高尔基体磷蛋白 3及蛋白激酶D2在肺腺癌中的表达及其临床意义

Abstract
Figure/Table
References
Related Citation (15)

Download: PDF (1934 KB) HTML (0 KB)
Export: BibTeX | EndNote (RIS)

Abstract Objective To explore the clinical significance of PKD2 and GOLPH3 expression in lung adenocarcinoma. Methods Clinical data of 106 patients with lung adenocarcinoma were collected from June 2014 to June 2018 in the 904th Hospital of Chinese PLA Joint Logistics support Force. The expression of GOLPH3 and PKD2 in lung adenocarcinoma and corresponding adjacent tissues were detected by immunohistochemistry. The expression levels of GOLPH3 and PKD2 in lung adenocarcinoma tissues and their effects on prognosis were analyzed by log-rank test and multivariate COX risk regression model. Results The expression levels of GOLPH3 and PKD2 in lung adenocarcinoma tissues were significantly higher than those in corresponding adjacent tissues (P<0.05). In addition, there was a positive correlation between the expression of GOLPH3 and PKD2 in lung adenocarcinoma. Univariate analysis showed that the expression of GOLPH3 and PKD2, tumor diameter, TNM stage, lymphatic metastasis and tissue differentiation affected the prognosis of the patients. Multivariate analysis showed high expression of GOLPH3 (HR=2.879,95%CI=1.590-5.212, P<0.05), high expression of PKD2 (HR=1.922,95%CI=1.078-3.427, P<0.05) and TNM stage (HR=2.022, 95%CI=1.144-3.573,P<0.05)were the independent risk factors affecting the survival of patients. Conclusions GOLPH3 and PKD2 which are characterized by high expression in lung adenocarcinoma are the independent risk factors affecting the prognosis of patients with lung adenocarcinoma.

Key words： lung adenocarcinoma GOLPH3 PKD2 prognosis

Received: 20 June 2022

ZTFLH:

R734.2

	Service

	E-mail this article
	Add to my bookshelf
	Add to citation manager
	E-mail Alert
	RSS
	Articles by authors

Cite this article:

URL:

http://journal08.magtechjournal.com/Jwk_wjyx/EN/ OR http://journal08.magtechjournal.com/Jwk_wjyx/EN/Y2022/V33/I11/976

[1]	Xu K, Zhang C, Du T, et al. Progress of exosomes in the diagnosis and treatment of lung cancer[J]. Biomed Pharmacother, 2021, 134:111111.
[2]	Herbst R S, Morgensztern D, Boshoff C. The biology and management of non-small cell lung cancer[J]. Nature, 2018, 553(7689): 446-454.
[3]	Denisenko T V, Budkevich I N, Zhivotovsky B. Cell death-based treatment of lung adenocarcinoma[J]. Cell Death Dis, 2018, 9(2): 117.
[4]	Duma N, Santana-Davila R, Molina J R. Non-small cell lung cancer: epidemiology, screening, diagnosis, and treatment[J]. Mayo Clin Proc, 2019, 94(8):1623-1640.
[5]	Ye Z, Huang Y, Ke J, et al. Breakthrough in targeted therapy for non-small cell lung cancer[J]. Biomed Pharmacother, 2021,133:111079.
[6]	Roy A, Ye J, Deng F, et al. Protein kinase D signaling in cancer: a friend or foe?[J]. Biochim Biophys Acta Rev Cancer, 2017,1868(1):283-294.
[7]	Sechi S, Frappaolo A, Karimpour-Ghahnavieh A, et al. Oncogenic roles of GOLPH3 in the physiopathology of cancer[J]. Int J Mol Sci, 2020, 21(3):933.
[8]	Tang W, Han M, Ruan B, et al. Overexpression of GOLPH3 is associated with poor survival in non-small-cell lung cancer [J].Am J Transl Res, 2016, 8(4):1756-1762.
[9]	Zhang X, Connelly J, Chao Y, et al. Multifaceted functions of protein kinase D in pathological processes and human diseases[J].Biomolecules, 2021,11(3):483.
[10]	Azoitei N, Cobbaut M, Becher A, et al. Protein kinase D2: a versatile player in cancer biology [J]. Oncogene, 2018, 37(10):1263-1278.
[11]	Pang Z, Wang Y, Ding N, et al. High PKD2 predicts poor prognosis in lung adenocarcinoma via promoting epithelial-mesenchymal transition[J]. Sci Rep, 2019,9(1):1324.
[12]	Azoitei N, Diepold K, Brunner C, et al. HSP90 supports tumor growth and angiogenesis through PRKD2 protein stabilization[J]. Cancer Res, 2014,74(23):7125-7136.
[13]	Zhu Y, Cheng Y, Guo Y, et al. Protein kinase D2 contributes to TNF-α-induced epithelial mesenchymal transition and invasion via the PI3K/GSK-3β/β-catenin pathway in hepatocellular carcinoma[J]. Oncotarget, 2016, 7(5):5327-5341.
[14]	Wille C, Köhler C, Armacki M, et al. Protein kinase D2 induces invasion of pancreatic cancer cells by regulating matrix metalloproteinases[J]. Mol Biol Cell, 2014, 25(3):324-336.
[15]	Bernhart E, Damm S, Wintersperger A, et al. Protein kinase D2 regulates migration and invasion of U87MG glioblastoma cells in vitro[J]. Exp Cell Res, 2013,319(13):2037-2048.
[16]	Scott K L, Kabbarah O, Liang M C, et al. GOLPH3 modulates mTOR signalling and rapamycin sensitivity in cancer[J]. Nature, 2009,459(7250):1085-1090.
[17]	Kuna R S, Field S J. GOLPH3: a Golgi phosphatidylinositol(4)phosphate effector that directs vesicle trafficking and drives cancer[J]. J Lipid Res, 2019,60(2):269-275.
[18]	Tan J Z A, Gleeson P A. Cargo sorting at the trans-Golgi network for shunting into specific transport routes: role of arf small G proteins and adaptor complexes[J]. Cells, 2019,8(6):531.
[19]	Godi A, Di Campli A, Konstantakopoulos A, et al. FAPPs control Golgi-to-cell-surface membrane traffic by binding to ARF and PtdIns(4)P[J]. Nat Cell Biol, 2004,6(5):393-404.
[20]	Dippold H C, Ng M M, Farber-Katz S E, et al. GOLPH3 bridges phosphatidylinositol-4- phosphate and actomyosin to stretch and shape the Golgi to promote budding[J]. Cell, 2009,139(2):337-351.
[21]	Taft M H, Behrmann E, Munske-Weidemann L C, et al. Functional characterization of human myosin-18A and its interaction with F-actin and GOLPH3[J]. J Biol Chem, 2013,288(42):30029-30041.
[22]	Buschman M D, Xing M, Field S J. The GOLPH3 pathway regulates Golgi shape and function and is activated by DNA damage[J]. Front Neurosci, 2015,9(7):362.
[23]	Ng M M, Dippold H C, Buschman M D, et al. GOLPH3L antagonizes GOLPH3 to determine Golgi morphology[J]. Mol Biol Cell, 2013,24(6):796-808.
[24]	Halberg N, Sengelaub C A, Navrazhina K, et al. PITPNC1 recruits RAB1B to the Golgi network to drive malignant secretion[J].Cancer Cell, 2016,29(3):339-353.
[25]	Eiseler T, Wille C, Koehler C, et al. Protein kinase D2 assembles a multiprotein complex at the trans-Golgi network to regulate matrix metalloproteinase secretion[J]. J Biol Chem, 2016,291(1):462-477.
[26]	Wei N, Chu E, Wipf P, et al. Protein kinase D as a potential chemotherapeutic target for colorectal cancer[J]. Mol Cancer Ther, 2014, 13(5):1130-1141.
[27]	Yu T, An Q, Cao X L, et al. GOLPH3 inhibition reverses oxaliplatin resistance of colon cancer cells via suppression of PI3K/AKT/mTOR pathway [J]. Life Sci, 2020, 260(1):118294.
[28]	Liu H, Wang X, Feng B, et al. Golgi phosphoprotein 3 (GOLPH3) promotes hepatocellular carcinoma progression by activating mTOR signaling pathway[J]. BMC Cancer, 2018, 18(1):661.
[29]	Núñez-Olvera S I, Chávez-Munguía B, Del Rocío Terrones-Gurrola M C, et al. A novel protective role for microRNA-3135b in Golgi apparatus fragmentation induced by chemotherapy via GOLPH3/AKT1/mTOR axis in colorectal cancer cells[J]. Sci Rep, 2020, 10(1):10555.
[30]	Zhou X, Xue P, Yang M, et al. Protein kinase D2 promotes the proliferation of glioma cells by regulating Golgi phosphoprotein 3[J]. Cancer Lett, 2014, 355(1):121-129.