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- HEPACAM abstract "Gene hapaCAM was identified, isolated, characterized and first reported by Shali Shen et al. in 2005[1]. The gene encodes a protein hepaCAM of 416 aa, which is a new immunoglobulin-like cell adhesion molecule and a putative tumor suppressor. The major biological functions of hepaCAM include a) modulating cell adhesion and migration and b) inhibiting cancer cell growth. Comparing the differential gene expression between hepatocellular carcinoma (HCC) and its adjacent non-tumorous tissues, Shen et al., identified more than 200 genes that were either up- or down-regulated in HCC. Sequencing analysis revealed a number of candidate molecules. These genes were then evaluated against a panel of HCC samples, leading to the identification of a novel gene HepN1[2]. Using HepN1 sequence, they subsequently cloned and characterized gene hepaCAM, named based on its original site of identification – hepatocytes and the nature of its protein product – an Ig-like cell adhesion molecule (CAM). To date, Shen’s team has reported that a) structurally, hepaCAM is a glycoprotein containing an extracellular domain with 2 Ig-like loops, a transmembrane region and a cytoplasmic tail[3]; b) matched to chromosome 11q24, gene hepaCAM is ubiquitously expressed in normal human tissues, highly expressed in the central nervous system (CNS), and is frequently suppressed in a variety of tumor types[4]; c) functionally, hepaCAM is involved in cell-extracellular matrix interactions and cell growth control of cancer cells[3], and is able to induce differentiation of glioblastoma cells[5]; d) in cell signaling, hepaCAM directly interacts with F-actin[6] and calveolin 1[7], and is capable of inducing senescence-like growth arrest via a p53/p21-dependent pathway[4]; and e) hepaCAM is proteolystically cleaved near the transmemberane region[8]. Refer to GenBank and PubMed for more information and findings.Other names of hepaCAM protein: glialCAM (when investigations done in the CNS in 2008[9]); hepaCAM1 (when hepaCAM2 emerged in 2010[10])References:1. Chung Moh M, Hoon Lee L, Shen S. Cloning and characterization of hepaCAM, a novel Ig-like cell adhesion molecule suppressed in human hepatocellular carcinoma. J Hepatol. 2005 Jun;42(6):833-41. Epub 2005 Apr 7.2. Moh MC, Lee LH, Yang X, Shen S. HEPN1, a novel gene that is frequently down-regulated in hepatocellular carcinoma, suppresses cell growth and induces apoptosis in HepG2 cells. J Hepatol. 2003 Oct;39(4):580-6.3. Moh MC, Zhang C, Luo C, Lee LH, Shen S. Structural and functional analyses of a novel ig-like cell adhesion molecule, hepaCAM, in the human breast carcinoma MCF7 cells. J Biol Chem. 2005 Jul 22;280(29):27366-74. Epub 2005 May 25.4. Moh MC, Zhang T, Lee LH, Shen S. Expression of hepaCAM is downregulated in cancers and induces senescence-like growth arrest via a p53/p21-dependent pathway in human breast cancer cells. Carcinogenesis. 2008 Dec;29(12):2298-305. Epub 2008 Oct 8.5. Lee LH, Moh MC, Zhang T, Shen S. The immunoglobulin-like cell adhesion molecule hepaCAM induces differentiation of human glioblastoma U373-MG cells. J Cell Biochem. 2009 Aug 15;107(6):1129-38.6. Moh MC, Tian Q, Zhang T, Lee LH, Shen S. The immunoglobulin-like cell adhesion molecule hepaCAM modulates cell adhesion and motility through direct interaction with the actin cytoskeleton. J Cell Physiol. 2009 May;219(2):382-91.7. Moh MC, Lee LH, Zhang T, Shen S. Interaction of the immunoglobulin-like cell adhesion molecule hepaCAM with caveolin-1. Biochem Biophys Res Commun. 2009 Jan 23;378(4):755-60. Epub 2008 Dec 6.8. Zhang T, Moh MC, Lee LH, Shen S. The immunoglobulin-like cell adhesion molecule hepaCAM is cleaved in the human breast carcinoma MCF7 cells. Int J Oncol. 2010 Jul;37(1):155-65.9. Favre-Kontula L, Rolland A, Bernasconi L, Karmirantzou M, Power C, Antonsson B, Boschert U. GlialCAM, an immunoglobulin-like cell adhesion molecule is expressed in glial cells of the central nervous system. Glia. 2008 Apr 15;56(6):633-45.10. Klopfleisch R, Klose P, da Costa A, Brunnberg L, Gruber AD. HEPACAM1 and 2 are differentially regulated in canine mammary adenomas and carcinomas and its lymph node metastases. BMC Vet Res. 2010 Mar 15;6:15.The hepatocyte cell adhesion molecules 1 and 2 (HEPACAM 1 and 2) are members of the immunoglobulin family of adhesion genes. HEPACAM1 is involved in negative cell cycle regulation via p53, p21 and p27 signalling but also mediates increased human breast cancer cell spread. Metastatic canine mammary carcinoma and their metastases are characterized by decreased HEPACAM2 but unchanged HEPACAM2 expression levels when compared to normal glands.".
- HEPACAM wikiPageID "30113806".
- HEPACAM wikiPageRevisionID "599754229".
- HEPACAM hasPhotoCollection HEPACAM.
- HEPACAM subject Category:Breast_cancer.
- HEPACAM subject Category:Immunoglobulin_superfamily.
- HEPACAM type BodyPart105220461.
- HEPACAM type Immunoglobulin-likeReceptors.
- HEPACAM type Part109385911.
- HEPACAM type PhysicalEntity100001930.
- HEPACAM type Receptor105608868.
- HEPACAM type Structure105225602.
- HEPACAM type Thing100002452.
- HEPACAM comment "Gene hapaCAM was identified, isolated, characterized and first reported by Shali Shen et al. in 2005[1]. The gene encodes a protein hepaCAM of 416 aa, which is a new immunoglobulin-like cell adhesion molecule and a putative tumor suppressor. The major biological functions of hepaCAM include a) modulating cell adhesion and migration and b) inhibiting cancer cell growth.".
- HEPACAM label "HEPACAM".
- HEPACAM sameAs m.0g58g1j.
- HEPACAM sameAs Q5629453.
- HEPACAM sameAs Q5629453.
- HEPACAM sameAs HEPACAM.
- HEPACAM wasDerivedFrom HEPACAM?oldid=599754229.
- HEPACAM isPrimaryTopicOf HEPACAM.