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http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/88289完整後設資料紀錄
| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 廖泰慶 | zh_TW |
| dc.contributor.advisor | Albert Tai-Ching Liao | en |
| dc.contributor.author | 楊書亞 | zh_TW |
| dc.contributor.author | Shu-Yia Yang | en |
| dc.date.accessioned | 2023-08-09T16:23:15Z | - |
| dc.date.available | 2023-11-09 | - |
| dc.date.copyright | 2023-08-09 | - |
| dc.date.issued | 2023 | - |
| dc.date.submitted | 2023-07-25 | - |
| dc.identifier.citation | Adan, A., Kiraz, Y., & Baran, Y. (2016). Cell Proliferation and Cytotoxicity Assays. Curr Pharm Biotechnol, 17(14), 1213-1221.
2. Archer, C. W., Morrison, H., & Pitsillides, A. A. (1994). Cellular aspects of the development of diarthrodial joints and articular cartilage. J Anat, 184 ( Pt 3)(Pt 3), 447-456. 3. Aresu, L., Arico, A., Comazzi, S., Gelain, M. E., Riondato, F., Mortarino, M., Morello, E., Stefanello, D., & Castagnaro, M. (2014). VEGF and MMP-9: biomarkers for canine lymphoma. Vet Comp Oncol, 12(1), 29-36. 4. Ballegeer, E. A., Hollinger, C., & Kunst, C. M. (2013). Imaging diagnosis-multicentric lymphoma of granular lymphocytes imaged with FDG PET/CT in a dog. Vet Radiol Ultrasound, 54(1), 75-80. 5. Below, J., & J, M. D. (2023). Vincristine. In StatPearls. 6. Bergmann, O. J., Johansen, J. S., Klausen, T. W., Mylin, A. K., Kristensen, J. S., Kjeldsen, E., & Johnsen, H. E. (2005). High serum concentration of YKL-40 is associated with short survival in patients with acute myeloid leukemia. Clin Cancer Res, 11(24 Pt 1), 8644-8652. 7. Berntsen, A., Trepiakas, R., Wenandy, L., Geertsen, P. F., thor Straten, P., Andersen, M. H., Pedersen, A. E., Claesson, M. H., Lorentzen, T., Johansen, J. S., & Svane, I. M. (2008). Therapeutic dendritic cell vaccination of patients with metastatic renal cell carcinoma: a clinical phase 1/2 trial. J Immunother, 31(8), 771-780. 8. Bi, J., Lau, S. H., Lv, Z. L., Xie, D., Li, W., Lai, Y. R., Zhong, J. M., Wu, H. Q., Su, Q., He, Y. L., Zhan, W. H., Wen, J. M., & Guan, X. Y. (2009). Overexpression of YKL-40 is an independent prognostic marker in gastric cancer. Hum Pathol, 40(12), 1790-1797. 9. Biggar, R. J., Johansen, J. S., Smedby, K. E., Rostgaard, K., Chang, E. T., Adami, H. O., Glimelius, B., Molin, D., Hamilton-Dutoit, S., Melbye, M., & Hjalgrim, H. (2008). Serum YKL-40 and interleukin 6 levels in Hodgkin lymphoma. Clin Cancer Res, 14(21), 6974-6978. 10. Boerkamp, K. M., Teske, E., Boon, L. R., Grinwis, G. C., van den Bossche, L., & Rutteman, G. R. (2014). Estimated incidence rate and distribution of tumours in 4,653 cases of archival submissions derived from the Dutch golden retriever population. BMC Vet Res, 10, 34. 11. Burnett, R. C., Vernau, W., Modiano, J. F., Olver, C. S., Moore, P. F., & Avery, A. C. (2003). Diagnosis of canine lymphoid neoplasia using clonal rearrangements of antigen receptor genes. Vet Pathol, 40(1), 32-41. 12. Chen, C. C., Pekow, J., Llado, V., Kanneganti, M., Lau, C. W., Mizoguchi, A., Mino-Kenudson, M., Bissonnette, M., & Mizoguchi, E. (2011). Chitinase 3-like-1 expression in colonic epithelial cells as a potentially novel marker for colitis-associated neoplasia. Am J Pathol, 179(3), 1494-1503. 13. Chen, H. Y., Zhou, Z. Y., Luo, Y. L., Luo, Q., & Fan, J. T. (2021). Knockdown of YKL-40 inhibits angiogenesis through regulation of VEGF/VEGFR2 and ERK1/2 signaling in endometrial cancer. Cell Biol Int, 45(12), 2557-2566. 14. Chen, Y., Zhang, S., Wang, Q., & Zhang, X. (2017). Tumor-recruited M2 macrophages promote gastric and breast cancer metastasis via M2 macrophage-secreted CHI3L1 protein. J Hematol Oncol, 10(1), 36. 15. Cheng, K. C., Lee, J. J., Wang, S. L., Lin, C. Y., Tseng, C. T., Lin, C. S., & Liao, A. T. (2019). Elevated plasma YKL-40 level is found in the dogs with cancer and is related to poor prognosis. J Vet Sci, 20(5), e53. 16. Chupp, G. L., Lee, C. G., Jarjour, N., Shim, Y. M., Holm, C. T., He, S., Dziura, J. D., Reed, J., Coyle, A. J., Kiener, P., Cullen, M., Grandsaigne, M., Dombret, M. C., Aubier, M., Pretolani, M., & Elias, J. A. (2007). A chitinase-like protein in the lung and circulation of patients with severe asthma. N Engl J Med, 357(20), 2016-2027. 17. Cintin, C., Johansen, J. S., Christensen, I. J., Price, P. A., Sorensen, S., & Nielsen, H. J. (1999). Serum YKL-40 and colorectal cancer. Br J Cancer, 79(9-10), 1494-1499. 18. Coyle, K. A., & Steinberg, H. (2004). Characterization of lymphocytes in canine gastrointestinal lymphoma. Vet Pathol, 41(2), 141-146. 19. Crabtree, A. C., Spangler, E., Beard, D., & Smith, A. (2010). Diagnostic accuracy of gray-scale ultrasonography for the detection of hepatic and splenic lymphoma in dogs. Vet Radiol Ultrasound, 51(6), 661-664. 20. Day, M. J., Pearson, G. R., Lucke, V. M., Lane, S. J., & Sparks, R. S. (1996). Lesions associated with mineral deposition in the lymph node and lung of the dog. Vet Pathol, 33(1), 29-42. 21. Dehn, H., Hogdall, E. V., Johansen, J. S., Jorgensen, M., Price, P. A., Engelholm, S. A., & Hogdall, C. K. (2003). Plasma YKL-40, as a prognostic tumor marker in recurrent ovarian cancer. Acta Obstet Gynecol Scand, 82(3), 287-293. 22. Di Rosa, M., Tibullo, D., Saccone, S., Distefano, G., Basile, M. S., Di Raimondo, F., & Malaguarnera, L. (2016). CHI3L1 nuclear localization in monocyte derived dendritic cells. Immunobiology, 221(2), 347-356. 23. Diefenbach, C. S., Shah, Z., Iasonos, A., Barakat, R. R., Levine, D. A., Aghajanian, C., Sabbatini, P., Hensley, M. L., Konner, J., Tew, W., Spriggs, D., Fleisher, M., Thaler, H., & Dupont, J. (2007). Preoperative serum YKL-40 is a marker for detection and prognosis of endometrial cancer. Gynecol Oncol, 104(2), 435-442. 24. Dobson, J. M. (2013). Breed-predispositions to cancer in pedigree dogs. ISRN Vet Sci, 2013, 941275. 25. Dorn, C. R., Taylor, D. O., Schneider, R., Hibbard, H. H., & Klauber, M. R. (1968). Survey of animal neoplasms in Alameda and Contra Costa Counties, California. II. Cancer morbidity in dogs and cats from Alameda County. J Natl Cancer Inst, 40(2), 307-318. 26. Elmore, S. (2007). Apoptosis: a review of programmed cell death. Toxicol Pathol, 35(4), 495-516. 27. Fan, T. M. (2003). Lymphoma updates. Vet Clin North Am Small Anim Pract, 33(3), 455-471. 28. Feitelson, M. A., Arzumanyan, A., Kulathinal, R. J., Blain, S. W., Holcombe, R. F., Mahajna, J., Marino, M., Martinez-Chantar, M. L., Nawroth, R., Sanchez-Garcia, I., Sharma, D., Saxena, N. K., Singh, N., Vlachostergios, P. J., Guo, S., Honoki, K., Fujii, H., Georgakilas, A. G., Bilsland, A., Amedei, A., Niccolai, E., Amin, A., Ashraf, S. S., Boosani, C. S., Guha, G., Ciriolo, M. R., Aquilano, K., Chen, S., Mohammed, S. I., Azmi, A. S., Bhakta, D., Halicka, D., Keith, W. N., & Nowsheen, S. (2015). Sustained proliferation in cancer: Mechanisms and novel therapeutic targets. Semin Cancer Biol, 35 Suppl(Suppl), S25-S54. 29. Fournel-Fleury, C., Ponce, F., Felman, P., Blavier, A., Bonnefont, C., Chabanne, L., Marchal, T., Cadore, J. L., Goy-Thollot, I., Ledieu, D., Ghernati, I., & Magnol, J. P. (2002). Canine T-cell lymphomas: a morphological, immunological, and clinical study of 46 new cases. Vet Pathol, 39(1), 92-109. 30. Francescone, R. A., Scully, S., Faibish, M., Taylor, S. L., Oh, D., Moral, L., Yan, W., Bentley, B., & Shao, R. (2011). Role of YKL-40 in the angiogenesis, radioresistance, and progression of glioblastoma. J Biol Chem, 286(17), 15332-15343. 31. Friedl, P., & Wolf, K. (2003). Tumour-cell invasion and migration: diversity and escape mechanisms. Nat Rev Cancer, 3(5), 362-374. 32. Fuksiewicz, M., Kotowicz, B., Rutkowski, A., Achinger-Kawecka, J., Wagrodzki, M., & Kowalska, M. M. (2018). The Assessment of Clinical Usage and Prognostic Value of YKL-40 Serum Levels in Patients With Rectal Cancer Without Distant Metastasis. Technol Cancer Res Treat, 17, 1533033818765209. 33. Gavazza, A., Lubas, G., Valori, E., & Gugliucci, B. (2008). Retrospective survey of malignant lymphoma cases in the dog: clinical, therapeutical and prognostic features. Vet Res Commun, 32 Suppl 1, S291-293. 34. Geng, B., Pan, J., Zhao, T., Ji, J., Zhang, C., Che, Y., Yang, J., Shi, H., Li, J., Zhou, H., Mu, X., Xu, C., Wang, C., Xu, Y., Liu, Z., Wen, H., & You, Q. (2018). Chitinase 3-like 1-CD44 interaction promotes metastasis and epithelial-to-mesenchymal transition through beta-catenin/Erk/Akt signaling in gastric cancer. J Exp Clin Cancer Res, 37(1), 208. 35. Hakala, B. E., White, C., & Recklies, A. D. (1993). Human cartilage gp-39, a major secretory product of articular chondrocytes and synovial cells, is a mammalian member of a chitinase protein family. J Biol Chem, 268(34), 25803-25810. 36. Hanahan, D., & Weinberg, R. A. (2011). Hallmarks of cancer: the next generation. Cell, 144(5), 646-674. 37. Hao, H., Chen, H., Xie, L., & Liu, H. (2021). YKL-40 promotes invasion and metastasis of bladder cancer by regulating epithelial mesenchymal transition. Ann Med, 53(1), 1170-1178. 38. Hao, H., Chen, H., Xie, L., Liu, H., & Wang, D. (2021). LncRNA KCNQ1OT1 Promotes Proliferation, Invasion and Metastasis of Prostate Cancer by Regulating miR-211-5p/CHI3L1 Pathway. Onco Targets Ther, 14, 1659-1671. 39. Hao, H., Wang, L., Chen, H., Xie, L., Bai, T., Liu, H., & Wang, D. (2017). YKL-40 promotes the migration and invasion of prostate cancer cells by regulating epithelial mesenchymal transition. Am J Transl Res, 9(8), 3749-3757. 40. Harvey, S., Weisman, M., O'Dell, J., Scott, T., Krusemeier, M., Visor, J., & Swindlehurst, C. (1998). Chondrex: new marker of joint disease. Clin Chem, 44(3), 509-516. 41. He, C. H., Lee, C. G., Dela Cruz, C. S., Lee, C. M., Zhou, Y., Ahangari, F., Ma, B., Herzog, E. L., Rosenberg, S. A., Li, Y., Nour, A. M., Parikh, C. R., Schmidt, I., Modis, Y., Cantley, L., & Elias, J. A. (2013). Chitinase 3-like 1 regulates cellular and tissue responses via IL-13 receptor alpha2. Cell Rep, 4(4), 830-841. 42. Huang, W. H., Liao, A. T., Chu, P. Y., Zhai, S. H., Yen, I. F., & Liu, C. H. (2017). A 3-year surveillance on causes of death or reasons for euthanasia of domesticated dogs in Taiwan. Prev Vet Med, 147, 1-10. 43. Itik, V., Kemik, O., Kemik, A., Dulger, A. C., Sumer, A., Soyoral, Y. U., Begenik, H., Purisa, S., & Kotan, C. (2011). Serum YKL-40 Levels in Patients with Gastric Cancer. Biomark Cancer, 3, 25-30. 44. Ito, D., Frantz, A. M., & Modiano, J. F. (2014). Canine lymphoma as a comparative model for human non-Hodgkin lymphoma: recent progress and applications. Vet Immunol Immunopathol, 159(3-4), 192-201. 45. Iwamoto, F. M., Hottinger, A. F., Karimi, S., Riedel, E., Dantis, J., Jahdi, M., Panageas, K. S., Lassman, A. B., Abrey, L. E., Fleisher, M., DeAngelis, L. M., Holland, E. C., & Hormigo, A. (2011). Serum YKL-40 is a marker of prognosis and disease status in high-grade gliomas. Neuro Oncol, 13(11), 1244-1251. 46. Jafari-Nakhjavani, M. R., Ghorbanihaghjo, A., Bagherzadeh-Nobari, B., Malek-Mahdavi, A., & Rashtchizadeh, N. (2019). Serum YKL-40 levels and disease characteristics in patients with rheumatoid arthritis. Caspian J Intern Med, 10(1), 92-97. 47. Jeet, V., Tevz, G., Lehman, M., Hollier, B., & Nelson, C. (2014). Elevated YKL40 is associated with advanced prostate cancer (PCa) and positively regulates invasion and migration of PCa cells. Endocr Relat Cancer, 21(5), 723-737. 48. Jefri, M., Huang, Y. N., Huang, W. C., Tai, C. S., & Chen, W. L. (2015). YKL-40 regulated epithelial-mesenchymal transition and migration/invasion enhancement in non-small cell lung cancer. BMC Cancer, 15, 590. 49. Jensen, B. V., Johansen, J. S., & Price, P. A. (2003). High levels of serum HER-2/neu and YKL-40 independently reflect aggressiveness of metastatic breast cancer. Clin Cancer Res, 9(12), 4423-4434. 50. Johansen, J. S., Christensen, I. J., Jorgensen, L. N., Olsen, J., Rahr, H. B., Nielsen, K. T., Laurberg, S., Brunner, N., & Nielsen, H. J. (2015). Serum YKL-40 in risk assessment for colorectal cancer: a prospective study of 4,496 subjects at risk of colorectal cancer. Cancer Epidemiol Biomarkers Prev, 24(3), 621-626. 51. Johansen, J. S., Jensen, B. V., Roslind, A., Nielsen, D., & Price, P. A. (2006). Serum YKL-40, a new prognostic biomarker in cancer patients? Cancer Epidemiol Biomarkers Prev, 15(2), 194-202. 52. Johansen, J. S., Olee, T., Price, P. A., Hashimoto, S., Ochs, R. L., & Lotz, M. (2001). Regulation of YKL-40 production by human articular chondrocytes. Arthritis Rheum, 44(4), 826-837. 53. Johansen, J. S., Schultz, N. A., & Jensen, B. V. (2009). Plasma YKL-40: a potential new cancer biomarker? Future Oncol, 5(7), 1065-1082. 54. Johansen, J. S., Williamson, M. K., Rice, J. S., & Price, P. A. (1992). Identification of proteins secreted by human osteoblastic cells in culture. J Bone Miner Res, 7(5), 501-512. 55. Junker, N., Johansen, J. S., Andersen, C. B., & Kristjansen, P. E. (2005). Expression of YKL-40 by peritumoral macrophages in human small cell lung cancer. Lung Cancer, 48(2), 223-231. 56. Jurikova, M., Danihel, L., Polak, S., & Varga, I. (2016). Ki67, PCNA, and MCM proteins: Markers of proliferation in the diagnosis of breast cancer. Acta Histochem, 118(5), 544-552. 57. Justus, C. R., Leffler, N., Ruiz-Echevarria, M., & Yang, L. V. (2014). In vitro cell migration and invasion assays. J Vis Exp(88). 58. Kahramanoglu, I., Tokgozoglu, N., Turan, H., Sal, V., Simsek, G., Gelisgen, R., Bese, T., Demirkiran, F., Arvas, M., & Uzun, H. (2018). YKL-40 in the diagnosis, prediction of prognosis, and platinum sensitivity in serous epithelial ovarian cancer. Turk J Obstet Gynecol, 15(3), 177-181. 59. Kawada, M., Seno, H., Kanda, K., Nakanishi, Y., Akitake, R., Komekado, H., Kawada, K., Sakai, Y., Mizoguchi, E., & Chiba, T. (2012). Chitinase 3-like 1 promotes macrophage recruitment and angiogenesis in colorectal cancer. Oncogene, 31(26), 3111-3123. 60. Kjaergaard, A. D., Chen, I. M., Johansen, A. Z., Nordestgaard, B. G., Bojesen, S. E., & Johansen, J. S. (2021). Inflammatory Biomarker Score Identifies Patients with Six-Fold Increased Risk of One-Year Mortality after Pancreatic Cancer. Cancers (Basel), 13(18). 61. Konradsen, J. R., James, A., Nordlund, B., Reinius, L. E., Soderhall, C., Melen, E., Wheelock, A. M., Lodrup Carlsen, K. C., Lidegran, M., Verhoek, M., Boot, R. G., Dahlen, B., Dahlen, S. E., & Hedlin, G. (2013). The chitinase-like protein YKL-40: a possible biomarker of inflammation and airway remodeling in severe pediatric asthma. J Allergy Clin Immunol, 132(2), 328-335 e325. 62. Kotowicz, B., Fuksiewicz, M., Jonska-Gmyrek, J., Wagrodzki, M., & Kowalska, M. (2017). Preoperative serum levels of YKL 40 and CA125 as a prognostic indicators in patients with endometrial cancer. Eur J Obstet Gynecol Reprod Biol, 215, 141-147. 63. Kramer, N., Walzl, A., Unger, C., Rosner, M., Krupitza, G., Hengstschlager, M., & Dolznig, H. (2013). In vitro cell migration and invasion assays. Mutat Res, 752(1), 10-24. 64. Ku, B. M., Lee, Y. K., Ryu, J., Jeong, J. Y., Choi, J., Eun, K. M., Shin, H. Y., Kim, D. G., Hwang, E. M., Yoo, J. C., Park, J. Y., Roh, G. S., Kim, H. J., Cho, G. J., Choi, W. S., Paek, S. H., & Kang, S. S. (2011). CHI3L1 (YKL-40) is expressed in human gliomas and regulates the invasion, growth and survival of glioma cells. Int J Cancer, 128(6), 1316-1326. 65. Kumari, R., Chouhan, S., Singh, S., Chhipa, R. R., Ajay, A. K., & Bhat, M. K. (2017). Constitutively activated ERK sensitizes cancer cells to doxorubicin: Involvement of p53-EGFR-ERK pathway. J Biosci, 42(1), 31-41. 66. Kzhyshkowska, J., Mamidi, S., Gratchev, A., Kremmer, E., Schmuttermaier, C., Krusell, L., Haus, G., Utikal, J., Schledzewski, K., Scholtze, J., & Goerdt, S. (2006). Novel stabilin-1 interacting chitinase-like protein (SI-CLP) is up-regulated in alternatively activated macrophages and secreted via lysosomal pathway. Blood, 107(8), 3221-3228. 67. Lee, C. G., Hartl, D., Lee, G. R., Koller, B., Matsuura, H., Da Silva, C. A., Sohn, M. H., Cohn, L., Homer, R. J., Kozhich, A. A., Humbles, A., Kearley, J., Coyle, A., Chupp, G., Reed, J., Flavell, R. A., & Elias, J. A. (2009). Role of breast regression protein 39 (BRP-39)/chitinase 3-like-1 in Th2 and IL-13-induced tissue responses and apoptosis. J Exp Med, 206(5), 1149-1166. 68. Lee, C. M., He, C. H., Nour, A. M., Zhou, Y., Ma, B., Park, J. W., Kim, K. H., Dela Cruz, C., Sharma, L., Nasr, M. L., Modis, Y., Lee, C. G., & Elias, J. A. (2016). IL-13Ralpha2 uses TMEM219 in chitinase 3-like-1-induced signalling and effector responses. Nat Commun, 7, 12752. 69. Lee, M. S., Park, W. S., Kim, Y. H., Ahn, W. G., Kwon, S. H., & Her, S. (2012). Intracellular ATP assay of live cells using PTD-conjugated luciferase. Sensors (Basel), 12(11), 15628-15637. 70. Libreros, S., & Iragavarapu-Charyulu, V. (2015). YKL-40/CHI3L1 drives inflammation on the road of tumor progression. J Leukoc Biol, 98(6), 931-936. 71. Ligasova, A., Frydrych, I., & Koberna, K. (2023). Basic Methods of Cell Cycle Analysis. Int J Mol Sci, 24(4). 72. Ling, H., & Recklies, A. D. (2004). The chitinase 3-like protein human cartilage glycoprotein 39 inhibits cellular responses to the inflammatory cytokines interleukin-1 and tumour necrosis factor-alpha. Biochem J, 380(Pt 3), 651-659. 73. Liu, K., Jin, M., Ye, S., & Yan, S. (2020). CHI3L1 promotes proliferation and improves sensitivity to cetuximab in colon cancer cells by down-regulating p53. J Clin Lab Anal, 34(1), e23026. 74. Liu, S., Yang, W., Li, Y., & Sun, C. (2023). Fetal bovine serum, an important factor affecting the reproducibility of cell experiments. Sci Rep, 13(1), 1942. 75. Lugowska, I., Kowalska, M., Fuksiewicz, M., Kotowicz, B., Mierzejewska, E., Kosela-Paterczyk, H., Szamotulska, K., & Rutkowski, P. (2015). Serum markers in early-stage and locally advanced melanoma. Tumour Biol, 36(11), 8277-8285. 76. Martelli, M., Ferreri, A. J., Agostinelli, C., Di Rocco, A., Pfreundschuh, M., & Pileri, S. A. (2013). Diffuse large B-cell lymphoma. Crit Rev Oncol Hematol, 87(2), 146-171. 77. Matsumoto, T., & Tsurumoto, T. (2001). Serum YKL-40 levels in rheumatoid arthritis: correlations between clinical and laborarory parameters. Clin Exp Rheumatol, 19(6), 655-660. 78. Meredith, A. M., & Dass, C. R. (2016). Increasing role of the cancer chemotherapeutic doxorubicin in cellular metabolism. J Pharm Pharmacol, 68(6), 729-741. 79. Michelsen, A. E., Rathcke, C. N., Skjelland, M., Holm, S., Ranheim, T., Krohg-Sorensen, K., Klingvall, M. F., Brosstad, F., Oie, E., Vestergaard, H., Aukrust, P., & Halvorsen, B. (2010). Increased YKL-40 expression in patients with carotid atherosclerosis. Atherosclerosis, 211(2), 589-595. 80. Mitsuhashi, A., Matsui, H., Usui, H., Nagai, Y., Tate, S., Unno, Y., Hirashiki, K., Seki, K., & Shozu, M. (2009). Serum YKL-40 as a marker for cervical adenocarcinoma. Ann Oncol, 20(1), 71-77. 81. Miura, T., Maruyama, H., Sakai, M., Takahashi, T., Koie, H., Yamaya, Y., Shibuya, H., Sato, T., Watari, T., Tokuriki, M., & Hasegawa, A. (2004). Endoscopic findings on alimentary lymphoma in 7 dogs. J Vet Med Sci, 66(5), 577-580. 82. Mizoguchi, E. (2006). Chitinase 3-like-1 exacerbates intestinal inflammation by enhancing bacterial adhesion and invasion in colonic epithelial cells. Gastroenterology, 130(2), 398-411. 83. Mohanty, A. K., Singh, G., Paramasivam, M., Saravanan, K., Jabeen, T., Sharma, S., Yadav, S., Kaur, P., Kumar, P., Srinivasan, A., & Singh, T. P. (2003). Crystal structure of a novel regulatory 40-kDa mammary gland protein (MGP-40) secreted during involution. J Biol Chem, 278(16), 14451-14460. 84. Moore, A. S. (2016). Treatment of T cell lymphoma in dogs. Vet Rec, 179(11), 277. 85. Moore, E. L., Vernau, W., Rebhun, R. B., Skorupski, K. A., & Burton, J. H. (2018). Patient characteristics, prognostic factors and outcome of dogs with high-grade primary mediastinal lymphoma. Vet Comp Oncol, 16(1), E45-E51. 86. Morera, E., Steinhauser, S. S., Budkova, Z., Ingthorsson, S., Kricker, J., Krueger, A., Traustadottir, G. A., & Gudjonsson, T. (2019). YKL-40/CHI3L1 facilitates migration and invasion in HER2 overexpressing breast epithelial progenitor cells and generates a niche for capillary-like network formation. In Vitro Cell Dev Biol Anim, 55(10), 838-853. 87. Mylin, A. K., Abildgaard, N., Johansen, J. S., Heickendorff, L., Kreiner, S., Waage, A., Turesson, I., Gimsing, P., & Nordic Myeloma Study, G. (2015). Serum YKL-40: a new independent prognostic marker for skeletal complications in patients with multiple myeloma. Leuk Lymphoma, 56(9), 2650-2659. 88. Nielsen, M. C., Andersen, M. N., & Moller, H. J. (2020). Monocyte isolation techniques significantly impact the phenotype of both isolated monocytes and derived macrophages in vitro. Immunology, 159(1), 63-74. 89. Nishikawa, K. C., & Millis, A. J. (2003). gp38k (CHI3L1) is a novel adhesion and migration factor for vascular cells. Exp Cell Res, 287(1), 79-87. 90. Nitiss, J. L. (2009). Targeting DNA topoisomerase II in cancer chemotherapy. Nat Rev Cancer, 9(5), 338-350. 91. Nojgaard, C., Johansen, J. S., Christensen, E., Skovgaard, L. T., Price, P. A., Becker, U., & Group, E. (2003). Serum levels of YKL-40 and PIIINP as prognostic markers in patients with alcoholic liver disease. J Hepatol, 39(2), 179-186. 92. Patnaik, A. K., Hurvitz, A. I., & Johnson, G. F. (1977). Canine gastrointestinal neoplasms. Vet Pathol, 14(6), 547-555. 93. Pelloski, C. E., Mahajan, A., Maor, M., Chang, E. L., Woo, S., Gilbert, M., Colman, H., Yang, H., Ledoux, A., Blair, H., Passe, S., Jenkins, R. B., & Aldape, K. D. (2005). YKL-40 expression is associated with poorer response to radiation and shorter overall survival in glioblastoma. Clin Cancer Res, 11(9), 3326-3334. 94. Perry, J. A., Thamm, D. H., Eickhoff, J., Avery, A. C., & Dow, S. W. (2011). Increased monocyte chemotactic protein-1 concentration and monocyte count independently associate with a poor prognosis in dogs with lymphoma. Vet Comp Oncol, 9(1), 55-64. 95. Pijuan, J., Barcelo, C., Moreno, D. F., Maiques, O., Siso, P., Marti, R. M., Macia, A., & Panosa, A. (2019). In vitro Cell Migration, Invasion, and Adhesion Assays: From Cell Imaging to Data Analysis. Front Cell Dev Biol, 7, 107. 96. Ponce, F., Marchal, T., Magnol, J. P., Turinelli, V., Ledieu, D., Bonnefont, C., Pastor, M., Delignette, M. L., & Fournel-Fleury, C. (2010). A morphological study of 608 cases of canine malignant lymphoma in France with a focus on comparative similarities between canine and human lymphoma morphology. Vet Pathol, 47(3), 414-433. 97. Rathcke, C. N., Johansen, J. S., & Vestergaard, H. (2006). YKL-40, a biomarker of inflammation, is elevated in patients with type 2 diabetes and is related to insulin resistance. Inflamm Res, 55(2), 53-59. 98. Rawat, P. S., Jaiswal, A., Khurana, A., Bhatti, J. S., & Navik, U. (2021). Doxorubicin-induced cardiotoxicity: An update on the molecular mechanism and novel therapeutic strategies for effective management. Biomed Pharmacother, 139, 111708. 99. Recklies, A. D., White, C., & Ling, H. (2002). The chitinase 3-like protein human cartilage glycoprotein 39 (HC-gp39) stimulates proliferation of human connective-tissue cells and activates both extracellular signal-regulated kinase- and protein kinase B-mediated signalling pathways. Biochem J, 365(Pt 1), 119-126. 100. Rehli, M., Krause, S. W., & Andreesen, R. (1997). Molecular characterization of the gene for human cartilage gp-39 (CHI3L1), a member of the chitinase protein family and marker for late stages of macrophage differentiation. Genomics, 43(2), 221-225. 101. Richards, K. L., & Suter, S. E. (2015). Man's best friend: what can pet dogs teach us about non-Hodgkin's lymphoma? Immunol Rev, 263(1), 173-191. 102. Rutgen, B. C., Hammer, S. E., Gerner, W., Christian, M., de Arespacochaga, A. G., Willmann, M., Kleiter, M., Schwendenwein, I., & Saalmuller, A. (2010). Establishment and characterization of a novel canine B-cell line derived from a spontaneously occurring diffuse large cell lymphoma. Leuk Res, 34(7), 932-938. 103. Saellstrom, S., Sharif, H., Jagarlamudi, K. K., Ronnberg, H., Wang, L., & Eriksson, S. (2022). Serum TK1 protein and C-reactive protein correlate to treatment response and predict survival in dogs with hematologic malignancies. Res Vet Sci, 145, 213-221. 104. Schmidt, H., Johansen, J. S., Gehl, J., Geertsen, P. F., Fode, K., & von der Maase, H. (2006). Elevated serum level of YKL-40 is an independent prognostic factor for poor survival in patients with metastatic melanoma. Cancer, 106(5), 1130-1139. 105. Schultz, N. A., & Johansen, J. S. (2010). YKL-40-A Protein in the Field of Translational Medicine: A Role as a Biomarker in Cancer Patients? Cancers (Basel), 2(3), 1453-1491. 106. Shackelton, L. M., Mann, D. M., & Millis, A. J. (1995). Identification of a 38-kDa heparin-binding glycoprotein (gp38k) in differentiating vascular smooth muscle cells as a member of a group of proteins associated with tissue remodeling. J Biol Chem, 270(22), 13076-13083. 107. Shao, R., Hamel, K., Petersen, L., Cao, Q. J., Arenas, R. B., Bigelow, C., Bentley, B., & Yan, W. (2009). YKL-40, a secreted glycoprotein, promotes tumor angiogenesis. Oncogene, 28(50), 4456-4468. 108. Sánchez, D., Sánchez-Verin, R., Corona, H., Gutiérrez, A., Núñez-Ochoa, L., Paredes, J., & Cesarman-Maus, G. (2019). Canine lymphoma: Pathological and clinical characteristics of patients treated at a referral hospital. Veterinaria México OA, 6(2). 109. Suzuki, H., Boki, H., Kamijo, H., Nakajima, R., Oka, T., Shishido-Takahashi, N., Suga, H., Sugaya, M., Sato, S., & Miyagaki, T. (2020). YKL-40 Promotes Proliferation of Cutaneous T-Cell Lymphoma Tumor Cells through Extracellular Signal-Regulated Kinase Pathways. J Invest Dermatol, 140(4), 860-868 e863. 110. Teske, E. (1994). Canine malignant lymphoma: a review and comparison with human non-Hodgkin's lymphoma. Vet Q, 16(4), 209-219. 111. Thamm, D. H. (2019). Novel Treatments for Lymphoma. Vet Clin North Am Small Anim Pract, 49(5), 903-915. 112. Thongsom, S., Chaocharoen, W., Silsirivanit, A., Wongkham, S., Sripa, B., Choe, H., Suginta, W., & Talabnin, C. (2016). YKL-40/chitinase-3-like protein 1 is associated with poor prognosis and promotes cell growth and migration of cholangiocarcinoma. Tumour Biol, 37(7), 9451-9463. 113. Thorn, C. F., Oshiro, C., Marsh, S., Hernandez-Boussard, T., McLeod, H., Klein, T. E., & Altman, R. B. (2011). Doxorubicin pathways: pharmacodynamics and adverse effects. Pharmacogenet Genomics, 21(7), 440-446. 114. Umeki, S., Ema, Y., Suzuki, R., Kubo, M., Hayashi, T., Okamura, Y., Yamazaki, J., Tsujimoto, H., Tani, K., Hiraoka, H., Okuda, M., & Mizuno, T. (2013). Establishment of five canine lymphoma cell lines and tumor formation in a xenotransplantation model. J Vet Med Sci, 75(4), 467-474. 115. Vaananen, T., Kallio, J., Vuolteenaho, K., Ojala, A., Luukkaala, T., Hamalainen, M., Tammela, T., Kellokumpu-Lehtinen, P. L., & Moilanen, E. (2017). High YKL-40 is associated with poor survival in patients with renal cell carcinoma: a novel independent prognostic marker. Scand J Urol, 51(5), 367-372. 116. Valli, V. E., San Myint, M., Barthel, A., Bienzle, D., Caswell, J., Colbatzky, F., Durham, A., Ehrhart, E. J., Johnson, Y., Jones, C., Kiupel, M., Labelle, P., Lester, S., Miller, M., Moore, P., Moroff, S., Roccabianca, P., Ramos-Vara, J., Ross, A., Scase, T., Tvedten, H., & Vernau, W. (2011). Classification of canine malignant lymphomas according to the World Health Organization criteria. Vet Pathol, 48(1), 198-211. 117. Valli, V. E., Vernau, W., de Lorimier, L. P., Graham, P. S., & Moore, P. F. (2006). Canine indolent nodular lymphoma. Vet Pathol, 43(3), 241-256. 118. Vermeulen, J., De Preter, K., Lefever, S., Nuytens, J., De Vloed, F., Derveaux, S., Hellemans, J., Speleman, F., & Vandesompele, J. (2011). Measurable impact of RNA quality on gene expression results from quantitative PCR. Nucleic Acids Res, 39(9), e63. 119. Vezzali, E., Parodi, A. L., Marcato, P. S., & Bettini, G. (2010). Histopathologic classification of 171 cases of canine and feline non-Hodgkin lymphoma according to the WHO. Vet Comp Oncol, 8(1), 38-49. 120. Vos, K., Steenbakkers, P., Miltenburg, A. M., Bos, E., van Den Heuvel, M. W., van Hogezand, R. A., de Vries, R. R., Breedveld, F. C., & Boots, A. M. (2000). Raised human cartilage glycoprotein-39 plasma levels in patients with rheumatoid arthritis and other inflammatory conditions. Ann Rheum Dis, 59(7), 544-548. 121. Wan, G., Xiang, L., Sun, X., Wang, X., Li, H., Ge, W., & Cao, F. (2017). Elevated YKL-40 expression is associated with a poor prognosis in breast cancer patients. Oncotarget, 8(3), 5382-5391. 122. Wang, Y., Wong, C. W., Yan, M., Li, L., Liu, T., Or, P. M., Tsui, S. K., Waye, M. M., & Chan, A. M. (2018). Differential regulation of the pro-inflammatory biomarker, YKL-40/CHI3L1, by PTEN/Phosphoinositide 3-kinase and JAK2/STAT3 pathways in glioblastoma. Cancer Lett, 429, 54-65. 123. Xing, Z., Gauldie, J., Cox, G., Baumann, H., Jordana, M., Lei, X. F., & Achong, M. K. (1998). IL-6 is an antiinflammatory cytokine required for controlling local or systemic acute inflammatory responses. J Clin Invest, 101(2), 311-320. 124. Yamaguchi, H., Wyckoff, J., & Condeelis, J. (2005). Cell migration in tumors. Curr Opin Cell Biol, 17(5), 559-564. 125. Yan, C., Ding, X., Wu, L., Yu, M., Qu, P., & Du, H. (2013). Stat3 downstream gene product chitinase 3-like 1 is a potential biomarker of inflammation-induced lung cancer in multiple mouse lung tumor models and humans. PLoS One, 8(4), e61984. 126. Yang, X., Fang, D., Li, M., Chen, J., Cheng, Y., & Luo, J. (2021). Knockdown of Chitinase 3-Like-1 Inhibits Cell Proliferation, Promotes Apoptosis, and Enhances Effect of Anti-Programmed Death Ligand 1 (PD-L1) in Diffuse Large B Cell Lymphoma Cells. Med Sci Monit, 27, e929431. 127. Yu, J. E., Yeo, I. J., Son, D. J., Yun, J., Han, S. B., & Hong, J. T. (2022). Anti-Chi3L1 antibody suppresses lung tumor growth and metastasis through inhibition of M2 polarization. Mol Oncol, 16(11), 2214-2234. 128. Zandvliet, M. (2016). Canine lymphoma: a review. Vet Q, 36(2), 76-104. 129. Zhao, T., Su, Z., Li, Y., Zhang, X., & You, Q. (2020). Chitinase-3 like-protein-1 function and its role in diseases. Signal Transduct Target Ther, 5(1), 201. 130. Zhao, T., Zeng, J., Xu, Y., Su, Z., Chong, Y., Ling, T., Xu, H., Shi, H., Zhu, M., Mo, Q., Huang, X., Li, Y., Zhang, X., Ni, H., & You, Q. (2022). Chitinase-3 like-protein-1 promotes glioma progression via the NF-kappaB signaling pathway and tumor microenvironment reprogramming. Theranostics, 12(16), 6989-7008. 131. Zhou, Y., He, C. H., Herzog, E. L., Peng, X., Lee, C. M., Nguyen, T. H., Gulati, M., Gochuico, B. R., Gahl, W. A., Slade, M. L., Lee, C. G., & Elias, J. A. (2015). Chitinase 3-like-1 and its receptors in Hermansky-Pudlak syndrome-associated lung disease. J Clin Invest, 125(8), 3178-3192. 132. Zhou, Y., He, C. H., Yang, D. S., Nguyen, T., Cao, Y., Kamle, S., Lee, C. M., Gochuico, B. R., Gahl, W. A., Shea, B. S., Lee, C. G., & Elias, J. A. (2018). Galectin-3 Interacts with the CHI3L1 Axis and Contributes to Hermansky-Pudlak Syndrome Lung Disease. J Immunol, 200(6), 2140-2153. | - |
| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/88289 | - |
| dc.description.abstract | YKL-40是一種分泌型的醣蛋白，其生物學功能尚未完全清楚，可能參與了血管生成和細胞外基質重塑，且高血清YKL-40量已經在多種人類炎症性疾病以及惡性腫瘤中被發現。以往的研究還顯示出，在癌症患者中，高血清YKL-40量在不同類型癌症中，有潛力做為與疾病預後不良和短生存時間有關的生物指標，因此，瞭解YKL-40在癌症中的作用機制非常重要。然而，大部分YKL-40於癌症的研究都在人類實體腫瘤進行，對於犬癌症的研究極少；我們先前的研究發現，罹患癌症犬隻的血清YKL-40顯著高於健康犬，且在經過治療後復發的淋巴瘤犬血清中YKL-40高於未復發的犬隻。為了研究YKL-40在犬癌症中的生物學作用，我們在本研究中純化了重組犬YKL-40 (rcYKL-40)，並將其應用於犬淋巴瘤細胞株CLBL-1 (B細胞) 和UL-1 (T細胞)，以評估其對犬淋巴瘤細胞的生物學功能的影響及其背後可能的細胞內信號傳遞途徑。研究結果顯示，包括外周血液淋巴細胞、單核球細胞、單核球來源巨噬細胞及成熟的單核球來源樹突細胞在內的多種犬血液細胞均會表現YKL-40，而未成熟的單核球來源樹突細胞和犬淋巴瘤細胞CLBL-1和UL-1則不表現；在細胞實驗中，rcYKL-40促進了UL-1細胞的增殖和遷移能力，但僅增進了CLBL-1細胞的侵襲能力，我們推測這是由於CLBL-1原本就生長較快，rcYKL-40無法更加促進其增殖與遷移的能力。此外，在細胞活力存活試驗中發現，化療藥物阿黴素可以有效抑制CLBL-1和UL-1的增殖，而給予rcYKL-40可以保護兩種細胞減少阿黴素的傷害，並提高細胞存活率。透過細胞內信號途徑分析結果可得知，經rcYKL-40處理後，CLBL-1的ERK和UL-1的AKT磷酸化蛋白的活性均增加，未來可以更深入探索YKL-40作用的分子機制，以及將YKL-40作為治療犬淋巴瘤潛在標靶的治療策略。 | zh_TW |
| dc.description.abstract | YKL-40 is a glycoprotein with incompletely understood biological functions. It was suggested to be involved in angiogenesis and extracellular matrix remodeling. Increased serum concentrations of YKL-40 have been detected in various human inflammatory diseases and malignancies. Previous studies also showed elevated serum levels of YKL-40 in cancer patients could be a potential biomarker that is associated with poor prognosis and short survival time in different kinds of cancer. Therefore, it’s important to clarify how YKL-40 plays in cancers. However, most of the YKL-40 studies on cancer are based on human solid tumors. There are few studies on canine cancers. Our previous studies found that the serum YKL-40 level in cancer dogs had a substantial elevation compared to healthy dogs. Additionally, serum YKL-40 level in lymphoma dogs who relapsed after treatment was higher than without relapse. To investigate the biological functions of YKL-40 in dog cancer, recombinant canine YKL-40 (rcYK-40) was purified and applied to canine lymphoma cells, CLBL-1 (B cell) and UL-1 (T cell), in this study. The results show various canine blood cells including peripheral blood lymphocytes, monocytes, monocyte-derived macrophages, and mature monocyte-derived dendritic cells express YKL-40, whereas immature monocyte-derived dendritic cells and both CLBL-1 and UL-1, do not. In the cellular assay, the rcYKL-40 promotes the abilities of proliferation and migration on UL-1 cells, while it only elicits the invasion ability of CLBL-1 cells. Besides, in viability assay, doxorubicin (DOX) effectively inhibits the proliferation of CLBL-1 and UL-1. However, the administration of rcYKL-40 protects both cells from DOX damage and increases cell survival. By treating with the rcYKL40, the phosphorylation activity of ERK in CLBL-1 and AKT in UL-1 increased. Co-treatment of DOX and rcYKL40 on UL-1, but not CLBL-1, the activity of both proteins was also increased. These imply the potential role of YKL-40 on cellular processes and DOX-induced damage in canine lymphoma. Further studies may explore the molecular mechanisms of YKL-40 and potential therapeutic strategies targeting YKL-40 in canine lymphoma treatment. | en |
| dc.description.provenance | Submitted by admin ntu (admin@lib.ntu.edu.tw) on 2023-08-09T16:23:15Z No. of bitstreams: 0 | en |
| dc.description.provenance | Made available in DSpace on 2023-08-09T16:23:15Z (GMT). No. of bitstreams: 0 | en |
| dc.description.tableofcontents | 誌謝 i
中文摘要 ii Abstract iii Chapter 1. Background and Literature Reviews 1 1.1 YKL-40 1 1.1.1 Expressions and regulations of YKL-40 2 1.1.2 The prognostic value of YKL-40 in inflammatory diseases and cancers 3 1.1.3 The correlation between YKL-40 and non-cancer diseases 4 1.1.4 The correlation between YKL-40 and cancers 5 1.1.5 The possible mechanisms of YKL-40 in cancers 6 1.2 Canine lymphoma 8 1.2.1 Incidence and predilection 9 1.2.2 Clinical subclassifications 10 1.2.3 Diagnosis 12 1.2.4 Treatment options 13 1.3 Oncogenic behavior of cancer cells 15 1.3.1 Abnormal proliferation 16 1.3.2 Migration and Invasion 17 1.3.3 Cell death resistance 18 1.4 Conclusion 19 Chapter 2 Introduction 20 Chapter 3. Materials and Methods 23 3.1 Cell cultures 23 3.2 Generation of canine peripheral blood lymphocytes, monocytes, macrophages, and dendritic cells 23 3.3 Expression and purification of recombinant canine YKL-40 protein 25 3.4 Total RNA extraction 26 3.5 RT-PCR 27 3.6 PCR 28 3.7 Genomic DNA extraction 29 3.8 PCR for antigen receptor rearrangements (PARR) 29 3.9 Proliferation assay 30 3.10 Transwell migration assay 31 3.11 Invasion assay 32 3.12 Viability assay 33 3.13 Cell signal pathway analysis 34 3.14 Western blot analysis 35 3.15 Statistical analysis 37 Chapter 4. Results 38 4.1 Examination of YKL-40 expression in various canine cells 38 4.2 Preparation of recombinant canine YKL-40 protein 38 4.2.1 Purification of recombinant canine YKL-40 protein 38 4.2.2 Identification of purified recombinant canine YKL-40 39 4.3 Detection of gene rearrangements in canine lymphoma cell lines 39 4.4 Proliferation assay 40 4.5 Transwell migration assay 40 4.6 Invasion assay 41 4.7 Viability assay 41 4.8 Cell signal pathway analysis 42 4.9 Expression of YKL-40-related receptor 42 Chapter 5. Discussion 43 Tables 54 Table 1. The primers used in this study 54 Figures 55 Figure 1. Experimental design 55 Figure 2. Schematic diagram of the construction of prcYKL-40 56 Figure 3. YKL-40 mRNA expressions of canine lymphoma cell lines and peripheral blood cells 57 Figure 4. Purification of recombinant canine YKL-40 protein (46.7kDa) 58 Figure 5. Detection of gene rearrangements in canine lymphoma cell lines 59 Figure 6. Effect of rcYKL-40 protein on cell proliferation rate 60 Figure 7. Effect of rcYKL-40 protein on cell viability 64 Figure 8. Cell signal pathway under rcYKL-40 and doxorubicin treatment 65 Figure 9. IL13Rα2 mRNA expressions of canine lymphoma cell lines 66 References 67 | - |
| dc.language.iso | en | - |
| dc.title | 探討YKL-40作用於犬隻淋巴瘤細胞的生物學功能 | zh_TW |
| dc.title | To investigate the biological functions of YKL-40 on canine lymphoma cells | en |
| dc.type | Thesis | - |
| dc.date.schoolyear | 111-2 | - |
| dc.description.degree | 碩士 | - |
| dc.contributor.oralexamcommittee | 王尚麟;黃威翔;詹昆衛 | zh_TW |
| dc.contributor.oralexamcommittee | Shang-Lin Wang;Wei-Hsiang Huang;Kun-Wei Chan | en |
| dc.subject.keyword | YKL-40,犬淋巴瘤,阿黴素,生物學功能,細胞內信號途徑, | zh_TW |
| dc.subject.keyword | YKL-40,canine lymphoma,doxorubicin,biological functions,intracellular signaling pathways, | en |
| dc.relation.page | 80 | - |
| dc.identifier.doi | 10.6342/NTU202301870 | - |
| dc.rights.note | 同意授權(全球公開) | - |
| dc.date.accepted | 2023-07-26 | - |
| dc.contributor.author-college | 生物資源暨農學院 | - |
| dc.contributor.author-dept | 獸醫學系 | - |
| 顯示於系所單位： | 獸醫學系 | |
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