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'''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.<ref name=pmid15885354>{{cite journal |vauthors=Chung Moh M, Hoon Lee L, Shen S |title=Cloning and characterization of hepaCAM, a novel Ig-like cell adhesion molecule suppressed in human hepatocellular carcinoma |journal=Journal of Hepatology |volume=42 |issue=6 |pages=833–41 | date=June  2005 |pmid=15885354 |doi=10.1016/j.jhep.2005.01.025}}</ref> The protein consists of 416 amino acids, and is a member of the [[IgSF CAM|immunoglobulin superfamily]] of [[cell adhesion molecule]]s. The main biological functions of HEPACAM include a) modulating [[cell adhesion]] and [[Cell migration|migration]], and b) inhibiting [[cancer]] [[cell growth]].<ref name=pmid15885354/>
Gene '''HEPACAM'''*, named based on its original site of identification - '''hepa'''tocytes 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.<ref name=pmid15885354>{{cite journal |vauthors=Chung Moh M, Hoon Lee L, Shen S |title=Cloning and characterization of hepaCAM, a novel Ig-like cell adhesion molecule suppressed in human hepatocellular carcinoma |journal=Journal of Hepatology |volume=42 |issue=6 |pages=833–41 | date=June  2005 |pmid=15885354 |doi=10.1016/j.jhep.2005.01.025}}</ref> The gene encodes a protein of 416 amino acids, designated as hepaCAM**, which is a new member of the [[IgSF CAM|immunoglobulin superfamily]] of [[cell adhesion molecule]]s ([[IgSF CAM]]). The main biological functions of hepaCAM include a) modulating cell-matrix adhesion and [[Cell migration|migration]], and b) inhibiting [[cancer]] [[cell growth]].<ref name=pmid15885354/>
 
(Note: *HEPACAM, gene name; **hepaCAM, protein name)


==Discovery==
==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]]'''''.<ref>{{cite journal |vauthors=Moh MC, Lee LH, Yang X, Shen S |title=HEPN1, a novel gene that is frequently down-regulated in hepatocellular carcinoma, suppresses cell growth and induces apoptosis in HepG2 cells |journal=Journal of Hepatology |volume=39 |issue=4 |pages=580–6 | date=October  2003 |pmid=12971969 |doi=10.1016/S0168-8278(03)00359-3}}</ref> Based on the sequence of ''HEPN1'', the new gene HEPACAM was then isolated and characterised.<ref name=pmid15917256>{{cite journal |vauthors=Moh MC, Zhang C, Luo C, Lee LH, Shen S |title=Structural and functional analyses of a novel ig-like cell adhesion molecule, hepaCAM, in the human breast carcinoma MCF7 cells |journal=The Journal of Biological Chemistry |volume=280 |issue=29 |pages=27366–74 | date=July  2005 |pmid=15917256 |doi=10.1074/jbc.M500852200}}</ref>
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]].<ref>{{cite journal |vauthors=Moh MC, Lee LH, Yang X, Shen S |title=HEPN1, a novel gene that is frequently down-regulated in hepatocellular carcinoma, suppresses cell growth and induces apoptosis in HepG2 cells |journal=Journal of Hepatology |volume=39 |issue=4 |pages=580–6 | date=October  2003 |pmid=12971969 |doi=10.1016/S0168-8278(03)00359-3}}</ref> Based on the sequence of HEPN1, the new gene HEPACAM was then isolated and characterised.<ref name=pmid15917256>{{cite journal |vauthors=Moh MC, Zhang C, Luo C, Lee LH, Shen S |title=Structural and functional analyses of a novel ig-like cell adhesion molecule, hepaCAM, in the human breast carcinoma MCF7 cells |journal=The Journal of Biological Chemistry |volume=280 |issue=29 |pages=27366–74 | date=July  2005 |pmid=15917256 |doi=10.1074/jbc.M500852200}}</ref>


==Characteristics and functions==
==Characteristics and functions==


Structurally, HEPACAM is a [[glycoprotein]] containing an extracellular domain with 2 Ig-like loops, a transmembrane region and a cytoplasmic domain.<ref name=pmid15917256/> 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.<ref name=pmid18845560>{{cite journal |vauthors=Moh MC, Zhang T, Lee LH, Shen S |title=Expression of hepaCAM is downregulated in cancers and induces senescence-like growth arrest via a p53/p21-dependent pathway in human breast cancer cells |journal=Carcinogenesis |volume=29 |issue=12 |pages=2298–305 | date=December  2008 |pmid=18845560 |doi=10.1093/carcin/bgn226}}</ref>  
Structurally, hepaCAM is a [[glycoprotein]] containing an extracellular domain with 2 Ig-like loops, a transmembrane region and a cytoplasmic domain.<ref name=pmid15917256/> 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.<ref name=pmid18845560>{{cite journal |vauthors=Moh MC, Zhang T, Lee LH, Shen S |title=Expression of hepaCAM is downregulated in cancers and induces senescence-like growth arrest via a p53/p21-dependent pathway in human breast cancer cells |journal=Carcinogenesis |volume=29 |issue=12 |pages=2298–305 | date=December  2008 |pmid=18845560 |doi=10.1093/carcin/bgn226}}</ref> Functionally, hepaCAM is involved in cell-extracellular matrix interactions and growth control of cancer cells,<ref name=pmid15917256/> and is able to induce differentiation of [[glioblastoma]] cells.<ref>{{cite journal |vauthors=Lee LH, Moh MC, Zhang T, Shen S |title=The immunoglobulin-like cell adhesion molecule hepaCAM induces differentiation of human glioblastoma U373-MG cells |journal=Journal of Cellular Biochemistry |volume=107 |issue=6 |pages=1129–38 | date=August  2009 |pmid=19507233 |doi=10.1002/jcb.22215}}</ref> In cell signaling, hepaCAM directly interacts with [[F-actin]]<ref name=pmid19142852>{{cite journal |vauthors=Moh MC, Tian Q, Zhang T, Lee LH, Shen S |title=The immunoglobulin-like cell adhesion molecule hepaCAM modulates cell adhesion and motility through direct interaction with the actin cytoskeleton |journal=Journal of Cellular Physiology |volume=219 |issue=2 |pages=382–91 | date=May  2009 |pmid=19142852 |doi=10.1002/jcp.21685}}</ref> and [[Caveolin 1|calveolin 1]],<ref>{{cite journal |vauthors=Moh MC, Lee LH, Zhang T, Shen S |title=Interaction of the immunoglobulin-like cell adhesion molecule hepaCAM with caveolin-1 |journal=Biochemical and Biophysical Research Communications |volume=378 |issue=4 |pages=755–60 | date=January  2009 |pmid=19059381 |doi=10.1016/j.bbrc.2008.11.119}}</ref> and is capable of inducing senescence-like growth arrest via a p53/p21-dependent pathway.<ref name=pmid18845560/> Moreover, hepaCAM is proteolystically cleaved near the transmemberane region.<ref>{{cite journal |vauthors=Zhang T, Moh MC, Lee LH, Shen S |title=The immunoglobulin-like cell adhesion molecule hepaCAM is cleaved in the human breast carcinoma MCF7 cells |journal=International Journal of Oncology |volume=37 |issue=1 |pages=155–65 | date=July  2010 |pmid=20514407 |url=http://www.spandidos-publications.com/ijo/37/1/155 |doi=10.3892/ijo_00000663}}</ref> These findings indicate that the new Ig-like cell adhesion molecule hepaCAM is also a [[tumor suppressor gene|tumour suppressor]].<ref>{{cite journal |vauthors=Moh MC, Shen S |title=The roles of cell adhesion molecules in tumor suppression and cell migration: a new paradox |journal=Cell Adhesion & Migration |volume=3 |issue=4 |pages=334–6 |year=2009 |pmid=19949308 |pmc=2802741 |url=http://www.landesbioscience.com/journals/cam/abstract.php?id=9246 |doi=10.4161/cam.3.4.9246}}</ref>
 
==Other names==
#glialCAM, which was cloned from a human brain cDNA library in 2008 and found to be identical to hepaCAM;<ref name=pmid18293412>{{cite journal  |vauthors=Favre-Kontula L, Rolland A, Bernasconi L, etal |title=GlialCAM, an immunoglobulin-like cell adhesion molecule is expressed in glial cells of the central nervous system |journal=Glia |volume=56 |issue=6 |pages=633–45 | date=April  2008 |pmid=18293412 |doi=10.1002/glia.20640}}</ref> and
#HEPACAM1, when HEPACAM2 emerged in 2010.<ref name=pmid20226097>{{cite journal |vauthors=Klopfleisch R, Klose P, da Costa A, Brunnberg L, Gruber AD |title=HEPACAM1 and 2 are differentially regulated in canine mammary adenomas and carcinomas and its lymph node metastases |journal=BMC Veterinary Research |volume=6 |issue= |pages=15 |year=2010 |pmid=20226097 |pmc=2842258 |doi=10.1186/1746-6148-6-15}}</ref>


Functionally, HEPACAM is involved in cell-extracellular matrix interactions and growth control of cancer cells,<ref name="pmid15917256" /> and is able to induce differentiation of [[glioblastoma]] cells.<ref>{{cite journal |vauthors=Lee LH, Moh MC, Zhang T, Shen S |title=The immunoglobulin-like cell adhesion molecule hepaCAM induces differentiation of human glioblastoma U373-MG cells |journal=Journal of Cellular Biochemistry |volume=107 |issue=6 |pages=1129–38 | date=August  2009 |pmid=19507233 |doi=10.1002/jcb.22215}}</ref> In cell signaling, HEPACAM directly interacts with [[F-actin]]<ref name="pmid19142852">{{cite journal |vauthors=Moh MC, Tian Q, Zhang T, Lee LH, Shen S |title=The immunoglobulin-like cell adhesion molecule hepaCAM modulates cell adhesion and motility through direct interaction with the actin cytoskeleton |journal=Journal of Cellular Physiology |volume=219 |issue=2 |pages=382–91 | date=May  2009 |pmid=19142852 |doi=10.1002/jcp.21685}}</ref> and [[Caveolin 1|calveolin 1]],<ref>{{cite journal |vauthors=Moh MC, Lee LH, Zhang T, Shen S |title=Interaction of the immunoglobulin-like cell adhesion molecule hepaCAM with caveolin-1 |journal=Biochemical and Biophysical Research Communications |volume=378 |issue=4 |pages=755–60 | date=January  2009 |pmid=19059381 |doi=10.1016/j.bbrc.2008.11.119}}</ref> and is capable of inducing senescence-like growth arrest via a p53/p21-dependent pathway.<ref name="pmid18845560" /> Moreover, HEPACAM is proteolystically cleaved near the transmemberane region.<ref>{{cite journal |vauthors=Zhang T, Moh MC, Lee LH, Shen S |title=The immunoglobulin-like cell adhesion molecule hepaCAM is cleaved in the human breast carcinoma MCF7 cells |journal=International Journal of Oncology |volume=37 |issue=1 |pages=155–65 | date=July  2010 |pmid=20514407 |url=http://www.spandidos-publications.com/ijo/37/1/155 |doi=10.3892/ijo_00000663}}</ref> These findings indicate that the new Ig-like cell adhesion molecule HEPACAM is also a [[tumor suppressor gene|tumour suppressor]].<ref>{{cite journal |vauthors=Moh MC, Shen S |title=The roles of cell adhesion molecules in tumor suppression and cell migration: a new paradox |journal=Cell Adhesion & Migration |volume=3 |issue=4 |pages=334–6 |year=2009 |pmid=19949308 |pmc=2802741 |url=http://www.landesbioscience.com/journals/cam/abstract.php?id=9246 |doi=10.4161/cam.3.4.9246}}</ref> HEPACAM1 is involved in negative [[cell cycle]] regulation via p53, p21 and p27 signalling<ref name=pmid18845560/> but also mediates increased human [[breast cancer]] cell spread.<ref name=pmid15917256/><ref name=pmid19142852/>
==About HEPACAM 2==
[[Metastatic]] [[domestic dog|canine]] [[mammary carcinoma]] and their metastases are characterized by decreased HEPACAM2 but unchanged HEPACAM2 expression levels when compared to normal glands.<ref name=pmid20226097/>


==References==
==References==

Latest revision as of 14:05, 12 October 2018

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Identifiers
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External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
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RefSeq (mRNA)

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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.[1] 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.[1]

(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.[2] Based on the sequence of HEPN1, the new gene HEPACAM was then isolated and characterised.[3]

Characteristics and functions

Structurally, hepaCAM is a glycoprotein containing an extracellular domain with 2 Ig-like loops, a transmembrane region and a cytoplasmic domain.[3] 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.[4] Functionally, hepaCAM is involved in cell-extracellular matrix interactions and growth control of cancer cells,[3] and is able to induce differentiation of glioblastoma cells.[5] 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] Moreover, hepaCAM is proteolystically cleaved near the transmemberane region.[8] These findings indicate that the new Ig-like cell adhesion molecule hepaCAM is also a tumour suppressor.[9]

Other names

  1. glialCAM, which was cloned from a human brain cDNA library in 2008 and found to be identical to hepaCAM;[10] and
  2. HEPACAM1, when HEPACAM2 emerged in 2010.[11]

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.[11]

References

  1. ↑ 1.0 1.1 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.
  2. ↑ 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.
  3. ↑ 3.0 3.1 3.2 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.
  4. ↑ 4.0 4.1 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.
  5. ↑ 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.
  6. ↑ 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.
  7. ↑ 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.
  8. ↑ 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.
  9. ↑ 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.
  10. ↑ 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.
  11. ↑ 11.0 11.1 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.
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