Antigen expression associated with lymph node metastasis in gastric adenocarcinomas

Wang, Shi‐Nong ‐N; Miyauchi, M; Koshikawa, Nobuko; Maruyama, Koshi; Miura, Katsukiyo; Kurosawa, Yoshikazu; Awaya, Akira; Kanai, Yoshiyuki

doi:10.1111/j.1440-1827.1994.tb01682.x

Cited by 28 publications

(22 citation statements)

References 16 publications

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“…However, Calnuc was not only well-associated with autoimmune disease, the higher expression of Calnuc was also observed in cancer. For example, a study on gastric adenocarcinoma has demonstrated that in 50 gastric adenocarcinomas with lymph node metastasis, 56% of cases showed a positive reaction to Calnuc, which was much higher compared to that in 50 gastric adenocarcinomas without lymph node metastasis (10%) (30). In another study, Kubota and his colleagues tested the expression of Calnuc in non-Hodgkin's lymphoma by immunohistochemical staining with anti-human Nuc monoclonal antibody; >90% of tumor cells were stained with anti-Nuc, and 65% were in a high grade of histological malignancy, 54% in the intermediate grade and 22% in the low grade (31).…”

Section: Discussionmentioning

confidence: 99%

Autoantibodies to Ca2+ binding protein Calnuc is a potential marker in colon cancer detection

Chen

Lin²,

Qiu³

et al. 2007

Int J Oncol

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Section: Discussionmentioning

confidence: 99%

Autoantibodies to Ca2+ binding protein Calnuc is a potential marker in colon cancer detection

Chen

Lin²,

Qiu³

et al. 2007

Int J Oncol

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“…The C-terminal (CT) region following the leucine zipper domain is predicted to be intrinsically disordered and unstructured. Intriguingly, NUCB1 is strongly conserved from flies to humans (21) and is widely distributed among Golgi (16,22), nucleus (19,23), endoplasmic reticulum (24,25), and cytoplasm (17). The N-terminal signal sequence of NUCB1 targets it to different membrane compartments and its deletion renders NUCB1 cytosolic.…”

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confidence: 99%

Nucleobindin 1 Is a Calcium-regulated Guanine Nucleotide Dissociation Inhibitor of Gαi1

Kapoor

Gupta

Menon

et al. 2010

Journal of Biological Chemistry

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Nucleobindin 1 (NUCB1) is a widely expressed multidomain calcium-binding protein whose precise physiological and biochemical functions are not well understood. We engineered and heterologously expressed a soluble form of NUCB1 (sNUCB1) and characterized its biophysical and biochemical properties. We show that sNUCB1 exists as a dimer in solution and that each monomer binds two divalent calcium cations. Calcium binding causes conformational changes in sNUCB1 as judged by circular dichroism and fluorescence spectroscopy experiments. Earlier reports suggested that NUCB1 might interact with heterotrimeric G protein ␣ subunits. We show that dimeric calcium-free sNUCB1 binds to expressed G␣ i1 and that calcium binding inhibits the interaction. The binding of sNUCB1 to G␣ i1 inhibits its basal rate of GDP release and slows its rate and extent of GTP␥S uptake. Additionally, our tissue culture experiments show that sNUCB1 prevents receptor-mediated G␣ i -dependent inhibition of adenylyl cyclase. Thus, we conclude that sNUCB1 is a calcium-dependent guanine nucleotide dissociation inhibitor (GDI) for G␣ i1 . To our knowledge, sNUCB1 is the first example of a calcium-dependent GDI for heterotrimeric G proteins. We also show that the mechanism of GDI activity of sNUCB1 is unique and does not arise from the consensus GoLoco motif found in RGS proteins. We propose that cytoplasmic NUCB1 might function to regulate heterotrimeric G protein trafficking and G protein-coupled receptor-mediated signal transduction pathways.Heterotrimeric guanine nucleotide-binding proteins, G proteins, couple to heptahelical cell surface G protein-coupled receptors (GPCRs) 3 and participate in intracellular signaling events. The G protein heterotrimer is composed of the G␣ subunit and the G␤␥ heterodimer. Upon ligand-mediated activation, GPCRs catalyze the exchange of GDP for GTP on G␣ leading to dissociation of the heterotrimer into G␣⅐GTP and G␤␥ subunits (1-3). These individual subunits then regulate downstream signaling cascades involving effector systems like adenylyl cyclases, Ca 2ϩ and K ϩ channels, phospholipase C isozymes, and cyclic nucleotide phosphodiesterases (4, 5). Thereafter, the intrinsic GTPase activity of G␣ reverts it back to the GDP-bound state, which can reassociate with G␤␥. This inhibits the interaction of G protein subunits with downstream effectors, which results in the turning-off of the signaling pathways. Hence, signaling by heterotrimeric G proteins is directly dependent on the lifetime of the GTP-bound state of G␣. This lifetime is regulated by GTPase-accelerating proteins (GAPs), which catalyze the rapid hydrolysis of the G␣-bound GTP to GDP and by guanine nucleotide dissociation inhibitors (GDIs), which inhibit the exchange of GDP for GTP in the catalytic pocket of G␣ (6).Together, GAPs and GDIs exert a regulatory control on G protein signaling. In recent years, novel interacting partners of heterotrimeric G proteins called the regulators of G protein signaling or RGS proteins have been discovered that possess GAP ...

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“…Wang et al studied the antigenic expression of calnuc in gastric adenocarcinomas with lymph-node metastasis by immunohistochemical reactivity studies in patients with and without this tumor (45). It was observed that calnuc was expressed in 56% of patients with lymph-node metastatic tumor when compared with just 10% of patients with tumors not related to lymph node metastasis.…”

Section: Calnuc-related Diseasesmentioning

confidence: 99%

Calnuc: Emerging roles in calcium signaling and human diseases

et al. 2010

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SummaryCalnuc is a recently discovered multidomain protein with EF-hand calcium binding sites. Several studies have reported various interacting partners for calnuc and, therefore, also different sites of localization in the cell. It interacts with important molecules such as DNA, G protein, COX, and amyloid precursor protein among others in addition to being involved in stress response and trafficking. The immense possibilities (of various functions this protein might be involved in) implicate great future in medicine and physiology. Preliminary studies also implicate the possibility of calnuc being involved in some of the human diseases. These initial observations imply the functions that this protein might be involved in. This review emphasizes the importance of further research on this protein. IUBMBIUBMB Life, 62(6): [436][437][438][439][440][441][442][443][444][445][446] 2010

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Antigen expression associated with lymph node metastasis in gastric adenocarcinomas

Cited by 28 publications

References 16 publications

Autoantibodies to Ca2+ binding protein Calnuc is a potential marker in colon cancer detection

Autoantibodies to Ca2+ binding protein Calnuc is a potential marker in colon cancer detection

Nucleobindin 1 Is a Calcium-regulated Guanine Nucleotide Dissociation Inhibitor of Gαi1

Calnuc: Emerging roles in calcium signaling and human diseases

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