The value of tumour markers in lung cancer

Gomm, S. A.; Keevil, Brian; Thatcher, Nick; Hasleton, Philip; Swindell, Ric

doi:10.1038/bjc.1988.312

Cited by 42 publications

(18 citation statements)

References 26 publications

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“…Of note, aberrations in PGI expressions or activities due to mutations or deletions in PGI are of significant clinical importance because mutations in PGI lead to hereditary nonspherocytic hemolytic anemia disease (14)(15)(16). In clinical cancer pathology, the presence of PGI/AMF in the serum and urine is of prognostic value indicating cancer progression (17)(18)(19). The levels of PGI/AMF and its cell surface receptor gp78/AMFR expressions are associated with the pathologic stage, grade, and degree of tumor penetration to surrounding tissues marking a poor prognosis (17)(18)(19)(20)(21).…”

Section: Introductionmentioning

confidence: 99%

“…In clinical cancer pathology, the presence of PGI/AMF in the serum and urine is of prognostic value indicating cancer progression (17)(18)(19). The levels of PGI/AMF and its cell surface receptor gp78/AMFR expressions are associated with the pathologic stage, grade, and degree of tumor penetration to surrounding tissues marking a poor prognosis (17)(18)(19)(20)(21). AMF-AMFR is thought to be involved in EMT because their up-regulation in epithelial cancers is concomitant with the down-regulation of E-cadherin and up-regulation of its repressor, the Snail zinc finger transcription factor (22,23).…”

Section: Introductionmentioning

confidence: 99%

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Down-Regulation of Phosphoglucose Isomerase/Autocrine Motility Factor Results in Mesenchymal-to-Epithelial Transition of Human Lung Fibrosarcoma Cells

Funasaka

Yanagawa

et al. 2007

Cancer Research

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Phosphoglucose isomerase (PGI) is one of the glycolytic enzymes and is a multifunctional enzyme that functions in glucose metabolism inside the cell while acting as a cytokine outside the cell, with properties that include autocrine motility factor (AMF) regulating tumor cell motility. Although there are many studies indicating that PGI/AMF has been implicated in progression of metastasis, no direct studies of the significance of exogenous PGI/AMF on tumor progression have been reported. Here, we report on the mesenchymal-toepithelial transition (MET), which is the reverse phenomenon of the epithelial-to-mesenchymal transition that is associated with loss of cell polarity, loss of epithelia markers, and enhancement of cell motility essential for tumor cell invasion and metastasis. Mesenchymal human fibrosarcoma HT1080 cells, which have naturally high levels of endogenous and exogenous PGI/AMF, were stably transfected with PGI

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Down-Regulation of Phosphoglucose Isomerase/Autocrine Motility Factor Results in Mesenchymal-to-Epithelial Transition of Human Lung Fibrosarcoma Cells

Funasaka

Yanagawa

et al. 2007

Cancer Research

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“…In contrast, enolase-related autoantibody is rarely found in cancer patients in spite of the fact that another isoform, g-enolase (neuron-specific enolase; ENO2), is a product of several types of tumors (12). One study identified ENO1 as antigenic target on human oral cancer cells that was recognized by autologous CD4 + T cells (13).…”

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confidence: 99%

Identification of α-Enolase as an Autoantigen in Lung Cancer: Its Overexpression Is Associated with Clinical Outcomes

Chang

Liu

Hsieh

et al. 2006

Clinical Cancer Research

143

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Purpose: Although existence of humoral immunity has been previously shown in malignant pleural effusions, only a limited number of immunogenic tumor-associated antigens (TAA) have been identified and associated with lung cancer. In this study, we intended to identify moreTAAs in pleural effusion^derived tumor cells. Experimental Design: Using morphologically normal lung tissues as a control lysate inWestern blotting analyses, 54 tumor samples were screened with autologous effusion antibodies. Biochemical purification and mass spectrometric identification of TAAs were done using established effusion tumor cell lines as antigen sources. We identified a p48 antigen as a-enolase (ENO1). Semiquantitative immunohistochemistry was used to evaluate expression status of ENO1 in the tissue samples of 80 patients with non^small cell lung cancer (NSCLC) and then correlated with clinical variables. Results: Using ENO1-specifc antiserum, up-regulation of ENO1expression in effusion tumor cells from 11of 17 patients was clearly observed compared with human normal lung primary epithelial and non-cancer-associated effusion cells. Immunohistochemical studies consistently showed high level of ENO1 expression in all the tumors we have examined thus far. Log-rank and Cox's analyses of ENO1 expression status revealed that its expression level in primary tumors was a key factor contributing to overall-and progression-free survivals of patients (P < 0.05). The same result was also obtained in the early stage of NSCLC patients, showing that tumors expressing relatively higher ENO1level were tightly correlated with poorer survival outcomes. Conclusions: Our data strongly support a prognostic role of ENO1in determining tumor malignancy of patients with NSCLC.

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“…There are studies that AMF has been detected in the urine and plasma of cancer patients (6,7), however, what happens to the level of AMF in the plasma of humans and animal treated with anticancer agents has not been reported. The present study reveals, for the first time, that the plasma concentration of AMF decreased with a reduction in tumor weights in A549-xenografted mice treated with sunitinib or cetuximab.…”

Section: Discussionmentioning

confidence: 99%

“…Although the secretion of AMF by normal cells has not been observed, its secretion into culture medium has been identified in various cancer cells. Clinical studies measuring AMF in the serum or urine of patients with lung, gastrointestinal and renal cancer, have suggested that it may be a useful biomarker for certain types of cancer (6,7). In addition to the cell motility stimulating activity, AMF is involved in cellular proliferation (8), cellular survival (9), invasion of malignant cells (10), tumor metastasis (11) and the induction of angiogenesis (12).…”

Section: Introductionmentioning

confidence: 99%

Monoclonal antibodies against autocrine motility factor suppress gastric cancer

et al. 2017

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Abstract. Autocrine motility factor (AMF), which is a secreted form of phosphoglucose isomerase, is mainly secreted by various tumors and has cytokine-like activity. AMF is known to stimulate proliferation, survival and metastasis of cancer cells, and angiogenesis within a tumor. The present study investigated whether inhibition of AMF using targeted-antibodies was able to suppress the growth of cancer. A migration assay using a Boyden chamber was utilized to measure the activity of AMF on the motility of cancer cells. A recombinant human AMF (rhAMF) prepared from E. coli transformed with the pET22b-AMF vector increased the motility of MDA-MB-231 and A549 cells, but it did not affect that of NCI-N87 or HepG2 cells, which exhibited the ability to secrete high amounts of their own endogenous AMF into the culture medium. The extent to which the AMF receptor was expressed on cancer cells did not correlate clearly with the cell motility stimulated by rhAMF. In A549-xenografted nude mice treated with sunitinib or cetuximab, a decrease in the plasma AMF concentration was accompanied by a reduction in tumor weight, suggesting an association between the plasma AMF concentration and anticancer activity. A monoclonal antibody (9A-4H), which revealed a high binding affinity for E. coli-derived rhAMF, significantly suppressed the growth of tumors in Balb/c nude mice transplanted with the human gastric cancer cell line NCI-N87, to the similar extent as trastuzumab, an anticancer antibody. The present study suggests, for the first time, that an antibody specific to AMF may be a therapeutic agent for gastric cancer. IntroductionPhosphoglucose isomerase (PGI), also termed phosphohexose isomerase (PHI), is a glycolytic enzyme that catalyzes the interconversion of glucose-6-phosphate and fructose-6-phosphate in the glycolysis process. A secreted version of PGI/PHI, which has cytokine activity, was originally purified from the conditioned culture medium of human melanoma cells and was termed autocrine motility factor (AMF) owing to its ability to stimulate cell motility (1). Until the respective protein sequences were determined, AMF was termed neuroleukin, a maturation factor mediating differentiation of human myeloid leukemia cells, a myofibril-bound serine proteinase inhibitor, and sperm antigen-36 (2-5). Although the secretion of AMF by normal cells has not been observed, its secretion into culture medium has been identified in various cancer cells. Clinical studies measuring AMF in the serum or urine of patients with lung, gastrointestinal and renal cancer, have suggested that it may be a useful biomarker for certain types of cancer (6,7). In addition to the cell motility stimulating activity, AMF is involved in cellular proliferation (8), cellular survival (9), invasion of malignant cells (10), tumor metastasis (11) and the induction of angiogenesis (12).AMF binds to and stimulates the AMF receptor (AMFR), which is a 78 kDa glycoprotein (gp78) with seven transmembrane domains (13). When stimulated by AMF, AMFR activates signa...

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The value of tumour markers in lung cancer

Cited by 42 publications

References 26 publications

Down-Regulation of Phosphoglucose Isomerase/Autocrine Motility Factor Results in Mesenchymal-to-Epithelial Transition of Human Lung Fibrosarcoma Cells

Down-Regulation of Phosphoglucose Isomerase/Autocrine Motility Factor Results in Mesenchymal-to-Epithelial Transition of Human Lung Fibrosarcoma Cells

Identification of α-Enolase as an Autoantigen in Lung Cancer: Its Overexpression Is Associated with Clinical Outcomes

Monoclonal antibodies against autocrine motility factor suppress gastric cancer

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