Increased expression of calcineurin in human colorectal adenocarcinomas

Lakshmikuttyamma, Ashakumary; Selvakumar, Ponniah; Kanthan, Rani; Kanthan, Selliah; Sharma, Rajendra K.

doi:10.1002/jcb.20437

Cited by 60 publications

(70 citation statements)

References 43 publications

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“…The correlation between expression of the proteins in normal-appearing peritumoral gastric mucosa and cancer tissue with each other. downregulation of calpastatin was observed (17). In human prostate cancer, the mRNA level of CAPN1 increased (22).…”

Section: Discussionmentioning

confidence: 95%

“…Calpain has been reported to be involved in apoptosis of cancer cells (15). In addition, the upregulation of calpain may be involved in cancer development and migration (16), and calpain expression is upregulated in a number of tumors, including colorectal adenocarcinoma (17), breast cancer (18) and ovarian cancer (19). In GC, it has been reported that the calpain activity was upregulated compared with normal tissue (20), and it is speculated that higher calpain and calpastatin expression may be a favorable prognostic marker for GC (21).…”

Section: Introductionmentioning

confidence: 99%

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Comparison of the protein expression of calpain-1, calpain-2, calpastatin and calmodulin between gastric cancer and normal gastric mucosa

Liu

Zhou

et al. 2017

Oncology Letters

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Abstract. The understanding of molecular mechanisms that are involved in the development and the progression of gastric cancer (GC) are of importance for the diagnosis and treatment. The calpain system, which contains the calpains and the endogenous inhibitor, has been suggested as an important factor in the tumorigenesis and migration of colorectal adenocarcinoma, breast and ovarian cancer, and as a prognostic marker for GC. However, the expression level of calpain system proteins in GC and normal-appearing peritumoral gastric mucosa remain unknown. The present study investigated the expression of calpain-1 (CAPN1), calpain-2 (CAPN2), calpastatin and calmodulin (CaM) in GC and uninvolved gastric mucosa tissues with immunohistochemistry. Results demonstrated that CAPN2 protein level increased in GCs compared with normal tissues, while calpastatin and CaM protein level decreased. No evident alterations were observed for CAPN1. Although the protein expression of all these four proteins was not in association with the clinical variables of GC in the present study, higher calpain enzyme activity could be a negative prognostic marker, since calpains are responsible for the generation of active forms of certain proteins that facilitate the progression of cancer. The ratio of (CAPN1 x CAPN2)/(calpastatin x CaM) may serve as a potential index for diagnosis of GC.

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Section: Discussionmentioning

confidence: 95%

Section: Introductionmentioning

confidence: 99%

Comparison of the protein expression of calpain-1, calpain-2, calpastatin and calmodulin between gastric cancer and normal gastric mucosa

Liu

Zhou

et al. 2017

Oncology Letters

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“…The expression of calpastatin has not been previously studied in prostate tumors. However, an increase in the calpain/calpastatin ratio has been reported in a study of colorectal cancer (31), which showed that calpastatin levels are high in normal mucosa but decreased in tumor tissue. Moreover, increased expression of calpain 2 was detected in colorectal tumors and polyps, suggesting that the increase of calpain 2 levels may be an early event in the tumorigenesis process.…”

Section: Discussionmentioning

confidence: 96%

ERK Regulates Calpain 2-induced Androgen Receptor Proteolysis in CWR22 Relapsed Prostate Tumor Cell Lines

Chen

Libertini

Wang

et al. 2010

Journal of Biological Chemistry

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and the ʈ Veterans Mather, California 95655 Androgen ablation therapy is effective in treating androgendependent prostate tumors; however, tumors that can proliferate in castrate levels of androgen eventually arise. We previously reported that in CWR22Rv1 (Rv1) cells, the protease calpain 2 can cleave the androgen receptor (AR) into a constitutively active ϳ80,000 low molecular weight (LMW) form. In this study, we further dissect the mechanisms that produce the AR LMW forms using Rv1 cells and the related CWR22-R1 (R1) cells. The 39-amino acid insertional mutation in the Rv1-AR (E3DM-AR) sensitizes this AR to calpain 2 proteolysis. R1 cells encode the same AR molecule as the parental CWR22 xenograft. Using calpain 2 small interfering RNA and calpeptin, we find that calpain 2 plays a role in the generation of the LMW-AR in R1 cells. Furthermore, LMW-AR expression is regulated by the activation of calpain 2 by ERK 1 and 2. Inhibition of ERK phosphorylation or small interfering RNA-mediated decrease of ERK expression reduces LMW-AR levels in R1 cells. Conversely, activation of the MAPK pathway results in increased ERK phosphorylation and increased levels of LMW-AR. Finally, analyses of human tumor samples found that LMW-AR levels are higher in tumors that have an increased calpain/calpastatin ratio and/or increased levels of phospho-ERK (pERK). This suggests that a higher calpain/calpastatin ratio collaborates with activated ERK to promote the generation of the LMW-AR.

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“…In mitochondrial DNA-depleted human lung carcinoma A549 cells, the cell morphology is altered while invasive behavior and the increased expression and activity of CaN could be observed (Amuthan et al, 2002). In addition, higher levels of CaN protein and activity are observed in human colorectal adenocarcinomas and neuronal tumors (Goto et al, 1987;Lakshmikuttyamma et al, 2005). However, information regarding the mechanism in which CaN-overexpression causes the formation of human tumors has been limited.…”

Section: Introductionmentioning

confidence: 99%

Calcineurin-mediated dephosphorylation of c-Jun Ser-243 is required for c-Jun protein stability and cell transformation

et al. 2007

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Increased expression of calcineurin in human colorectal adenocarcinomas

Cited by 60 publications

References 43 publications

Comparison of the protein expression of calpain-1, calpain-2, calpastatin and calmodulin between gastric cancer and normal gastric mucosa

Comparison of the protein expression of calpain-1, calpain-2, calpastatin and calmodulin between gastric cancer and normal gastric mucosa

ERK Regulates Calpain 2-induced Androgen Receptor Proteolysis in CWR22 Relapsed Prostate Tumor Cell Lines

Calcineurin-mediated dephosphorylation of c-Jun Ser-243 is required for c-Jun protein stability and cell transformation

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