Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0699790 (colon cancer)
 28,837 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We have identified a novel gene, designated KRAP (Ki- ras-induced actin-interacting protein), encoding a protein of 1,259 amino acids with coiled-coil regions and transmembrane regions, from the cDNA library of human colon cancer HCT116 cells, as one of the genes upregulated by activated Ki- ras. While KRAP was rarely expressed in normal colon epithelium, deregulated constitutive KRAP expression was observed in some other colon cancer cells. In normal tissues, KRAP was strongly expressed in pancreas and testis. Anti-KRAP polyclonal antibodies detected endogenous KRAP as the molecular size of Mr 180,000, and immunofluorescence microscopy and cytochalasin E treatment revealed that KRAP was clearly associated with the actin filaments. Furthermore, KRAP was localized as a membrane-bound form with extracellular regions. These results together suggested KRAP might be involved in the regulation of filamentous actin and signals from the outside of the cells.
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PMID:Deregulated expression of KRAP, a novel gene encoding actin-interacting protein, in human colon cancer cells. 1467 6

We previously identified the human KRAP (Ki-ras-induced actin-interacting protein) gene from the cDNA library of human colon cancer HCT116 cells as one of the genes whose expression levels were up-regulated by activated Ki-ras. Although the KRAP gene is structurally conserved from fish to mammalian species, the expression pattern and function of KRAP still remain to be elucidated. Here, we have generated a specific polyclonal antibody for KRAP and characterized the histological expression of KRAP in mouse tissues. KRAP was ubiquitously expressed in mouse tissues, with high levels in pancreas, liver, and brown adipose tissues, and KRAP was co-localized with filamentous actin along the apical membranes in both pancreas and liver tissues. A subfractionation study revealed that KRAP is a cytoplasmic protein and that the majority is associated with the cytoskeleton. Furthermore, microarray gene expression profile by inhibiting KRAP expression in HCT116 cells showed that several receptors and signal molecules frequently deregulated in cancers were differentially expressed in the KRAP-knockdown cells. All of these results suggested that KRAP might be a cytoskeleton-associated protein involving the structural integrity and/or signal transductions in human cancers.
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PMID:Analysis of KRAP expression and localization, and genes regulated by KRAP in a human colon cancer cell line. 1793 91

We previously reported that Tespa1 (thymocyte-expressed, positive selection-associated gene 1) protein expressed in lymphocytes physically interacts with IP3R (Inositol 1,4,5-trisphosphate receptor), a Ca(2+) channel protein spanning endoplasmic reticulum (ER) membrane. However, the biochemical characterization of Tespa1 protein remains unknown. In this study, we have found that Tespa1 protein was posttranslationally modified upon intracellular Ca(2+) increase in thymocytes. Through the analyses using various inhibitors, store-operated Ca(2+) entry (SOCE) was found to be an essential factor for the Tespa1 protein modification induced by T cell receptor (TCR)-stimulation. Remarkably, the Ca(2+)-dependent Tespa1 protein modification was restored by in vitro protein phosphatase treatment, indicating that this modification was due to phosphorylation. Moreover, we examined whether Ca(2+)-dependent phosphorylation of Tespa1 protein would affect the physical association between Tespa1 and IP3R proteins, revealing that physical association of these proteins is maintained regardless of the presence or absence of phosphorylation of Tespa1. In addition, KRAP protein which represents substantial amino acid sequence homology to Tespa1 was also posttranslationally phosphorylated by intracellular Ca(2+) increase in HCT116 human colon cancer cells and HEK293 human embryonic kidney cells, suggesting that common signaling mechanism(s) may contribute to the molecular modification of Tespa1 and KRAP in different cellular processes. All these results suggested a novel molecular modification of Tespa1 and the existence of the regulatory pathway that SOCE affects the Tespa1-IP3R molecular complex.
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PMID:Tespa1 protein is phosphorylated in response to store-operated calcium entry. 2354 77