CABYR Is a Novel Cancer-Testis Antigen in Lung Cancer

Luo, Chonglin; Xiao, Xueyuan; Liu, Danhui; Chen, Shaosong; Li, Mingying; Xu, Anjian; Liu, Jifu; Gao, Shugeng; Wu, Shanshan; He, Dacheng

doi:10.1158/1078-0432.ccr-06-1742

Cited by 23 publications

(25 citation statements)

References 31 publications

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“…CABYR was initially reported to be testis specific and localized to the principal piece of the sperm flagellum that associates with the fibrous sheath during capacitation (8). In our previous study, we confirmed that CABYR is a novel cancer testis antigen in lung cancer (9). In addition to lung cancer and brain tumors (9,10), CABYR was also shown to be aberrantly expressed in liver cancer and esophageal cancer (11).…”

Section: Introductionsupporting

confidence: 71%

“…In our previous study, we confirmed that CABYR is a novel cancer testis antigen in lung cancer (9). In addition to lung cancer and brain tumors (9,10), CABYR was also shown to be aberrantly expressed in liver cancer and esophageal cancer (11). The knockdown of CABYR-c in HepG2 cells resulted in the inhibition of cell growth (12).…”

Section: Introductionsupporting

confidence: 57%

“…Immunohistochemistry was performed as described in our previous study (9). Mouse anti-CABYR-a/b antisera (1:100 dilution), anti-Akt (1:300 dilution), and anti-pAkt (1:50 dilution) were separately incubated with the specimens, and biotinylated secondary antibodies were applied at a dilution of 1:200 before HRP application (Vectastain ABComplex; Vector Laboratories, Inc.), resulting in a positive brown staining.…”

Section: Immunohistochemistry and Tunel Assaymentioning

confidence: 99%

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Knockdown of CABYR-a/b Increases Chemosensitivity of Human Non–Small Cell Lung Cancer Cells through Inactivation of Akt

Qian

Wang

et al. 2014

Molecular Cancer Research

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CABYR is a calcium-binding tyrosine phosphorylation-regulated protein that was identified as a novel cancer testis antigen in lung cancer in our previous study. However, the role of CABYR as a driver of disease progression or as a chemosensitizer is poorly understood. This study sought to investigate the relationship between the expression levels of CABYR-a/b, which are the two predominant isoforms of the five isoform proteins encoded by CABYR, and chemosensitivity in non-small cell lung cancer cells. We found that the short hairpin RNA-mediated knockdown of CABYR-a/b significantly inhibited the proliferation of NCI-H460 and A549 cells and resulted in the attenuation of Akt phosphorylation, which is constitutively active in lung cancer cells. The silencing of CABYR-a/b expression notably impacted the downstream components of the Akt pathways: decreasing the phospho-GSK-3b (Ser9) levels and increasing the expression of the p53 and p27 proteins. Furthermore, CABYR-a/b knockdown led to a significant increase in chemosensitivity in response to chemotherapeutic drugs and drug-induced apoptosis, both in vitro and in vivo. Conversely, the transient transfection of CABYR-a/b-depleted cells with constitutively active Akt partially restored the resistance to cisplatin and paclitaxel and significantly decreased the activation of GSK-3b and cleaved PARP. Taken together, our results suggest that the inhibition of CABYR-a/b is a novel method to improve the apoptotic response and chemosensitivity in lung cancer and that this cancer testis antigen is an attractive target for lung cancer drug development.

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Section: Introductionsupporting

confidence: 71%

Section: Introductionsupporting

confidence: 57%

Section: Immunohistochemistry and Tunel Assaymentioning

confidence: 99%

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Knockdown of CABYR-a/b Increases Chemosensitivity of Human Non–Small Cell Lung Cancer Cells through Inactivation of Akt

Qian

Wang

et al. 2014

Molecular Cancer Research

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“…Sp17 has been reported in various malignancies (14)(15)(16). In contrast, the expression of CABYR has only been examined in brain and lung cancers (4,6). In this study, we analyzed the expression of CABYR in tissues from liver, esophagus, and lung and in human cell lines of different histological origin at the mRNA and protein levels by RT-PCR and Western blot analysis, respectively.…”

Section: Discussionmentioning

confidence: 99%

“…Although CABYR was originally reported as a testis-specific protein localized exclusively in the sperm flagellum, which gains calcium-binding capacity when phosphorylated during capacitation (1), CABYR-c and CABYR-d are also detected in the normal human brain and also in the fetal brain and brain tumors in which the expression is more distinct than in the adult brain (4). This evidence, together with the detection of aberrant expression of CABYR-a/b and CABYR-c in lung cancers and the presence of specific IgG antibodies in some sera from lung cancer patients but not from the healthy donors, has defined CABYR as a novel cancer/testis (CT) antigen and a new potential target for the use in development of therapeutics for human cancer (5,6).…”

Section: Introductionmentioning

confidence: 99%

Expression of the sperm fibrous sheath protein CABYR in human cancers and identification of α-enolase as an interacting partner of CABYR-a

Yang

2011

Oncol Rep

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Protein kinase A RII‐like (R2D2) proteins exhibit differential localization and AKAP interaction

Newell

Fiedler

Ruan

et al. 2008

Cell Motil. Cytoskeleton

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A-kinase anchoring proteins (AKAPs) bind to protein kinase A (PKA) via an amphipathic helix domain that interacts with a dimerization/docking domain on the regulatory (R) subunit of PKA. Four other mammalian proteins (ROPN1, ASP, SP17, and CABYR) also contain a highly conserved RII dimerization/docking (R2D2) domain, suggesting all four proteins may interact with all AKAPs in a manner similar to RII. All four of these proteins were originally detected in the flagellum of mammalian sperm. In this report, we demonstrate that all four R2D2 proteins are expressed in a wide variety of tissues and three of the proteins SP17, CABYR, and ASP are located in motile cilia of human bronchus and fallopian tubes. In addition, we detect SP17 in primary cilia. We also provide evidence that ROPN1 and ASP bind to a variety of AKAPs and this interaction can be disrupted with anchoring inhibitor peptides. The interaction of SP17 and CABYR with AKAPs appears to be much more limited. None of the R2D2 proteins appears to bind cAMP, a fundamental characteristic of the regulatory subunits of PKA. These observations suggest that R2D2 proteins utilize docking interactions with AKAPs to accomplish their function of regulating cilia and flagella. Based on location, affinity for AKAPs and lack of affinity for cAMP, it appears that each R2D2 protein has a unique role in this process.

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CABYR Is a Novel Cancer-Testis Antigen in Lung Cancer

Cited by 23 publications

References 31 publications

Knockdown of CABYR-a/b Increases Chemosensitivity of Human Non–Small Cell Lung Cancer Cells through Inactivation of Akt

Knockdown of CABYR-a/b Increases Chemosensitivity of Human Non–Small Cell Lung Cancer Cells through Inactivation of Akt

Expression of the sperm fibrous sheath protein CABYR in human cancers and identification of α-enolase as an interacting partner of CABYR-a

Protein kinase A RII‐like (R2D2) proteins exhibit differential localization and AKAP interaction

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