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Jiro Fujita - One of the best experts on this subject based on the ideXlab platform.
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Full-length Cytokeratin 8 is released and circulates in patients with non-small cell lung cancer.
Tumor Biology, 2008Co-Authors: Tomoya Ishii, Jiro Fujita, Yuji Ohtsuki, Shuji Bandoh, Yasunori Tojo, Nobuhiro Kanaji, Yoko Fukunaga, Yutaka Ueda, Toshihiko Ishida, Akihito KuboAbstract:Background/Aim: Cytokeratin 8 (CK8) is a type II intermediate filament protein that is persistently expressed in most epithelial malignancies. Circulating CK-related polypeptides ha
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Aberrant messenger RNA splicing of the Cytokeratin 8 in lung cancer.
Lung Cancer, 2003Co-Authors: Yasunori Tojo, Jiro Fujita, Tomoya Ishii, Shuji Bandoh, Yoko Fukunaga, Yutaka Ueda, Akihito Kubo, Yu Yang, Cheng-long HuangAbstract:Cytokeratin 8 (CK8) is one of the cytoskeletal components and shows caspase-mediated degradation when cells undergo apoptosis. We previously reported that CK8 is highly expressed in non-small cell lung cancer (NSCLC) cell lines and increasing values of serum CK8 are significantly associated with tumor progression in patients with NSCLC. In this investigation, reverse transcriptase-polymerase chain reaction (RT-PCR) analysis in lung cancer cell lines, revealed a shorter PCR product, which differed from the wild-type product of CK8. The nucleotide sequence of the shorter PCR products and genomic DNA for CK8 demonstrated that the shorter product was an aberrantly spliced form of CK8 (AS-CK8) which lacked a caspases cleavage site within the linker lesion in exon 5. The putative protein products predicted by the mRNA of AS-CK8 were demonstrated by Western blotting with monoclonal antibodies for CK8. In addition, AS-CK8 mRNA and its protein products were highly expressed in NSCLC cell lines compared with small-cell lung cancer (SCLC) cell lines. Tissue samples obtained from NSCLC patients also expressed mRNA of AS-CK8. In conclusion, we identified aberrantly spliced CK8 (AS-CK8) which lacked a caspases cleavage site in lung cancer cell lines and primary tumors of NSCLC. AS-CK8 was preferentially expressed in NSCLC, rather than SCLC. These findings lead to speculation that cancer cells expressing AS-CK8 may have a resistance to apoptosis and may perturb keratin network formation.
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expression of Cytokeratin 8 in lung cancer cell lines and measurement of serum Cytokeratin 8 in lung cancer patients
Lung Cancer, 2002Co-Authors: Yoko Fukunaga, Jiro Fujita, Satoko Hojo, Jiro Takahara, Shuji Bandoh, Yasunori Tojo, Yutaka Ueda, Yu Yang, Kazutaka Dohmoto, Toshihiko IshidaAbstract:It has been reported that Cytokeratin 8 (CK8) can be expressed in several cancers and expression of CK8 is correlated with increased invasiveness of the tumor in vitro and in vivo. In the present study, we investigated expressions of CK8 in human lung cancer cell lines. In addition, we also evaluated the clinical significance of CK8 measurements in sera of patients with lung cancer. Expression of mRNA for CK8 was semi-quantitatively evaluated by the competitive reverse transcriptase-polymerase chain reaction (competitive RT-PCR), using human lung cancer cell lines. The level of CK8 protein in culture supernatants of lung cancer cell lines and 70 sera of patients with lung cancer was measured by enzyme-linked immunosorbent assay (ELISA). Levels of serum CK8 according to clinical parameters were also examined. The level of expression of CK8 mRNA in non-small cell lung cancer (NSCLC) cell lines was significantly high compared with that of small cell lung cancer (SCLC) cell lines (P<0.05). The level of CK8 in culture supernatants in NSCLC was significantly high compared with that of SCLC. The level of serum CK8 in patients with NSCLC was significantly high compared with that of normal non-smokers and compared with that of SCLC (P<0.05). Patients with a CK8 value of 50.0 ng/ml, or higher, had a statistically significant diminished survival compared with those patients whose CK8 values were lower. In conclusion, CK8 was preferentially expressed in NSCLC. Increasing values of CK8 were significantly associated with tumor progression and decreased survival in patients with NSCLC. Therefore, CK8 in sera may become a novel tumor marker in patients with lung cancer.
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Expression of Cytokeratin 8 in lung cancer cell lines and measurement of serum Cytokeratin 8 in lung cancer patients.
Lung Cancer, 2002Co-Authors: Yoko Fukunaga, Jiro Fujita, Satoko Hojo, Jiro Takahara, Shuji Bandoh, Yasunori Tojo, Yutaka Ueda, Yu Yang, Kazutaka Dohmoto, Toshihiko IshidaAbstract:It has been reported that Cytokeratin 8 (CK8) can be expressed in several cancers and expression of CK8 is correlated with increased invasiveness of the tumor in vitro and in vivo. In the present study, we investigated expressions of CK8 in human lung cancer cell lines. In addition, we also evaluated the clinical significance of CK8 measurements in sera of patients with lung cancer. Expression of mRNA for CK8 was semi-quantitatively evaluated by the competitive reverse transcriptase-polymerase chain reaction (competitive RT-PCR), using human lung cancer cell lines. The level of CK8 protein in culture supernatants of lung cancer cell lines and 70 sera of patients with lung cancer was measured by enzyme-linked immunosorbent assay (ELISA). Levels of serum CK8 according to clinical parameters were also examined. The level of expression of CK8 mRNA in non-small cell lung cancer (NSCLC) cell lines was significantly high compared with that of small cell lung cancer (SCLC) cell lines (P
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circulating Cytokeratin 8 anti Cytokeratin 8 antibody immune complexes in sera of patients with pulmonary fibrosis
Respiration, 2000Co-Authors: N. Dobashi, Jiro Fujita, Yuji Ohtsuki, Ichiro Yamadori, Takeo Yoshinouchi, Tadashi Kamei, Michiaki Tokuda, Satoko Hojo, Shuji Bandou, Yutaka UedaAbstract:Background: It has been suggested that the humoral immune system plays a role in the pathogenesis of idiopathic pulmonary fibrosis (IPF) and pulmonary fibrosis associated with colla
Yutaka Ueda - One of the best experts on this subject based on the ideXlab platform.
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Full-length Cytokeratin 8 is released and circulates in patients with non-small cell lung cancer.
Tumor Biology, 2008Co-Authors: Tomoya Ishii, Jiro Fujita, Yuji Ohtsuki, Shuji Bandoh, Yasunori Tojo, Nobuhiro Kanaji, Yoko Fukunaga, Yutaka Ueda, Toshihiko Ishida, Akihito KuboAbstract:Background/Aim: Cytokeratin 8 (CK8) is a type II intermediate filament protein that is persistently expressed in most epithelial malignancies. Circulating CK-related polypeptides ha
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Aberrant messenger RNA splicing of the Cytokeratin 8 in lung cancer.
Lung Cancer, 2003Co-Authors: Yasunori Tojo, Jiro Fujita, Tomoya Ishii, Shuji Bandoh, Yoko Fukunaga, Yutaka Ueda, Akihito Kubo, Yu Yang, Cheng-long HuangAbstract:Cytokeratin 8 (CK8) is one of the cytoskeletal components and shows caspase-mediated degradation when cells undergo apoptosis. We previously reported that CK8 is highly expressed in non-small cell lung cancer (NSCLC) cell lines and increasing values of serum CK8 are significantly associated with tumor progression in patients with NSCLC. In this investigation, reverse transcriptase-polymerase chain reaction (RT-PCR) analysis in lung cancer cell lines, revealed a shorter PCR product, which differed from the wild-type product of CK8. The nucleotide sequence of the shorter PCR products and genomic DNA for CK8 demonstrated that the shorter product was an aberrantly spliced form of CK8 (AS-CK8) which lacked a caspases cleavage site within the linker lesion in exon 5. The putative protein products predicted by the mRNA of AS-CK8 were demonstrated by Western blotting with monoclonal antibodies for CK8. In addition, AS-CK8 mRNA and its protein products were highly expressed in NSCLC cell lines compared with small-cell lung cancer (SCLC) cell lines. Tissue samples obtained from NSCLC patients also expressed mRNA of AS-CK8. In conclusion, we identified aberrantly spliced CK8 (AS-CK8) which lacked a caspases cleavage site in lung cancer cell lines and primary tumors of NSCLC. AS-CK8 was preferentially expressed in NSCLC, rather than SCLC. These findings lead to speculation that cancer cells expressing AS-CK8 may have a resistance to apoptosis and may perturb keratin network formation.
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expression of Cytokeratin 8 in lung cancer cell lines and measurement of serum Cytokeratin 8 in lung cancer patients
Lung Cancer, 2002Co-Authors: Yoko Fukunaga, Jiro Fujita, Satoko Hojo, Jiro Takahara, Shuji Bandoh, Yasunori Tojo, Yutaka Ueda, Yu Yang, Kazutaka Dohmoto, Toshihiko IshidaAbstract:It has been reported that Cytokeratin 8 (CK8) can be expressed in several cancers and expression of CK8 is correlated with increased invasiveness of the tumor in vitro and in vivo. In the present study, we investigated expressions of CK8 in human lung cancer cell lines. In addition, we also evaluated the clinical significance of CK8 measurements in sera of patients with lung cancer. Expression of mRNA for CK8 was semi-quantitatively evaluated by the competitive reverse transcriptase-polymerase chain reaction (competitive RT-PCR), using human lung cancer cell lines. The level of CK8 protein in culture supernatants of lung cancer cell lines and 70 sera of patients with lung cancer was measured by enzyme-linked immunosorbent assay (ELISA). Levels of serum CK8 according to clinical parameters were also examined. The level of expression of CK8 mRNA in non-small cell lung cancer (NSCLC) cell lines was significantly high compared with that of small cell lung cancer (SCLC) cell lines (P<0.05). The level of CK8 in culture supernatants in NSCLC was significantly high compared with that of SCLC. The level of serum CK8 in patients with NSCLC was significantly high compared with that of normal non-smokers and compared with that of SCLC (P<0.05). Patients with a CK8 value of 50.0 ng/ml, or higher, had a statistically significant diminished survival compared with those patients whose CK8 values were lower. In conclusion, CK8 was preferentially expressed in NSCLC. Increasing values of CK8 were significantly associated with tumor progression and decreased survival in patients with NSCLC. Therefore, CK8 in sera may become a novel tumor marker in patients with lung cancer.
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Expression of Cytokeratin 8 in lung cancer cell lines and measurement of serum Cytokeratin 8 in lung cancer patients.
Lung Cancer, 2002Co-Authors: Yoko Fukunaga, Jiro Fujita, Satoko Hojo, Jiro Takahara, Shuji Bandoh, Yasunori Tojo, Yutaka Ueda, Yu Yang, Kazutaka Dohmoto, Toshihiko IshidaAbstract:It has been reported that Cytokeratin 8 (CK8) can be expressed in several cancers and expression of CK8 is correlated with increased invasiveness of the tumor in vitro and in vivo. In the present study, we investigated expressions of CK8 in human lung cancer cell lines. In addition, we also evaluated the clinical significance of CK8 measurements in sera of patients with lung cancer. Expression of mRNA for CK8 was semi-quantitatively evaluated by the competitive reverse transcriptase-polymerase chain reaction (competitive RT-PCR), using human lung cancer cell lines. The level of CK8 protein in culture supernatants of lung cancer cell lines and 70 sera of patients with lung cancer was measured by enzyme-linked immunosorbent assay (ELISA). Levels of serum CK8 according to clinical parameters were also examined. The level of expression of CK8 mRNA in non-small cell lung cancer (NSCLC) cell lines was significantly high compared with that of small cell lung cancer (SCLC) cell lines (P
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circulating Cytokeratin 8 anti Cytokeratin 8 antibody immune complexes in sera of patients with pulmonary fibrosis
Respiration, 2000Co-Authors: N. Dobashi, Jiro Fujita, Yuji Ohtsuki, Ichiro Yamadori, Takeo Yoshinouchi, Tadashi Kamei, Michiaki Tokuda, Satoko Hojo, Shuji Bandou, Yutaka UedaAbstract:Background: It has been suggested that the humoral immune system plays a role in the pathogenesis of idiopathic pulmonary fibrosis (IPF) and pulmonary fibrosis associated with colla
Steven L. Gonias - One of the best experts on this subject based on the ideXlab platform.
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Cytokeratin 8 functions as a major plasminogen receptor in select epithelial and carcinoma cells.
Frontiers in Bioscience, 2001Co-Authors: Steven L. Gonias, Todd A. Hembrough, Mauricio SankovicAbstract:Cytokeratin 8 (K8) is a member of the intermediate filament (IF) gene family expressed by simple epithelial cells and by some carcinoma cells. The majority of the cellular K8 is assembled with its partner, K18, into highly insoluble 10 nm filaments that extend from the nucleus to the internal leaflet of the plasma membrane. At desmosomes and hemidesmosomes, K8, K18, and other IF proteins are bridged to proteins with transmembrane domains by a family of proteins called plakins. K8 does not have a signal peptide or a well-defined transmembrane domain; however, there is substantial evidence that this protein is available to bind plasminogen and K8-specific antibodies on the surfaces of certain epithelial cells in culture, including hepatocytes, hepatocellular carcinoma cells, and various breast cancer cell lines. This may reflect a novel mechanism of protein penetration through the plasma membrane or binding of secreted K8 to other cell-surface molecules. Cancer cells are known to secrete K8-containing protein complexes in vitro and in vivo. These complexes bind plasminogen as well. The plasminogen-binding activity of K8 is unique amongst IF proteins, probably because its sequence includes a carboxyl-terminal Lys residue. However, a K8 mutant that lacks the C-terminal Lys still binds plasminogen, albeit with decreased affinity. K18 does not bind plasminogen; however, K8 and K18 bind tissue-type plasminogen activator (tPA) equivalently. tPA-binding to K18 may be important in the mechanism whereby K8-K18 complexes promote plasminogen activation by tPA. Numerous studies have demonstrated correlations between high levels of K8 expression and increased migration and invasion of certain cancer cells. These correlations are most easily explained by the function of IF proteins in determining the rigidity of the cytoskeleton; however, the function of cell-surface K8 as a plasminogen receptor merits consideration. We have demonstrated that certain aggressive breast cancer cell lines, which have highly activated endogenous urokinase type-plasminogen activator (uPA)-uPA receptor (uPAR) systems, do not express high levels of cell-surface K8. The membrane macromolecule that is responsible for plasminogen-binding and for supporting activation of plasminogen by uPA on the surfaces of these cell types remains to be determined. This review focuses on the function of K8 as a plasminogen receptor and its potential role in cancer.
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Characterization of the binding sites for plasminogen and tissue-type plasminogen activator in Cytokeratin 8 and Cytokeratin 18.
Journal of Protein Chemistry, 1998Co-Authors: Kristen R. Kralovich, Todd A. Hembrough, Donna J. Webb, Larry R. Karns, Steven L. GoniasAbstract:Cytokeratin 8 (CK8) is an intermediate filament protein that penetrates to the external surfaces of breast cancer cells and is released from cells in the form of soluble heteropolymers. CK8 binds plasminogen and tissue-type plasminogen activator (t-PA) and accelerates plasminogen activation on cancer cell surfaces. The plasminogen-binding site is located at the C-terminus of CK8. In this study, we prepared GST-fusion proteins which contained either 174 amino acids from the C-terminus of CK8 (CK8f) or 134 amino acids from the C-terminus of CK18 (CK18f). A third GST-CK fusion protein was identical to CK8f except that the C-terminal lysine was mutated to glutamine (CK8fK483Q). CK8f bound plasminogen; the K D was 0.5 μM. Binding was completely inhibited by eACA. CK8fK483Q also bound plasminogen, albeit with decreased affinity (K D ≍ 1.5 μM). CK18f did not bind plasminogen at all. All three fusion proteins bound t-PA equivalently, providing the first evidence that CK18 may function as a t-PA receptor. t-PA and plasminogen cross-competed for binding to CK8f. Thus, t-PA and plasminogen cannot bind to the same CK8f monomer simultaneously. Nevertheless, CK8f still promoted plasminogen activation, probably reflecting the fact that CK8f was purified in dimeric or tetrameric form. These studies demonstrate that CK8 may promote plasminogen activation by t-PA only when present in an oligomerized state. CK18 may participate in the oligomer, together with CK8, based on its ability to bind t-PA.
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cell surface Cytokeratin 8 is the major plasminogen receptor on breast cancer cells and is required for the accelerated activation of cell associated plasminogen by tissue type plasminogen activator
Journal of Biological Chemistry, 1996Co-Authors: Todd A. Hembrough, Steven L. GoniasAbstract:Cytokeratin 8 (CK 8) has been identified on the external surfaces of viable, unpermeabilized epithelial cells (Hembrough, T. A., Vasudevan, J., Allietta, M. M., Glass, W. F., and Gonias, S. L. (1995) J. Cell Sci. 108, 1071-1082). In this study, we demonstrated that CK 8 is the major plasminogen-binding protein in plasma membrane fractions isolated from three breast cancer cell lines, BT20, MCF-7, and MDA-MB-157. To assess the function of CK 8 as a plasminogen receptor, monoclonal antibody 1E8 was raised against the carboxyl-terminal 12 amino acids of CK 8. The 1E8 epitope was present on the external surfaces of breast cancer cells, as determined by immunofluorescence microscopy. 125I-1E8 bound to MCF-7 cells; the maximum binding capacity (1.5 x 10(6) sites per cell) was comparable with that determined for plasminogen. When MCF-7 cells were incubated with Fab fragments of 1E8, specific 125I-plasminogen binding was decreased up to 82%. Specific plasminogen binding was decreased up to 67%, even when the unbound 1E8 Fab was removed by washing the cells prior to adding 125I-plasminogen. Preincubation with 1E8 Fab decreased plasminogen binding to BT20 and MDA-MB-157 cells, although to a lesser extent than with MCF-7 cells. Plasminogen activation by tissue-type plasminogen activator was greatly accelerated, due to a large decrease in Km, when the plasminogen was bound to MCF-7 cells. Pretreatment with 1E8 Fab decreased the rate of plasminogen activation by up to 83%, implicating CK 8 in the MCF-7 cell-accelerated reaction. These studies identify cell-surface CK 8 as a major plasminogen receptor in breast cancer cells and as a required component for the rapid activation of cell-associated plasminogen by tissue-type plasminogen activator.
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Cytokeratin 8 released by breast carcinoma cells in vitro binds plasminogen and tissue-type plasminogen activator and promotes plasminogen activation
Biochemical Journal, 1996Co-Authors: Todd A. Hembrough, Kristen R. Kralovich, Li Li, Steven L. GoniasAbstract:Cell-surface activation of plasminogen may be important in diseases that involve cellular migration, including atherosclerosis and tumour invasion/metastasis. Cytokeratin 8 (CK 8) has been identified as a plasminogen-binding protein expressed on the external surfaces of hepatocytes and breast carcinoma cells [Hembrough, Vasudevan, Allietta, Glass and Gonias (1995) J. Cell Sci. 108 , 1071–1082]. In this investigation, we demonstrate that a soluble form of CK 8 is released into the culture medium of breast cancer cell lines. The released CK 8 is in the form of variably sized polymers that bind plasminogen and promote the activation of [Glu 1 ]plasminogen and [Lys 78 ]plasminogen by single-chain tissue-type plasminogen activator (sct-PA). To assess the mechanism by which CK 8 promotes plasminogen activation, CK 8 was purified from rat hepatocytes and immobilized in microtitre plates. Immobilized CK 8 bound 125 I-plasminogen and 125 I-sct-PA in a specific and saturable manner. The K D s were 160±40 nM and 250±48 nM, respectively. Activation of plasminogen bound to immobilized CK 8 was accelerated compared with plasminogen in solution, as determined using a coupled-substrate fluorescence assay and SDS/PAGE. The ability of CK 8 to promote plasminogen activation may be important in the pericellular spaces surrounding breast cancer cells and at the cell surface.
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A Cytokeratin 8-like protein with plasminogen-binding activity is present on the external surfaces of hepatocytes, HepG2 cells and breast carcinoma cell lines
Journal of Cell Science, 1995Co-Authors: Todd A. Hembrough, Jayanand Vasudevan, Margaretta Allietta, William F. Glass, Steven L. GoniasAbstract:Plasminogen binding to cell surfaces may be important for tumor invasion and other processes that involve cellular migration. In this investigation, the principal plasminogen-binding protein was identified in the plasma membrane fraction of rat hepatocytes. The protein had an apparent mass of 59 kDa, was insoluble in a spectrum of detergents, and was identical to Cytokeratin 8 (CK 8) as determined by sequence analysis of nine amino acids at the N terminus of two cyanogen bromide fragments. The 59 kDa protein bound CK 8-specific antibody in western blot analyses. These studies demonstrate that CK 8 or a CK 8-like protein binds plasminogen. Given this newly determined and potentially important CK 8 function, immunofluorescence and immunoelectron microscopy studies were performed to determine whether CK 8 may be present on the external surfaces of unpermeabilized, viable hepatocytes. All of the cells in each preparation were immunopositive with two separate CK 8-specific antibodies. A punctate pattern of immunofluorescence was detected on the cell surface with approximately even intensity from cell to cell. By immunoelectron microscopy, CK 8 was preferentially associated with microvilli. In order to determine whether other epithelial cells express cell-surface CK 8, immunofluorescence and immunoelectron microscopy studies were performed with HepG2 hepatocellular carcinoma cells and with BT20 and MCF-7 breast carcinoma cells. The pattern of antigen expression was equivalent with each cell type and comparable to that observed with hepatocytes. These studies support the hypothesis that CK 8 is associated with the external cell surface where it may express important proteinase receptor function.
Muhammad Muzzammil Edhi - One of the best experts on this subject based on the ideXlab platform.
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Cytokeratin 5/6 and Cytokeratin 8/18 expression in triple negative breast cancers: clinicopathologic significance in South-Asian population.
BMC Research Notes, 2018Co-Authors: Atif Ali Hashmi, Samreen Naz, Shumaila Kanwal Hashmi, Zubaida Fida Hussain, Muhammad Irfan, Syed Muhammad Abu Bakar, Naveen Faridi, Amir Nawaz Khan, Muhammad Muzzammil EdhiAbstract:Cytokeratin 5/6 and Cytokeratin 8/18 are basal and luminal markers of breast cancer and they have pathological and prognostic significance in breast cancer. We performed Cytokeratin 5/6 and CK8/18 immunohistochemistry on 150 cases of triple negative breast cancers and association with various clinicopathological features was evaluated. Positive CK5/6 expression was noted in 8% (12 cases) of TNBC while 2.4% (4 cases) showed focal positive (
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Cytokeratin 5 6 and Cytokeratin 8 18 expression in triple negative breast cancers clinicopathologic significance in south asian population
BMC Research Notes, 2018Co-Authors: Atif Ali Hashmi, Samreen Naz, Shumaila Kanwal Hashmi, Zubaida Fida Hussain, Muhammad Irfan, Naveen Faridi, Amir Nawaz Khan, Syed Muhammad Abu Bakar, Muhammad Muzzammil EdhiAbstract:Cytokeratin 5/6 and Cytokeratin 8/18 are basal and luminal markers of breast cancer and they have pathological and prognostic significance in breast cancer. We performed Cytokeratin 5/6 and CK8/18 immunohistochemistry on 150 cases of triple negative breast cancers and association with various clinicopathological features was evaluated. Positive CK5/6 expression was noted in 8% (12 cases) of TNBC while 2.4% (4 cases) showed focal positive (< 10%) and 89.3% (134) were negative with CK5/6. Complete loss of CK8/18 expression was seen in 4.7% (7 cases) while 32.7% (49 cases) revealed focal loss of CK8/18 and 62.7% (94 cases) showed intact normal expression of CK8/18. No significant association of CK5/6 and CK8/18 with various clinicopathological parameters was observed. We found a low expression of basal Cytokeratin (CK5/6) in TNBC our studied population, while loss/altered expression of CK8/18 in approximately 38% of TNBC. Although no prognostic relevance of these finding was noted in our study, however these findings are different from those reported in literature in other parts of the world. Therefore we suggest a more through immunohistochemical and genomic profiling of TNBC in our population for better understanding of this disease in this part of the world.
Toshihiko Ishida - One of the best experts on this subject based on the ideXlab platform.
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Full-length Cytokeratin 8 is released and circulates in patients with non-small cell lung cancer.
Tumor Biology, 2008Co-Authors: Tomoya Ishii, Jiro Fujita, Yuji Ohtsuki, Shuji Bandoh, Yasunori Tojo, Nobuhiro Kanaji, Yoko Fukunaga, Yutaka Ueda, Toshihiko Ishida, Akihito KuboAbstract:Background/Aim: Cytokeratin 8 (CK8) is a type II intermediate filament protein that is persistently expressed in most epithelial malignancies. Circulating CK-related polypeptides ha
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expression of Cytokeratin 8 in lung cancer cell lines and measurement of serum Cytokeratin 8 in lung cancer patients
Lung Cancer, 2002Co-Authors: Yoko Fukunaga, Jiro Fujita, Satoko Hojo, Jiro Takahara, Shuji Bandoh, Yasunori Tojo, Yutaka Ueda, Yu Yang, Kazutaka Dohmoto, Toshihiko IshidaAbstract:It has been reported that Cytokeratin 8 (CK8) can be expressed in several cancers and expression of CK8 is correlated with increased invasiveness of the tumor in vitro and in vivo. In the present study, we investigated expressions of CK8 in human lung cancer cell lines. In addition, we also evaluated the clinical significance of CK8 measurements in sera of patients with lung cancer. Expression of mRNA for CK8 was semi-quantitatively evaluated by the competitive reverse transcriptase-polymerase chain reaction (competitive RT-PCR), using human lung cancer cell lines. The level of CK8 protein in culture supernatants of lung cancer cell lines and 70 sera of patients with lung cancer was measured by enzyme-linked immunosorbent assay (ELISA). Levels of serum CK8 according to clinical parameters were also examined. The level of expression of CK8 mRNA in non-small cell lung cancer (NSCLC) cell lines was significantly high compared with that of small cell lung cancer (SCLC) cell lines (P<0.05). The level of CK8 in culture supernatants in NSCLC was significantly high compared with that of SCLC. The level of serum CK8 in patients with NSCLC was significantly high compared with that of normal non-smokers and compared with that of SCLC (P<0.05). Patients with a CK8 value of 50.0 ng/ml, or higher, had a statistically significant diminished survival compared with those patients whose CK8 values were lower. In conclusion, CK8 was preferentially expressed in NSCLC. Increasing values of CK8 were significantly associated with tumor progression and decreased survival in patients with NSCLC. Therefore, CK8 in sera may become a novel tumor marker in patients with lung cancer.
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Expression of Cytokeratin 8 in lung cancer cell lines and measurement of serum Cytokeratin 8 in lung cancer patients.
Lung Cancer, 2002Co-Authors: Yoko Fukunaga, Jiro Fujita, Satoko Hojo, Jiro Takahara, Shuji Bandoh, Yasunori Tojo, Yutaka Ueda, Yu Yang, Kazutaka Dohmoto, Toshihiko IshidaAbstract:It has been reported that Cytokeratin 8 (CK8) can be expressed in several cancers and expression of CK8 is correlated with increased invasiveness of the tumor in vitro and in vivo. In the present study, we investigated expressions of CK8 in human lung cancer cell lines. In addition, we also evaluated the clinical significance of CK8 measurements in sera of patients with lung cancer. Expression of mRNA for CK8 was semi-quantitatively evaluated by the competitive reverse transcriptase-polymerase chain reaction (competitive RT-PCR), using human lung cancer cell lines. The level of CK8 protein in culture supernatants of lung cancer cell lines and 70 sera of patients with lung cancer was measured by enzyme-linked immunosorbent assay (ELISA). Levels of serum CK8 according to clinical parameters were also examined. The level of expression of CK8 mRNA in non-small cell lung cancer (NSCLC) cell lines was significantly high compared with that of small cell lung cancer (SCLC) cell lines (P
