • (2010) PLoS ONE , vol.5 , Issue.6 , pp. 11078
    • McCormick, N.1    Velasquez, V.2    Finney, L.3
  • 52
    • 84856998257 scopus 로고    scopus 로고
    • Protein kinase CK2 triggers cytosolic zinc signaling pathways by phosphorylation of zinc channel ZIP7
    • 3428905 22317921
    • Taylor KM, Hiscox S, Nicholson RI, et al. Protein kinase CK2 triggers cytosolic zinc signaling pathways by phosphorylation of zinc channel ZIP7. Sci Signal. 2012;5(210):ra11.
    • (2012) Sci Signal , vol.5 , Issue.210 , pp. 11
    • Taylor, K.M.1    Hiscox, S.2    Nicholson, R.I.3
  • 53
    • 61849121844 scopus 로고    scopus 로고
    • Zinc transporters and cancer: A potential role for ZIP7 as a hub for tyrosine kinase activation
    • 1:CAS:528:DC%2BD1MXjt1ahu78%3D 19246244
    • Hogstrand C, Kille P, Nicholson RI, et al. Zinc transporters and cancer: a potential role for ZIP7 as a hub for tyrosine kinase activation. Trends Mol Med. 2009;15(3):101-11.
    • (2009) Trends Mol Med , vol.15 , Issue.3 , pp. 101-111
    • Hogstrand, C.1    Kille, P.2    Nicholson, R.I.3
  • 54
    • 81155137295 scopus 로고    scopus 로고
    • LIV-1 promotes prostate cancer epithelial-to-mesenchymal transition and metastasis through HB-EGF shedding and EGFR-mediated ERK signaling
    • 1:CAS:528:DC%2BC3MXhs1WjurrP 3218022 22110740
    • Lue HW, Yang X, Wang R, et al. LIV-1 promotes prostate cancer epithelial-to-mesenchymal transition and metastasis through HB-EGF shedding and EGFR-mediated ERK signaling. PLoS ONE. 2011;6(11):e27720.
    • (2011) PLoS ONE , vol.6 , Issue.11 , pp. 27720
    • Lue, H.W.1    Yang, X.2    Wang, R.3
  • 55
    • 79851508232 scopus 로고    scopus 로고
    • Protein secretion in human mammary epithelial cells following HER1 receptor activation: Influence of HER2 and HER3 expression
    • 1:CAS:528:DC%2BC3MXisFSrtb0%3D 3050851 21320340
    • Zhang Y, Gonzalez RM, Zangar RC. Protein secretion in human mammary epithelial cells following HER1 receptor activation: influence of HER2 and HER3 expression. BMC Cancer. 2011;11:69.
    • (2011) BMC Cancer , vol.11 , pp. 69
    • Zhang, Y.1    Gonzalez, R.M.2    Zangar, R.C.3
  • 56
    • 49749124150 scopus 로고    scopus 로고
    • Intracellular zinc homeostasis and zinc signaling
    • 1:CAS:528:DC%2BD1cXhtFKntbfP 18754861
    • Murakami M, Hirano T. Intracellular zinc homeostasis and zinc signaling. Cancer Sci. 2008;99(8):1515-22.
    • (2008) Cancer Sci , vol.99 , Issue.8 , pp. 1515-1522
    • Murakami, M.1    Hirano, T.2
  • 57
    • 59149096668 scopus 로고    scopus 로고
    • A distinct role in breast cancer for two LIV-1 family zinc transporters
    • 1:CAS:528:DC%2BD1cXhsVCgsb7N 19021534
    • Taylor KM. A distinct role in breast cancer for two LIV-1 family zinc transporters. Biochem Soc Trans. 2008;36(Pt 6):1247-51.
    • (2008) Biochem Soc Trans , vol.36 , Issue.PART 6 , pp. 1247-1251
    • Taylor, K.M.1
  • 58
    • 84863921509 scopus 로고    scopus 로고
    • ZnT-1 enhances the activity and surface expression of T-type calcium channels through activation of Ras-ERK signaling
    • 1:CAS:528:DC%2BC38Xht1Olu7jL 22572848
    • Mor M, Beharier O, Levy S, et al. ZnT-1 enhances the activity and surface expression of T-type calcium channels through activation of Ras-ERK signaling. Am J Physiol Cell Physiol. 2012;303(2):C192-203.
    • (2012) Am J Physiol Cell Physiol , vol.303 , Issue.2 , pp. 192-203
    • Mor, M.1    Beharier, O.2    Levy, S.3
  • 59
    • 84874718742 scopus 로고    scopus 로고
    • Essential role of the zinc transporter ZIP9/SLC39A9 in regulating the activations of Akt and Erk in B-cell receptor signaling pathway in DT40 cells
    • 1:CAS:528:DC%2BC3sXktlyit74%3D 3591455 23505453
    • Taniguchi M, Fukunaka A, Hagihara M, et al. Essential role of the zinc transporter ZIP9/SLC39A9 in regulating the activations of Akt and Erk in B-cell receptor signaling pathway in DT40 cells. PLoS ONE. 2013;8(3):e58022.
    • (2013) PLoS ONE , vol.8 , Issue.3 , pp. 58022
    • Taniguchi, M.1    Fukunaka, A.2    Hagihara, M.3
  • 60
    • 67449168402 scopus 로고    scopus 로고
    • Zinc transporter Znt5/Slc30a5 is required for the mast cell-mediated delayed-type allergic reaction but not the immediate-type reaction
    • 1:CAS:528:DC%2BD1MXntFGmu7c%3D 2715059 19451265
    • Nishida K, Hasegawa A, Nakae S, et al. Zinc transporter Znt5/Slc30a5 is required for the mast cell-mediated delayed-type allergic reaction but not the immediate-type reaction. J Exp Med. 2009;206(6):1351-64.
    • (2009) J Exp Med , vol.206 , Issue.6 , pp. 1351-1364
    • Nishida, K.1    Hasegawa, A.2    Nakae, S.3
  • 61
    • 38349156656 scopus 로고    scopus 로고
    • Lumen formation during mammary epithelial morphogenesis: Insights from in vitro and in vivo models
    • 1:CAS:528:DC%2BD1cXjsVKntbk%3D 18196964
    • Mailleux AA, Overholtzer M, Brugge JS. Lumen formation during mammary epithelial morphogenesis: insights from in vitro and in vivo models. Cell Cycle. 2008;7(1):57-62.
    • (2008) Cell Cycle , vol.7 , Issue.1 , pp. 57-62
    • Mailleux, A.A.1    Overholtzer, M.2    Brugge, J.S.3
  • 62
    • 84870325678 scopus 로고    scopus 로고
    • Cellular mechanisms of zinc dysregulation: A perspective on zinc homeostasis as an etiological factor in the development and progression of breast cancer
    • 1:CAS:528:DC%2BC38XhtFGgtrzL 3448077 23016122
    • Alam S, Kelleher SL. Cellular mechanisms of zinc dysregulation: a perspective on zinc homeostasis as an etiological factor in the development and progression of breast cancer. Nutrients. 2012;4(8):875-903.
    • (2012) Nutrients , vol.4 , Issue.8 , pp. 875-903
    • Alam, S.1    Kelleher, S.L.2
  • 63
    • 68749108391 scopus 로고    scopus 로고
    • Zinc transporter-2 (ZnT2) variants are localized to distinct subcellular compartments and functionally transport zinc
    • 1:CAS:528:DC%2BD1MXhtVGhs7bM 3381892 19496757
    • Lopez V, Kelleher SL. Zinc transporter-2 (ZnT2) variants are localized to distinct subcellular compartments and functionally transport zinc. Biochem J. 2009;422(1):43-52.
    • (2009) Biochem J , vol.422 , Issue.1 , pp. 43-52
    • Lopez, V.1    Kelleher, S.L.2
  • 64
    • 48949119323 scopus 로고    scopus 로고
    • The human zinc transporter SLC39A8 (Zip8) is critical in zinc-mediated cytoprotection in lung epithelia
    • 1:CAS:528:DC%2BD1cXnsVGgtb0%3D 18390834
    • Besecker B, Bao S, Bohacova B, et al. The human zinc transporter SLC39A8 (Zip8) is critical in zinc-mediated cytoprotection in lung epithelia. Am J Physiol Lung Cell Mol Physiol. 2008;294(6):L1127-36.
    • (2008) Am J Physiol Lung Cell Mol Physiol , vol.294 , Issue.6 , pp. 1127-1136
    • Besecker, B.1    Bao, S.2    Bohacova, B.3
  • 65
    • 0035479845 scopus 로고    scopus 로고
    • Matrix metalloproteinases: They're not just for matrix anymore!
    • 1:CAS:528:DC%2BD3MXmsFersLw%3D 11544020
    • McCawley LJ, Matrisian LM. Matrix metalloproteinases: they're not just for matrix anymore! Curr Opin Cell Biol. 2001;13(5):534-40.
    • (2001) Curr Opin Cell Biol , vol.13 , Issue.5 , pp. 534-540
    • McCawley, L.J.1    Matrisian, L.M.2
  • 66
    • 0141768243 scopus 로고    scopus 로고
    • Site-specific inductive and inhibitory activities of MMP-2 and MMP-3 orchestrate mammary gland branching morphogenesis
    • 1:CAS:528:DC%2BD3sXnsVWjsbw%3D 2172848 12975354
    • Wiseman BS, Sternlicht MD, Lund LR, et al. Site-specific inductive and inhibitory activities of MMP-2 and MMP-3 orchestrate mammary gland branching morphogenesis. J Cell Biol. 2003;162(6):1123-33.
    • (2003) J Cell Biol , vol.162 , Issue.6 , pp. 1123-1133
    • Wiseman, B.S.1    Sternlicht, M.D.2    Lund, L.R.3
  • 67
    • 0036468911 scopus 로고    scopus 로고
    • Activation of membrane-type matrix metalloproteinase 3 zymogen by the proprotein convertase furin in the trans-Golgi network
    • 1:CAS:528:DC%2BD38Xht1Krtbs%3D 11830519
    • Kang T, Nagase H, Pei D. Activation of membrane-type matrix metalloproteinase 3 zymogen by the proprotein convertase furin in the trans-Golgi network. Cancer Res. 2002;62(3):675-81.
    • (2002) Cancer Res , vol.62 , Issue.3 , pp. 675-681
    • Kang, T.1    Nagase, H.2    Pei, D.3
  • 68
    • 15744404638 scopus 로고    scopus 로고
    • Furin directly cleaves proMMP-2 in the trans-Golgi network resulting in a nonfunctioning proteinase
    • 1:CAS:528:DC%2BD2MXisVOqtbY%3D 15637056
    • Cao J, Rehemtulla A, Pavlaki M, et al. Furin directly cleaves proMMP-2 in the trans-Golgi network resulting in a nonfunctioning proteinase. J Biol Chem. 2005;280(12):10974-80.
    • (2005) J Biol Chem , vol.280 , Issue.12 , pp. 10974-10980
    • Cao, J.1    Rehemtulla, A.2    Pavlaki, M.3
  • 69
    • 4344670926 scopus 로고    scopus 로고
    • Furin inhibition by compounds of copper and zinc
    • 1:CAS:528:DC%2BD2cXmvFCntL0%3D 15140896
    • Podsiadlo P, Komiyama T, Fuller RS, et al. Furin inhibition by compounds of copper and zinc. J Biol Chem. 2004;279(35):36219-27.
    • (2004) J Biol Chem , vol.279 , Issue.35 , pp. 36219-36227
    • Podsiadlo, P.1    Komiyama, T.2    Fuller, R.S.3
  • 70
    • 17644400171 scopus 로고    scopus 로고
    • The ZIP7 gene (Slc39a7) encodes a zinc transporter involved in zinc homeostasis of the Golgi apparatus
    • 1:CAS:528:DC%2BD2MXjtFSltbY%3D 15705588
    • Huang L, Kirschke CP, Zhang Y, et al. The ZIP7 gene (Slc39a7) encodes a zinc transporter involved in zinc homeostasis of the Golgi apparatus. J Biol Chem. 2005;280(15):15456-63.
    • (2005) J Biol Chem , vol.280 , Issue.15 , pp. 15456-15463
    • Huang, L.1    Kirschke, C.P.2    Zhang, Y.3
  • 71
    • 0037151036 scopus 로고    scopus 로고
    • A novel zinc-regulated human zinc transporter, hZTL1, is localized to the enterocyte apical membrane
    • 1:CAS:528:DC%2BD38XltVGku78%3D 11937503
    • Cragg RA, Christie GR, Phillips SR, et al. A novel zinc-regulated human zinc transporter, hZTL1, is localized to the enterocyte apical membrane. J Biol Chem. 2002;277(25):22789-97.
    • (2002) J Biol Chem , vol.277 , Issue.25 , pp. 22789-22797
    • Cragg, R.A.1    Christie, G.R.2    Phillips, S.R.3
  • 72
    • 67650069902 scopus 로고    scopus 로고
    • Zip3 (Slc39a3) functions in zinc reuptake from the alveolar lumen in lactating mammary gland
    • 1:CAS:528:DC%2BD1MXovVKhsr4%3D 2711697 19458277
    • Kelleher SL, Lopez V, Lönnerdal B, et al. Zip3 (Slc39a3) functions in zinc reuptake from the alveolar lumen in lactating mammary gland. Am J Physiol Regul Integr Comp Physiol. 2009;297(1):R194-201.
    • (2009) Am J Physiol Regul Integr Comp Physiol , vol.297 , Issue.1 , pp. 194-201
    • Kelleher, S.L.1    Lopez, V.2    Lönnerdal, B.3
  • 73
    • 0016590403 scopus 로고
    • Hydrogen-exchange study of the conformational stability of human carbonic-anhydrase B and its metallocomplexes
    • 240709
    • Závodszky P, Johansen JT, Hvidt A. Hydrogen-exchange study of the conformational stability of human carbonic-anhydrase B and its metallocomplexes. Eur J Biochem. 1975;56(1):67-72.
    • (1975) Eur J Biochem , vol.56 , Issue.1 , pp. 67-72
    • Závodszky, P.1    Johansen, J.T.2    Hvidt, A.3
  • 74
    • 0035949696 scopus 로고    scopus 로고
    • The identification of secreted carbonic anhydrase VI as a constitutive glycoprotein of human and rat milk
    • 1:CAS:528:DC%2BD3MXnt12js7g%3D 58776 11553764
    • Karhumaa P, Leinonen J, Parkkila S, et al. The identification of secreted carbonic anhydrase VI as a constitutive glycoprotein of human and rat milk. Proc Natl Acad Sci U S A. 2001;98(20):11604-8.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , Issue.20 , pp. 11604-11608
    • Karhumaa, P.1    Leinonen, J.2    Parkkila, S.3
  • 75
    • 0030963913 scopus 로고    scopus 로고
    • Salivary carbonic anhydrase protects gastroesophageal mucosa from acid injury
    • 1:CAS:528:DyaK2sXjs1CrtLg%3D 9149056
    • Parkkila S, Parkkila AK, Lehtola J, et al. Salivary carbonic anhydrase protects gastroesophageal mucosa from acid injury. Dig Dis Sci. 1997;42(5):1013-9.
    • (1997) Dig Dis Sci , vol.42 , Issue.5 , pp. 1013-1019
    • Parkkila, S.1    Parkkila, A.K.2    Lehtola, J.3
  • 76
    • 0032578599 scopus 로고    scopus 로고
    • Gustin from human parotid saliva is carbonic anhydrase VI
    • 1:CAS:528:DyaK1cXmsF2qs7g%3D 9784398
    • Thatcher BJ, Doherty AE, Orvisky E, et al. Gustin from human parotid saliva is carbonic anhydrase VI. Biochem Biophys Res Commun. 1998;250(3):635-41.
    • (1998) Biochem Biophys Res Commun , vol.250 , Issue.3 , pp. 635-641
    • Thatcher, B.J.1    Doherty, A.E.2    Orvisky, E.3
  • 77
    • 84879671151 scopus 로고    scopus 로고
    • Protein trafficking abnormalities in Drosophila tissues with impaired activity of the ZIP7 zinc transporter Catsup
    • 1:CAS:528:DC%2BC3sXhtlClsr%2FM 23785054
    • Groth C, Sasamura T, Khanna MR, et al. Protein trafficking abnormalities in Drosophila tissues with impaired activity of the ZIP7 zinc transporter Catsup. Development. 2013;140(14):3018-27.
    • (2013) Development , vol.140 , Issue.14 , pp. 3018-3027
    • Groth, C.1    Sasamura, T.2    Khanna, M.R.3
  • 78
    • 0018871097 scopus 로고
    • Isolation of a low molecular weight zinc binding ligand from human milk
    • 7189547
    • Lönnerdal B, Stanislowski AG, Hurley LS. Isolation of a low molecular weight zinc binding ligand from human milk. J Inorg Biochem. 1980;12(1):71-8.
    • (1980) J Inorg Biochem , vol.12 , Issue.1 , pp. 71-78
    • Lönnerdal, B.1    Stanislowski, A.G.2    Hurley, L.S.3
  • 79
    • 0020357681 scopus 로고
    • Zinc and copper binding proteins in human milk
    • 7148736
    • Lönnerdal B, Hoffman B, Hurley LS. Zinc and copper binding proteins in human milk. Am J Clin Nutr. 1982;36(6):1170-6.
    • (1982) Am J Clin Nutr , vol.36 , Issue.6 , pp. 1170-1176
    • Lönnerdal, B.1    Hoffman, B.2    Hurley, L.S.3
  • 80
    • 0019941764 scopus 로고
    • Binding of zinc to casein
    • 1:CAS:528:DyaL38XktVGjs7k%3D 7081095
    • Harzer G, Kauer H. Binding of zinc to casein. Am J Clin Nutr. 1982;35(5):981-7.
    • (1982) Am J Clin Nutr , vol.35 , Issue.5 , pp. 981-987
    • Harzer, G.1    Kauer, H.2
  • 81
    • 84878579262 scopus 로고    scopus 로고
    • Compound Heterozygous Mutations in SLC30A2/ZnT2 Results in Low Milk Zinc Concentrations: A Novel Mechanism for Zinc Deficiency in a Breast-Fed Infant
    • 1:CAS:528:DC%2BC3sXpslOhtrg%3D 3669329 23741301
    • Itsumura N, Inamo Y, Okazaki F, et al. Compound Heterozygous Mutations in SLC30A2/ZnT2 Results in Low Milk Zinc Concentrations: A Novel Mechanism for Zinc Deficiency in a Breast-Fed Infant. PLoS ONE. 2013;8(5):e64045.
    • (2013) PLoS ONE , vol.8 , Issue.5 , pp. 64045
    • Itsumura, N.1    Inamo, Y.2    Okazaki, F.3
  • 82
    • 0017870725 scopus 로고
    • Zinc deficiency in murine milk underlies expression of the lethal milk (lm) mutation
    • 1:CAS:528:DyaE1cXnt1CmsA%3D%3D 619449
    • Piletz JE, Ganschow RE. Zinc deficiency in murine milk underlies expression of the lethal milk (lm) mutation. Science. 1978;199(4325):181-3.
    • (1978) Science , vol.199 , Issue.4325 , pp. 181-183
    • Piletz, J.E.1    Ganschow, R.E.2
  • 83
    • 0042065348 scopus 로고    scopus 로고
    • Analysis of zinc transporter, hZnT4 (Slc30A4), gene expression in a mammary gland disorder leading to reduced zinc secretion into milk
    • 1:CAS:528:DC%2BD3sXlsFKmsrs%3D 12743795
    • Michalczyk A, Varigos G, Catto-Smith A, et al. Analysis of zinc transporter, hZnT4 (Slc30A4), gene expression in a mammary gland disorder leading to reduced zinc secretion into milk. Hum Genet. 2003;113(3):202-10.
    • (2003) Hum Genet , vol.113 , Issue.3 , pp. 202-210
    • Michalczyk, A.1    Varigos, G.2    Catto-Smith, A.3
  • 84
    • 0028215344 scopus 로고
    • Protein kinase A and AP-1 (c-Fos/JunD) are induced during apoptosis of mouse mammary epithelial cells
    • 1:CAS:528:DyaK2cXis1KksL0%3D 8134124
    • Marti A, Jehn B, Costello E, et al. Protein kinase A and AP-1 (c-Fos/JunD) are induced during apoptosis of mouse mammary epithelial cells. Oncogene. 1994;9(4):1213-23.
    • (1994) Oncogene , vol.9 , Issue.4 , pp. 1213-1223
    • Marti, A.1    Jehn, B.2    Costello, E.3
  • 85
    • 79952257741 scopus 로고    scopus 로고
    • Stat3 controls lysosomal-mediated cell death in vivo
    • 1:CAS:528:DC%2BC3MXisFKntrY%3D 21336304
    • Kreuzaler PA, Staniszewska AD, Li W, et al. Stat3 controls lysosomal-mediated cell death in vivo. Nat Cell Biol. 2011;13(3):303-9.
    • (2011) Nat Cell Biol , vol.13 , Issue.3 , pp. 303-309
    • Kreuzaler, P.A.1    Staniszewska, A.D.2    Li, W.3
  • 86
    • 84865177539 scopus 로고    scopus 로고
    • Calpains mediate epithelial-cell death during mammary gland involution: Mitochondria and lysosomal destabilization
    • 1:CAS:528:DC%2BC38Xht1Wltb%2FL 3422479 22555453
    • Arnandis T, Ferrer-Vicens I, García-Trevijano ER, et al. Calpains mediate epithelial-cell death during mammary gland involution: mitochondria and lysosomal destabilization. Cell Death Differ. 2012;19(9):1536-48.
    • (2012) Cell Death Differ , vol.19 , Issue.9 , pp. 1536-1548
    • Arnandis, T.1    Ferrer-Vicens, I.2    García-Trevijano, E.R.3
  • 88
    • 33947155299 scopus 로고    scopus 로고
    • The beginning of the end: Death signaling in early involution
    • 17340185
    • Baxter FO, Neoh K, Tevendale MC. The beginning of the end: death signaling in early involution. J Mammary Gland Biol Neoplasia. 2007;12(1):3-13.
    • (2007) J Mammary Gland Biol Neoplasia , vol.12 , Issue.1 , pp. 3-13
    • Baxter, F.O.1    Neoh, K.2    Tevendale, M.C.3
  • 89
    • 34247551104 scopus 로고    scopus 로고
    • Involution: Apoptosis and tissue remodelling that convert the mammary gland from milk factory to a quiescent organ
    • 1557708 16677411
    • Watson CJ. Involution: apoptosis and tissue remodelling that convert the mammary gland from milk factory to a quiescent organ. Breast Cancer Res. 2006;8(2):203.
    • (2006) Breast Cancer Res , vol.8 , Issue.2 , pp. 203
    • Watson, C.J.1
  • 90
    • 0028922876 scopus 로고
    • The influence of zinc on apoptosis
    • 1:CAS:528:DyaK2MXlsVektLc%3D 7785963
    • Sunderman FW. The influence of zinc on apoptosis. Ann Clin Lab Sci. 1995;25(2):134-42.
    • (1995) Ann Clin Lab Sci , vol.25 , Issue.2 , pp. 134-142
    • Sunderman, F.W.1
  • 91
    • 70349096774 scopus 로고    scopus 로고
    • Oxidative injury triggers autophagy in astrocytes: The role of endogenous zinc
    • 19229997
    • Lee SJ, Cho KS, Koh JY. Oxidative injury triggers autophagy in astrocytes: the role of endogenous zinc. Glia. 2009;57(12):1351-61.
    • (2009) Glia , vol.57 , Issue.12 , pp. 1351-1361
    • Lee, S.J.1    Cho, K.S.2    Koh, J.Y.3
  • 92
    • 84872006971 scopus 로고    scopus 로고
    • Where killers meet-permeabilization of the outer mitochondrial membrane during apoptosis
    • 23284044
    • Bender T, Martinou JC. Where killers meet-permeabilization of the outer mitochondrial membrane during apoptosis. Cold Spring Harb Perspect Biol. 2013;5(1):a011106.
    • (2013) Cold Spring Harb Perspect Biol , vol.5 , Issue.1 , pp. 011106
    • Bender, T.1    Martinou, J.C.2
  • 93
    • 0035947776 scopus 로고    scopus 로고
    • Cathepsin B acts as a dominant execution protease in tumor cell apoptosis induced by tumor necrosis factor
    • 1:CAS:528:DC%2BD3MXktVagsrw%3D 2174340 11381085
    • Foghsgaard L, Wissing D, Mauch D, et al. Cathepsin B acts as a dominant execution protease in tumor cell apoptosis induced by tumor necrosis factor. J Cell Biol. 2001;153(5):999-1010.
    • (2001) J Cell Biol , vol.153 , Issue.5 , pp. 999-1010
    • Foghsgaard, L.1    Wissing, D.2    Mauch, D.3
  • 94
    • 79954628520 scopus 로고    scopus 로고
    • Clioquinol induces autophagy in cultured astrocytes and neurons by acting as a zinc ionophore
    • 1:CAS:528:DC%2BC3MXkvVGltL8%3D 21220021
    • Park MH, Lee SJ, Byun HR, et al. Clioquinol induces autophagy in cultured astrocytes and neurons by acting as a zinc ionophore. Neurobiol Dis. 2011;42(3):242-51.
    • (2011) Neurobiol Dis , vol.42 , Issue.3 , pp. 242-251
    • Park, M.H.1    Lee, S.J.2    Byun, H.R.3
  • 95
    • 41149133254 scopus 로고    scopus 로고
    • Zinc and 4-hydroxy-2-nonenal mediate lysosomal membrane permeabilization induced by H2O2 in cultured hippocampal neurons
    • 1:CAS:528:DC%2BD1cXjvFCjsb0%3D 18354014
    • Hwang JJ, Lee SJ, Kim TY, et al. Zinc and 4-hydroxy-2-nonenal mediate lysosomal membrane permeabilization induced by H2O2 in cultured hippocampal neurons. J Neurosci. 2008;28(12):3114-22.
    • (2008) J Neurosci , vol.28 , Issue.12 , pp. 3114-3122
    • Hwang, J.J.1    Lee, S.J.2    Kim, T.Y.3
  • 96
    • 84867866496 scopus 로고    scopus 로고
    • Induction of autophagy and cell death by tamoxifen in cultured retinal pigment epithelial and photoreceptor cells
    • 1:CAS:528:DC%2BC38XhvVGqsLnP
    • Cho KS, Yoon YH, Choi JA, et al. Induction of autophagy and cell death by tamoxifen in cultured retinal pigment epithelial and photoreceptor cells. Investig Ophthalmol Vis Sci. 2012;53(9):5344-53.
    • (2012) Investig Ophthalmol Vis Sci , vol.53 , Issue.9 , pp. 5344-5353
    • Cho, K.S.1    Yoon, Y.H.2    Choi, J.A.3
  • 97
    • 78349307959 scopus 로고    scopus 로고
    • Zinc(II) ion mediates tamoxifen-induced autophagy and cell death in MCF-7 breast cancer cell line
    • 1:CAS:528:DC%2BC3cXhtlyrsrrI 20524045
    • Hwang JJ, Kim HN, Kim J, et al. Zinc(II) ion mediates tamoxifen-induced autophagy and cell death in MCF-7 breast cancer cell line. Biometals. 2010;23(6):997-1013.
    • (2010) Biometals , vol.23 , Issue.6 , pp. 997-1013
    • Hwang, J.J.1    Kim, H.N.2    Kim, J.3
  • 98
    • 33947727880 scopus 로고    scopus 로고
    • Zinc transporter 2 (SLC30A2) can suppress the vesicular zinc defect of adaptor protein 3-depleted fibroblasts by promoting zinc accumulation in lysosomes
    • 1885236 17349999
    • Falcón-Pérez JM, Dell'Angelica EC. Zinc transporter 2 (SLC30A2) can suppress the vesicular zinc defect of adaptor protein 3-depleted fibroblasts by promoting zinc accumulation in lysosomes. Exp Cell Res. 2007;313(7):1473-83.
    • (2007) Exp Cell Res , vol.313 , Issue.7 , pp. 1473-1483
    • Falcón-Pérez, J.M.1    Dell'Angelica, E.C.2
  • 99
    • 0036868477 scopus 로고    scopus 로고
    • High-level expression of zinc transporter-2 in the rat lateral and dorsal prostate
    • 1:CAS:528:DC%2BD38XptV2hur8%3D 12399528
    • Iguchi K, Usui S, Inoue T, et al. High-level expression of zinc transporter-2 in the rat lateral and dorsal prostate. J Androl. 2002;23(6):819-24.
    • (2002) J Androl , vol.23 , Issue.6 , pp. 819-824
    • Iguchi, K.1    Usui, S.2    Inoue, T.3
  • 100
    • 0029873677 scopus 로고    scopus 로고
    • ZnT-2, a mammalian protein that confers resistance to zinc by facilitating vesicular sequestration
    • 1:CAS:528:DyaK28XivVant7s%3D 450094 8617223
    • Palmiter RD, Cole TB, Findley SD. ZnT-2, a mammalian protein that confers resistance to zinc by facilitating vesicular sequestration. EMBO J. 1996;15(8):1784-91.
    • (1996) EMBO J , vol.15 , Issue.8 , pp. 1784-1791
    • Palmiter, R.D.1    Cole, T.B.2    Findley, S.D.3
  • 101
    • 33749342905 scopus 로고    scopus 로고
    • Mammary gland copper transport is stimulated by prolactin through alterations in Ctr1 and Atp7A localization
    • 1:CAS:528:DC%2BD28XhtFegtLjE 16741141
    • Kelleher SL, Lönnerdal B. Mammary gland copper transport is stimulated by prolactin through alterations in Ctr1 and Atp7A localization. Am J Physiol Regul Integr Comp Physiol. 2006;291(4):R1181-91.
    • (2006) Am J Physiol Regul Integr Comp Physiol , vol.291 , Issue.4 , pp. 1181-1191
    • Kelleher, S.L.1    Lönnerdal, B.2
  • 102
    • 84875588858 scopus 로고    scopus 로고
    • Zinc-dependent lysosomal enlargement in TRPML1-deficient cells involves MTF-1 transcription factor and ZnT4 (Slc30a4) transporter
    • 1:CAS:528:DC%2BC3sXkvFOhur8%3D 3654546 23368743
    • Kukic I, Lee JK, Coblentz J, et al. Zinc-dependent lysosomal enlargement in TRPML1-deficient cells involves MTF-1 transcription factor and ZnT4 (Slc30a4) transporter. Biochem J. 2013;451(2):155-63.
    • (2013) Biochem J , vol.451 , Issue.2 , pp. 155-163
    • Kukic, I.1    Lee, J.K.2    Coblentz, J.3
  • 103
    • 0038002071 scopus 로고    scopus 로고
    • Cathepsin L plays an active role in involution of the mouse mammary gland
    • 1:CAS:528:DC%2BD3sXmt12htbc%3D 12815617
    • Burke MA, Hutter D, Reshamwala RP, et al. Cathepsin L plays an active role in involution of the mouse mammary gland. Dev Dyn. 2003;227(3):315-22.
    • (2003) Dev Dyn , vol.227 , Issue.3 , pp. 315-322
    • Burke, M.A.1    Hutter, D.2    Reshamwala, R.P.3
  • 104
  • 105
    • 0014730642 scopus 로고
    • Lysosomal changes during castration-induced prostatic involution in the rat
    • 1:STN:280:DyaE3M%2Fis1Ojsg%3D%3D 5476635
    • Helminen HJ, Ericsson JL, Niemi M. Lysosomal changes during castration-induced prostatic involution in the rat. Acta Pathol Microbiol Scand A. 1970;78(4):493-4.
    • (1970) Acta Pathol Microbiol Scand A , vol.78 , Issue.4 , pp. 493-494
    • Helminen, H.J.1    Ericsson, J.L.2    Niemi, M.3
  • 106
    • 0014805846 scopus 로고
    • Quantitation of lysosomal enzyme changes during enforced mammary gland involution
    • 1:CAS:528:DyaE3cXktlejtr8%3D 5463638
    • Helminen HJ, Ericsson JL. Quantitation of lysosomal enzyme changes during enforced mammary gland involution. Exp Cell Res. 1970;60(3):419-26.
    • (1970) Exp Cell Res , vol.60 , Issue.3 , pp. 419-426
    • Helminen, H.J.1    Ericsson, J.L.2
  • 107
    • 67650050212 scopus 로고    scopus 로고
    • Zinc transporter ZIP8 (SLC39A8) and zinc influence IFN-gamma expression in activated human T cells
    • 1:CAS:528:DC%2BD1MXps1elsr4%3D 2726764 19401385
    • Aydemir TB, Liuzzi JP, McClellan S, et al. Zinc transporter ZIP8 (SLC39A8) and zinc influence IFN-gamma expression in activated human T cells. J Leukoc Biol. 2009;86(2):337-48.
    • (2009) J Leukoc Biol , vol.86 , Issue.2 , pp. 337-348
    • Aydemir, T.B.1    Liuzzi, J.P.2    McClellan, S.3
  • 108
    • 54049156405 scopus 로고    scopus 로고
    • The type IV mucolipidosis-associated protein TRPML1 is an endolysosomal iron release channel
    • 1:CAS:528:DC%2BD1cXht1GgurvE 18794901
    • Dong XP, Cheng X, Mills E, et al. The type IV mucolipidosis-associated protein TRPML1 is an endolysosomal iron release channel. Nature. 2008;455(7215):992-6.
    • (2008) Nature , vol.455 , Issue.7215 , pp. 992-996
    • Dong, X.P.1    Cheng, X.2    Mills, E.3
  • 109
    • 78049405392 scopus 로고    scopus 로고
    • Zinc dyshomeostasis is linked with the loss of mucolipidosis IV-associated TRPML1 ion channel
    • 1:CAS:528:DC%2BC3cXhtlGktLfE 2966043 20864526
    • Eichelsdoerfer JL, Evans JA, Slaugenhaupt SA, et al. Zinc dyshomeostasis is linked with the loss of mucolipidosis IV-associated TRPML1 ion channel. J Biol Chem. 2010;285(45):34304-8.
    • (2010) J Biol Chem , vol.285 , Issue.45 , pp. 34304-34308
    • Eichelsdoerfer, J.L.1    Evans, J.A.2    Slaugenhaupt, S.A.3
  • 110
    • 0027501386 scopus 로고
    • Correlation of apoptosis with change in intracellular labile Zn(II) using zinquin [(2-methyl-8-p-toluenesulphonamido-6-quinolyloxy)acetic acid], a new specific fluorescent probe for Zn(II)
    • 1:CAS:528:DyaK2cXjvVer 1137710 8257431
    • Zalewski PD, Forbes IJ, Betts WH. Correlation of apoptosis with change in intracellular labile Zn(II) using zinquin [(2-methyl-8-p-toluenesulphonamido-6- quinolyloxy)acetic acid], a new specific fluorescent probe for Zn(II). Biochem J. 1993;296(Pt 2):403-8.
    • (1993) Biochem J , vol.296 , Issue.PART 2 , pp. 403-408
    • Zalewski, P.D.1    Forbes, I.J.2    Betts, W.H.3
  • 111
    • 0030881603 scopus 로고    scopus 로고
    • Biochemical characteristics of caspases-3, -6, -7, and -8
    • 1:CAS:528:DyaK2sXms1Glsrs%3D 9325297
    • Stennicke HR, Salvesen GS. Biochemical characteristics of caspases-3, -6, -7, and -8. J Biol Chem. 1997;272(41):25719-23.
    • (1997) J Biol Chem , vol.272 , Issue.41 , pp. 25719-25723
    • Stennicke, H.R.1    Salvesen, G.S.2
  • 112
    • 0035693751 scopus 로고    scopus 로고
    • The role of zinc in caspase activation and apoptotic cell death
    • 1:CAS:528:DC%2BD38XpsFWrtQ%3D%3D 11831462
    • Truong-Tran AQ, Carter J, Ruffin RE, et al. The role of zinc in caspase activation and apoptotic cell death. Biometals. 2001;14(3-4):315-30.
    • (2001) Biometals , vol.14 , Issue.3-4 , pp. 315-330
    • Truong-Tran, A.Q.1    Carter, J.2    Ruffin, R.E.3
  • 113
    • 84877875231 scopus 로고    scopus 로고
    • Zinc-rich inhibitor of apoptosis proteins (IAPs) as regulatory factors in the epithelium of normal and inflamed airways
    • 1:CAS:528:DC%2BC3sXlsF2itro%3D 23460081
    • Roscioli E, Hamon R, Lester S, et al. Zinc-rich inhibitor of apoptosis proteins (IAPs) as regulatory factors in the epithelium of normal and inflamed airways. Biometals. 2013;26(2):205-27.
    • (2013) Biometals , vol.26 , Issue.2 , pp. 205-227
    • Roscioli, E.1    Hamon, R.2    Lester, S.3
  • 114
    • 84878013693 scopus 로고    scopus 로고
    • Intracellular zinc is required for intestinal cell survival signals triggered by the inflammatory cytokine TNFα
    • 1:CAS:528:DC%2BC38Xhtlamu7zM 22967671
    • Ranaldi G, Ferruzza S, Canali R, et al. Intracellular zinc is required for intestinal cell survival signals triggered by the inflammatory cytokine TNFα. J Nutr Biochem. 2013;24(6):967-76.
    • (2013) J Nutr Biochem , vol.24 , Issue.6 , pp. 967-976
    • Ranaldi, G.1    Ferruzza, S.2    Canali, R.3
  • 115
    • 33749656530 scopus 로고    scopus 로고
    • The lysosomal-mitochondrial axis theory of postmitotic aging and cell death
    • 1:CAS:528:DC%2BD28XhtFSksbzO 16737690
    • Terman A, Gustafsson B, Brunk UT. The lysosomal-mitochondrial axis theory of postmitotic aging and cell death. Chem Biol Interact. 2006;163(1-2):29-37.
    • (2006) Chem Biol Interact , vol.163 , Issue.1-2 , pp. 29-37
    • Terman, A.1    Gustafsson, B.2    Brunk, U.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.