[1]
|
(2020) Erratum: Global Cancer Statistics 2018: GLOBOCAN Estimates of Incidence and Mortality Worldwide for 36 Cancers in 185 Countries. CA: A Cancer Journal for Clinicians, 70, 313. https://doi.org/10.3322/caac.21609
|
[2]
|
Hashimoto, I. and Oshima, T. (2022) Claudins and Gastric Cancer: An Overview. Cancers, 14, Article No. 290.
https://doi.org/10.3390/cancers14020290
|
[3]
|
Tsukita, S. and Furuse, M. (2000) The Structure and Function of Claudins, Cell Adhesion Molecules at Tight Junctions. Annals of the New York Academy of Sciences, 915, 129-135. https://doi.org/10.1111/j.1749-6632.2000.tb05235.x
|
[4]
|
Lal-Nag, M. and Morin, P.J. (2009) The Claudins. Ge-nome Biology, 10, Article No. 235.
https://doi.org/10.1186/gb-2009-10-8-235
|
[5]
|
Colegio, O.R., Van Itallie, C.M., McCrea, H.J., Rahner, C. and Anderson, J.M. (2002) Claudins Create Charge-Selec- tive Channels in the Paracellular Pathway between Epithelial Cells. American Journal of Physiology-Cell Physiology, 283, C142-C147. https://doi.org/10.1152/ajpcell.00038.2002
|
[6]
|
Angelow, S., Ahlstrom, R. and Yu, A.S.L. (2008) Biology of Claudins. American Journal of Physiology-Renal Physiology, 295, F867-F876. https://doi.org/10.1152/ajprenal.90264.2008
|
[7]
|
Piontek, J., Winkler, L., Wolburg, H., Müller, S.L., Zuleger, N., Piehl, C., Wiesner, B., Krause, G. and Blasig, I.E. (2008) Formation of Tight Junction: Determinants of Homophilic In-teraction between Classic Claudins. The FASEB Journal, 22, 146-158. https://doi.org/10.1096/fj.07-8319com
|
[8]
|
Huo, L., Wen, W., Wang, R., Kam, C., Xia, J., Feng, W. and Zhang, M. (2011) Cdc42-Dependent Formation of the ZO-1/MRCKβ Complex at the Leading Edge Controls Cell Migration. The EMBO Journal, 30, 665-678.
https://doi.org/10.1038/emboj.2010.353
|
[9]
|
Van Itallie, C.M., Tietgens, A.J., LoGrande, K., Aponte, A., Gucek, M. and Anderson, J.M. (2012) Phosphorylation of Claudin-2 on Serine 208 Promotes Membrane Retention and Reduces Trafficking to Lysosomes. Journal of Cell Science, 125, 4902-4912. https://doi.org/10.1242/jcs.111237
|
[10]
|
Singh, P., Toom, S. and Huang, Y. (2017) Anti-Claudin 18.2 Antibody as New Targeted Therapy for Advanced Gastric Cancer. Journal of Hematology & Oncology, 10, Article No.105. https://doi.org/10.1186/s13045-017-0473-4
|
[11]
|
Ding, L., Lu, Z., Lu, Q. and Chen, Y.H. (2013) The Claudin Family of Proteins in Human Malignancy: A Clinical Perspective. Cancer Management and Research, 5, 367-375. https://doi.org/10.2147/CMAR.S38294
|
[12]
|
Hu, Y.J., Wang, Y.D., Tan, F.Q. and Yang, W.X. (2013) Regulation of Paracellular Permeability: Factors and Mechanisms. Cancer Management and Research, 40, 6123-6142. https://doi.org/10.1007/s11033-013-2724-y
|
[13]
|
Gyõrffy, H., Holczbauer, A., Nagy, P., Szabó, Z., Kupcsulik, P., Páska, C., Papp, J., Schaff, Z. and Kiss, A. (2005) Claudin Expression in Barrett’s Esophagus and Adenocarcinoma. Virchows Archiv, 447, 961-968.
https://doi.org/10.1007/s00428-005-0045-9
|
[14]
|
D’Souza, T., Agarwal, R. and Morin, P.J. (2005) Phosphoryla-tion of Claudin-3 at Threonine 192 by CAMP-Dependent Protein Kinase Regulates Tight Junction Barrier Function in Ovarian Cancer Cells. Journal of Biological Chemistry, 280, 26233-26240. https://doi.org/10.1074/jbc.M502003200
|
[15]
|
Tanaka, M., Kamata, R. and Sakai, R. (2005) EphA2 Phosphory-lates the Cytoplasmic Tail of Claudin-4 and Mediates Paracellular Permeability. Journal of Biological Chemistry, 280, 42375-42382.
https://doi.org/10.1074/jbc.M503786200
|
[16]
|
Turner, J.R., Buschmann, M.M., Romero-Calvo, I., Sailer, A. and Shen, L. (2014) The Role of Molecular Remodeling in Differential Regulation of Tight Junction Permeability. Seminars in Cell & Developmental Biology, 36, 204-212.
https://doi.org/10.1016/j.semcdb.2014.09.022
|
[17]
|
Tabariès, S. and Siegel, P.M. (2017) The Role of Claudins in Cancer Metastasis. Oncogene, 36, 1176-1190.
https://doi.org/10.1038/onc.2016.289
|
[18]
|
Yao, F., Kausalya, J.P., Sia, Y.Y., Teo, A.S., Lee, W.H., Ong, A.G., Zhang, Z., Tan, J.H., Li, G., Bertrand, D., Liu, X., Poh, H.M., Guan, P., Zhu, F., Pathiraja, T.N., Ariyaratne, P.N., Rao, J., Woo, X.Y., Cai, S., Mulawadi, F.H., Poh, W.T., Veeravalli, L., Chan, C.S., Lim, S.S., Leong, S.T., Neo, S.C., Choi, P.S., Chew, E.G., Nagarajan, N., Jacques, P.E., So, J.B., Ruan, X., Yeoh, K.G., Tan, P., Sung, W.K., Hunziker, W., Ruan, Y. and Hillmer, A.M. (2015) Recurrent Fusion Genes in Gastric Cancer: Cldn18-Arhgap26 Induces Loss of Epi-thelial Integrity. Cell Reports, 12, 272-285.
https://doi.org/10.1016/j.celrep.2015.06.020
|
[19]
|
Baek, J.H., Park, D.J., Kim, G.Y., et al. (2019) Clinical Implica-tions of Claudin18.2 Expression in Patients with Gastric Cancer. Anticancer Research, 39, 6973-6979. https://doi.org/10.21873/anticanres.13919
|
[20]
|
Tanaka, A., Ishikawa, S., Ushiku, T., Yamazawa, S., Katoh, H., Hayashi, A., Kunita, A. and Fukayama, M. (2018) Frequent Cldn18-Arhgap Fusion in Highly Metastatic Diffuse-Type Gastric Cancer with Relatively Early Onset. Oncotarget, 9, 29336-29350. https://doi.org/10.18632/oncotarget.25464
|
[21]
|
Khokha, R., Murthy A. and Weiss, A. (2013) Metalloproteinases and Their Natural Inhibitors in Inflammation and Immunity. Nature Reviews Immunology, 13, 649-665. https://doi.org/10.1038/nri3499
|
[22]
|
Klein, T. and Bischoff, R. (2011) Physiology and Pathophysiology of Matrix Metalloproteases. Amino Acids, 41, 271-290. https://doi.org/10.1007/s00726-010-0689-x
|
[23]
|
Bonnans, C., Chou, J. and Werb, Z. (2014) Remodeling the Extracellular Matrix in Development and Disease. Nature Reviews Molecular Cell Biology, 15, 786-801. https://doi.org/10.1038/nrm3904
|
[24]
|
Butler, G.S. and Overall, C.M. (2009) Proteomic Identification of Multitasking Proteins in Unexpected Locations Complicates Drug Targeting. Nature Reviews Drug Dis-covery, 8, 935-948. https://doi.org/10.1038/nrd2945
|
[25]
|
Khokha, R., Murthy A. and Weiss, A. (2013) Metallo-proteinases and Their Natural Inhibitors in Inflammation and Immunity. Nature Reviews Immunology, 13, 649-665. https://doi.org/10.1038/nri3499
|
[26]
|
Overall, C.M. (2001) Matrix Metalloproteinase Substrate Binding Domains, Modules and Exosites. Overview and Experimental Strategies. Methods in Molecular Biology, 151, 79-120.
|
[27]
|
Overall, C.M. and Butler, G.S. (2007) Protease Yoga: Extreme Flexibility of a Matrix Metalloproteinase. Structure, 15, 1159-1161. https://doi.org/10.1016/j.str.2007.10.001
|
[28]
|
Jobin, P.G., Butler, G.S. and Overall, C.M. (2017) New Intracellular Activities of Matrix Metalloproteinases Shine in the Moonlight. Biochimica et Biophysica Acta—Molecular Cell Research, 1864, 2043-2055.
https://doi.org/10.1016/j.bbamcr.2017.05.013
|
[29]
|
Huang, H. (2018) Matrix Metalloproteinase-9 (MMP-9) as a Cancer Biomarker and MMP-9 Biosensors: Recent Advances. Sensors, 18, Article No. 3249. https://doi.org/10.3390/s18103249
|
[30]
|
Hou, H., Zhang, G., Wang, H., Gong, H., Wang, C. and Zhang, X. (2014) High Matrix Metalloproteinase-9 Expression Induces Angiogenesis and Basement Membrane Degradation in Stroke-Prone Spontaneously Hypertensive Rats after Cerebral Infarction. Neural Regeneration Research, 9, 1154-1162. https://doi.org/10.4103/1673-5374.135318
|
[31]
|
董刚强, 王永占, 蒲红, 岳光平. 基质金属蛋白酶MMP-9在胃癌中的表达及其临床意义[J]. 肿瘤预防与治疗, 2012, 25(4): 240-242.
|
[32]
|
Chu, D., Zhang, Z., Li, Y., et al. (2011) Matrix Metalloproteinase-9 Is Associated with Disease-Free Survival and Overall Survival in Patients with Gas-tric Cancer. International Journal of Cancer, 129, 887-895.
https://doi.org/10.1002/ijc.25734
|