HEPACAM

Last updated
HEPACAM
Identifiers
Aliases HEPACAM , GlialCAM, MLC2A, MLC2B, hepatic and glial cell adhesion molecule, HEPACAM1, HEPN1
External IDs OMIM: 611642 MGI: 1920177 HomoloGene: 17652 GeneCards: HEPACAM
Orthologs
SpeciesHumanMouse
Entrez

220296

72927

Ensembl

ENSG00000165478

ENSMUSG00000046240

UniProt

Q14CZ8

Q640R3

RefSeq (mRNA)

NM_152722

NM_175189

RefSeq (protein)

NP_689935

NP_780398

Location (UCSC) Chr 11: 124.92 – 124.94 Mb Chr 9: 37.28 – 37.3 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Gene HEPACAM*, named based on its original site of identification - hepatocytes and the nature of its protein product - a cell adhesion molecule (CAM), was first discovered and characterised in human liver and reported by Shali Shen (MD, PhD) in 2005. [5] The gene encodes a protein of 416 amino acids, designated as hepaCAM**, which is a new member of the immunoglobulin superfamily of cell adhesion molecules (IgSF CAM). The main biological functions of hepaCAM include a) modulating cell-matrix adhesion and migration, and b) inhibiting cancer cell growth. [5]

Contents

(Note: *HEPACAM, gene name; **hepaCAM, protein name)

Discovery

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

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 proteolytically cleaved near the transmemberane region. [12] These findings indicate that the new Ig-like cell adhesion molecule hepaCAM is also a tumour suppressor. [13]

Other names

  1. glialCAM, which was cloned from a human brain cDNA library in 2008 and found to be identical to hepaCAM; [14] and
  2. HEPACAM1, when HEPACAM2 emerged in 2010. [15]

About HEPACAM 2

Metastatic canine mammary carcinoma and their metastases are characterized by decreased HEPACAM2 but unchanged HEPACAM2 expression levels when compared to normal glands. [15]

Related Research Articles

<span class="mw-page-title-main">L1 (protein)</span> Mammalian protein found in Homo sapiens

L1, also known as L1CAM, is a transmembrane protein member of the L1 protein family, encoded by the L1CAM gene. This protein, of 200-220 kDa, is a neuronal cell adhesion molecule with a strong implication in cell migration, adhesion, neurite outgrowth, myelination and neuronal differentiation. It also plays a key role in treatment-resistant cancers due to its function. It was first identified in 1984 by M. Schachner who found the protein in post-mitotic mice neurons.

<span class="mw-page-title-main">Neural cell adhesion molecule</span> Mammalian protein found in Homo sapiens

Neural cell adhesion molecule (NCAM), also called CD56, is a homophilic binding glycoprotein expressed on the surface of neurons, glia and skeletal muscle. Although CD56 is often considered a marker of neural lineage commitment due to its discovery site, CD56 expression is also found in, among others, the hematopoietic system. Here, the expression of CD56 is mostly associated with, but not limited to, natural killer cells. CD56 has been detected on other lymphoid cells, including gamma delta (γδ) Τ cells and activated CD8+ T cells, as well as on dendritic cells. NCAM has been implicated as having a role in cell–cell adhesion, neurite outgrowth, synaptic plasticity, and learning and memory.

<span class="mw-page-title-main">CD31</span> Mammalian protein found in Homo sapiens

Platelet endothelial cell adhesion molecule (PECAM-1) also known as cluster of differentiation 31 (CD31) is a protein that in humans is encoded by the PECAM1 gene found on chromosome17q23.3. PECAM-1 plays a key role in removing aged neutrophils from the body.

<span class="mw-page-title-main">CD164</span> Protein-coding gene in the species Homo sapiens

Sialomucin core protein 24 also known as endolyn or CD164 is a protein that in humans is encoded by the CD164 gene. CD164 functions as a cell adhesion molecule.

<span class="mw-page-title-main">CD146</span> Protein-coding gene in the species Homo sapiens

CD146 also known as the melanoma cell adhesion molecule (MCAM) or cell surface glycoprotein MUC18, is a 113kDa cell adhesion molecule currently used as a marker for endothelial cell lineage. In humans, the CD146 protein is encoded by the MCAM gene.

<span class="mw-page-title-main">Poliovirus receptor-related 2</span> Protein-coding gene in the species Homo sapiens

Poliovirus receptor-related 2 (PVRL2), also known as nectin-2 and CD112, is a human plasma membrane glycoprotein.

<span class="mw-page-title-main">Epithelial cell adhesion molecule</span> Transmembrane glycoprotein

Epithelial cell adhesion molecule (EpCAM), also known as CD326 among other names, is a transmembrane glycoprotein mediating Ca2+-independent homotypic cell–cell adhesion in epithelia. EpCAM is also involved in cell signaling, migration, proliferation, and differentiation. Additionally, EpCAM has oncogenic potential via its capacity to upregulate c-myc, e-fabp, and cyclins A & E. Since EpCAM is expressed exclusively in epithelia and epithelial-derived neoplasms, EpCAM can be used as diagnostic marker for various cancers. It appears to play a role in tumorigenesis and metastasis of carcinomas, so it can also act as a potential prognostic marker and as a potential target for immunotherapeutic strategies.

<span class="mw-page-title-main">Poliovirus receptor-related 1</span> Protein-coding gene in the species Homo sapiens

Poliovirus receptor-related 1 (PVRL1), also known as nectin-1 and CD111 (formerly herpesvirus entry mediator C, HVEC) is a human protein of the immunoglobulin superfamily (IgSF), also considered a member of the nectins. It is a membrane protein with three extracellular immunoglobulin domains, a single transmembrane helix and a cytoplasmic tail. The protein can mediate Ca2+-independent cellular adhesion further characterizing it as IgSF cell adhesion molecule (IgSF CAM).

<span class="mw-page-title-main">Contactin 1</span> Protein-coding gene in the species Homo sapiens

Contactin 1, also known as CNTN1, is a protein which in humans is encoded by the CNTN1 gene.

<span class="mw-page-title-main">ALCAM</span> Protein-coding gene in the species Homo sapiens

CD166 antigen is a 100-105 kD typeI transmembrane glycoprotein that is a member of the immunoglobulin superfamily of proteins. In humans it is encoded by the ALCAM gene. It is also called CD166, MEMD, SC-1/DM-GRASP/BEN in the chicken, and KG-CAM in the rat.

<span class="mw-page-title-main">NFASC</span> Protein-coding gene in the species Homo sapiens

Neurofascin is a protein that in humans is encoded by the NFASC gene.

<span class="mw-page-title-main">Basal cell adhesion molecule</span> Protein-coding gene in the species Homo sapiens

Basal cell adhesion molecule, also known as Lutheran antigen, is a plasma membrane glycoprotein that in humans is encoded by the BCAM gene. BCAM has also recently been designated CD239.

<span class="mw-page-title-main">NRCAM</span> Protein-coding gene in the species Homo sapiens

Neuronal cell adhesion molecule is a protein that in humans is encoded by the NRCAM gene.

<span class="mw-page-title-main">PNKD</span> Protein-coding gene in the species Homo sapiens

PNKD is the abbreviation for a human neurological movement disorder paroxysmal nonkinesiogenic dyskinesia. Like many other human genetics disorders, PNKD also refers to the disease, the disease gene and the encoded protein. (PNKD) is a protein that in humans is encoded by the PNKD gene. Alternative splicing results in the transcription of three isoforms. The mouse ortholog is called brain protein 17 (Brp17).

<span class="mw-page-title-main">PCDHGC3</span> Protein-coding gene in the species Homo sapiens

Protocadherin gamma-C3 is a protein that in humans is encoded by the PCDHGC3 gene.

<span class="mw-page-title-main">CADM3</span> Protein-coding gene in the species Homo sapiens

Cell adhesion molecule 3 is a protein that in humans is encoded by the CADM3 gene.

<span class="mw-page-title-main">Neurotrimin</span> Protein-coding gene in the species Homo sapiens

Neurotrimin is a protein that in humans is encoded by the NTM gene.

<span class="mw-page-title-main">EGFL7</span> Protein-coding gene in the species Homo sapiens

EGF-like domain-containing protein 7 is a protein that in humans is encoded by the EGFL7 gene. Intron 7 of EGFL7 hosts the miR-126 microRNA gene.

JAML or Junctional Adhesion Molecule-Like, or AMICA1 is a JAM transmembrane protein family member. It is composed of two extracellular immunoglobulin-like domains, a membrane-spanning region, and a cytoplasmic tail involved in activation signaling. A known ligand of JAML is Coxsackie virus and Adenovirus Receptor which has been shown to localize to the tight junctions of epithelial cells.

<span class="mw-page-title-main">HEPN1</span> Protein-coding gene in the species Homo sapiens

Hepatocellular carcinoma, down-regulated 1 is a protein that in humans is encoded by the HEPN1 gene.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000165478 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000046240 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. 1 2 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. 1 2 3 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. 1 2 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. S2CID   21271941.
  10. ↑ 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. S2CID   206047365.
  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   2802741 . PMID   19949308.
  14. ↑ Favre-Kontula L, Rolland A, Bernasconi L, et al. (April 2008). "GlialCAM, an immunoglobulin-like cell adhesion molecule is expressed in glial cells of the central nervous system". Glia. 56 (6): 633–45. doi:10.1002/glia.20640. PMID   18293412. S2CID   27263006.
  15. 1 2 Klopfleisch R, Klose P, da Costa A, Brunnberg L, Gruber AD (2010). "HEPACAM1 and 2 are differentially regulated in canine mammary adenomas and carcinomas and its lymph node metastases". BMC Veterinary Research. 6: 15. doi: 10.1186/1746-6148-6-15 . PMC   2842258 . PMID   20226097.
This page is based on this Wikipedia article
Text is available under the CC BY-SA 4.0 license; additional terms may apply.
Images, videos and audio are available under their respective licenses.