HEPACAM

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HEPACAM
Identifiers
Aliases HEPACAM, GlialCAM, MLC2A, MLC2B, hepatic and glial cell adhesion molecule, HEPACAM1
External IDs MGI: 1920177 HomoloGene: 17652 GeneCards: HEPACAM
Gene location (Human)
Chromosome 11 (human)
Chr. Chromosome 11 (human)[1]
Chromosome 11 (human)
Genomic location for HEPACAM
Genomic location for HEPACAM
Band 11q24.2 Start 124,919,193 bp[1]
End 124,936,412 bp[1]
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_152722

NM_175189

RefSeq (protein)

NP_689935

NP_780398

Location (UCSC) Chr 11: 124.92 – 124.94 Mb Chr 11: 37.37 – 37.39 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Hepatic and glial cell adhesion molecule (HEPACAM) is a protein encoded by HEPACAM gene. It was first discovered and characterised in human liver cells by Shali Shen in 2005.[5] The protein consists of 416 amino acids, and is a member of the immunoglobulin superfamily of cell adhesion molecules. The main biological functions of HEPACAM include a) modulating cell adhesion and migration, and b) inhibiting cancer cell growth.[5]

Discovery[edit]

Through differential screening of gene expression, over 200 genes were found to be either up- or down-regulated in a hepatocellular carcinoma patient. These genes were subsequently evaluated against a panel of human HCC specimens, leading to the identification of a novel gene HEPN1.[6] Based on the sequence of HEPN1, the new gene HEPACAM was then isolated and characterised.[7]

Characteristics and functions[edit]

Structurally, HEPACAM is a glycoprotein containing an extracellular domain with 2 Ig-like loops, a transmembrane region and a cytoplasmic domain.[7] Matched to chromosome 11q24, gene HEPACAM is ubiquitously expressed in normal human tissues, with particularly high expression levels in the central nervous system (CNS), and is frequently suppressed in a variety of tumour types.[8]

Functionally, HEPACAM is involved in cell-extracellular matrix interactions and growth control of cancer cells,[7] and is able to induce differentiation of glioblastoma cells.[9] In cell signaling, HEPACAM directly interacts with F-actin[10] and calveolin 1,[11] and is capable of inducing senescence-like growth arrest via a p53/p21-dependent pathway.[8] Moreover, HEPACAM is proteolystically cleaved near the transmemberane region.[12] These findings indicate that the new Ig-like cell adhesion molecule HEPACAM is also a tumour suppressor.[13] HEPACAM1 is involved in negative cell cycle regulation via p53, p21 and p27 signalling[8] but also mediates increased human breast cancer cell spread.[7][10]

References[edit]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000165478 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000046240 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". 
  4. ^ "Mouse PubMed Reference:". 
  5. ^ a b Chung Moh M, Hoon Lee L, Shen S (June 2005). "Cloning and characterization of hepaCAM, a novel Ig-like cell adhesion molecule suppressed in human hepatocellular carcinoma". Journal of Hepatology. 42 (6): 833–41. doi:10.1016/j.jhep.2005.01.025. PMID 15885354. 
  6. ^ Moh MC, Lee LH, Yang X, Shen S (October 2003). "HEPN1, a novel gene that is frequently down-regulated in hepatocellular carcinoma, suppresses cell growth and induces apoptosis in HepG2 cells". Journal of Hepatology. 39 (4): 580–6. doi:10.1016/S0168-8278(03)00359-3. PMID 12971969. 
  7. ^ a b c d Moh MC, Zhang C, Luo C, Lee LH, Shen S (July 2005). "Structural and functional analyses of a novel ig-like cell adhesion molecule, hepaCAM, in the human breast carcinoma MCF7 cells". The Journal of Biological Chemistry. 280 (29): 27366–74. doi:10.1074/jbc.M500852200. PMID 15917256. 
  8. ^ a b c Moh MC, Zhang T, Lee LH, Shen S (December 2008). "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. 29 (12): 2298–305. doi:10.1093/carcin/bgn226. PMID 18845560. 
  9. ^ Lee LH, Moh MC, Zhang T, Shen S (August 2009). "The immunoglobulin-like cell adhesion molecule hepaCAM induces differentiation of human glioblastoma U373-MG cells". Journal of Cellular Biochemistry. 107 (6): 1129–38. doi:10.1002/jcb.22215. PMID 19507233. 
  10. ^ a b Moh MC, Tian Q, Zhang T, Lee LH, Shen S (May 2009). "The immunoglobulin-like cell adhesion molecule hepaCAM modulates cell adhesion and motility through direct interaction with the actin cytoskeleton". Journal of Cellular Physiology. 219 (2): 382–91. doi:10.1002/jcp.21685. PMID 19142852. 
  11. ^ Moh MC, Lee LH, Zhang T, Shen S (January 2009). "Interaction of the immunoglobulin-like cell adhesion molecule hepaCAM with caveolin-1". Biochemical and Biophysical Research Communications. 378 (4): 755–60. doi:10.1016/j.bbrc.2008.11.119. PMID 19059381. 
  12. ^ Zhang T, Moh MC, Lee LH, Shen S (July 2010). "The immunoglobulin-like cell adhesion molecule hepaCAM is cleaved in the human breast carcinoma MCF7 cells". International Journal of Oncology. 37 (1): 155–65. doi:10.3892/ijo_00000663. PMID 20514407. 
  13. ^ Moh MC, Shen S (2009). "The roles of cell adhesion molecules in tumor suppression and cell migration: a new paradox". Cell Adhesion & Migration. 3 (4): 334–6. doi:10.4161/cam.3.4.9246. PMC 2802741Freely accessible. PMID 19949308.