K K Waltering M A Helenius
 K.K. Waltering, M.A. Helenius, B. Sahu, V. Manni, M.J. Linja, O.A. Janne,
 X.Q. Zhang, D. Kondrikov, T.C. Yuan, F.F. Lin, J. Hansen, M.F. Lin, Receptor protein tyrosine phosphatase alpha signaling is involved in androgen depletion-induced neuroendocrine diﬀerentiation of androgen-sensitive LNCaP human prostate cancer cells, Oncogene 22 (2003) 6704–6716.
D. Mercola, P.M. Carpenter, D. Bowtell, Z.A. Ronai, Siah2-dependent concerted activity of HIF and FoxA2 regulates formation of neuroendocrine Ac-DEVD-CHO and neuroendocrine prostate tumors, Cancer Cell 18 (2010) 23–38.  J.M. Winter, N.L. Curry, D.M. Gildea, K.A. Williams, M. Lee, Y. Hu, N.P.S. Crawford, Modifier locus mapping of a transgenic F2 mouse population identifies CCDC115 as a novel aggressive prostate cancer modifier gene in humans, BMC Genomics 19 (2018) 450.
 T. Karantanos, P.G. Corn, T.C. Thompson, Prostate cancer progression after an-drogen deprivation therapy: mechanisms of castrate resistance and novel ther-apeutic approaches, Oncogene 32 (2013) 5501–5511.  M. Nouri, E. Ratther, N. Stylianou, C.C. Nelson, B.G. Hollier, E.D. Williams, Androgen-targeted therapy-induced epithelial mesenchymal plasticity and neu-roendocrine transdiﬀerentiation in prostate cancer: an opportunity for intervention, Front. Oncol. 4 (2014) 370.
 T. Ito, S. Yamamoto, Y. Ohno, K. Namiki, T. Aizawa, A. Akiyama, M. Tachibana, Up-regulation of neuroendocrine diﬀerentiation in prostate cancer after androgen de-privation therapy, degree and androgen independence, Oncol. Rep. 8 (2001)
 P.S. Nelson, Molecular states underlying androgen receptor activation: a framework for therapeutics targeting androgen signaling in prostate cancer, J. Clin. Oncol. 30 (2012) 644–646.
Contents lists available at ScienceDirect
journal homepage: www.elsevier.com/locate/cellsig
Angio-associated migratory cell protein interacts with epidermal growth factor receptor and enhances proliferation and drug resistance in human non-small cell lung cancer cells
Shun Yaoa, Feifei Shia, Yingying Wanga,b, Xiaoyang Suna, Wenbo Suna, Yifeng Zhanga, Xianfang Liuc, Xiangguo Liua,b, , Ling Sua,b,
a Shandong Provincial Key Laboratory of Animal Cell and Developmental Biology, School of Life Sciences, Shandong University, Qingdao, China
b Shandong Provincial Collaborative Innovation Center of Cell Biology, School of Life Sciences, Shandong Normal University, Jinan, China
c The Department of Otolaryngology Head and Neck Surgery, Shandong Provincial Hospital, Aﬃliated to Shandong University, Jinan, China
Keywords: Angio-associated migratory cell protein (AAMP) is expressed in some human cancer cells. Previous studies have
AAMP shown AAMP high expression predicted poor prognosis. But its biological role in non-small cell lung cancer
Proliferation (NSCLC) cells is still unknown. In our present study, we attempted to explore the functions of AAMP in NSCLC
Tumorigenesis cells. According to our findings, AAMP knockdown inhibited lung cancer cell proliferation and inhibited lung
cancer cell tumorigenesis in the mouse xenograft model. Epidermal growth factor receptor (EGFR) is a primary
receptor tyrosine kinase (RTK) that promotes proliferation and plays an important role in cancer pathology. We
found AAMP interacted with EGFR and enhanced its dimerization and phosphorylation at tyrosine 1173 which
activated ERK1/2 in NSCLC cells. In addition, we showed AAMP conferred the lung cancer cells resistance to
chemotherapeutic agents such as icotinib and doxorubicin. Taken together, our data indicate that loss of AAMP
from NSCLC inhibits tumor growth and elevates drug sensitivity, and these findings have clinical implications to
treat NSCLC cancers.
Angio-associated migratory cell protein (AAMP) was initially iso-lated from a human melanoma cell line in 1995 . AAMP is a 52kD protein that contains two immunoglobulin-like domains, a heparin binding consensus sequence and a repeat WD40 motif which plays various roles in cell cycle control, protein-protein interaction, tran-scriptional activation, and signal transduction [2,3]. AAMP is expressed in diﬀerent cell types, including smooth muscle cells, dermal fibro-blasts, renal proximal tubular cells and cancerous cells like human breast carcinoma cells, melanoma cells and prostate cancer cells [4–8].
Recent studies suggest AAMP plays an important role in angiogen-esis by promoting endothelial tube formation [9,10]. And, it is im-plicated in cell migration via the ROCK/RHOA signaling pathway . AAMP was also reported to aﬀect cell growth in HECV cells, but its