The authors apologize to the readers, reviewers, and editors for publishing this check details erroneous data. References 1. Tu X, Zhuang J, Wang W, Zhao L, Zhao L, Zhao J, Deng C, Qiu S, Zhang Y: Screening and Identification of a Renal Carcinoma Specific Peptide from a Phage Display Peptide Library. J Exp Clin Cancer Res 2011, 30:105.PubMedCrossRef”
“Background Epithelial ovarian cancer (EOC) is the sixth most common cancer and the

fifth leading cause of cancer mortality in women worldwide [1]. This lethal NSC23766 mw gynecological malignancy is commonly diagnosed at a late stage due to the silent early stage and easily metastasis. Many advances took place in the pathological study and in understanding the mechanisms involved in EOC progression, details still need further investigations [2, 3]. Therefore, this is an urgent need of more effective and new molecular targeted therapies for EOC. Adrenomedullin (AM) is a 52-amino-acid peptide first isolated from human pheochromocytoma [4]. It belongs to a family of peptides with calcitonin Emricasan clinical trial gene-related peptide

(CGRP) and Amylin [5]. AM was identified as a major regulator of carcinogenesis and tumor progression, and autocrine loop of AM was targeted as new strategies against human cancers [6–8]. AM gene expression was proved to be associated with histological grade and poor prognosis of ovarian cancer [9]. The expression of its receptor calcitonin receptor-like receptor CRLR together with modulation factors RAMP2/RAMP3 were also found in EOC tissues and OVCAR3 cells [10, 11]. Our previous study

had found that AM was autocrined in EOC cell line CAOV3 by bFGF stimulation [12].Thus we supposed that AM may play an important role in EOC heptaminol progression. Integrins are family of transmembrane proteins, which are composed of 2 subunits as α- and β- formed heterodimer, and work as receptors of extracellular matrix (ECM) [13]. Integrins received and transmitted the signal from ECM into cells and modified various function of cells including shape, motility, and involved in EOC metastasis [14, 15]. It was well accepted that integrin α5 specifically bound to integrin β1 to form specific receptor for fibronectin (FN). Activated integrin α5β1 could activate the focal adhension kinase (FAK) and Src, which consequently promoted cancer cells migration and invasion via activating various skeleton proteins, such as paxillin. It was reported that overexpression of integrin α5β1 predicted poor prognosis for EOCs [16]. And integrin α5β1 promoted ovarian cancer cells invasion by directly activating c-Met followed by FAK activation [17].