Recombinant Human Hepatocyte cell adhesion molecule (HEPACAM), partial

1. On the whole, this study indicates that HepaCAM potentially represents a therapeutic target and PF3084014 may prove to a promising agent for use in the treatment of refractory prostate cancer. PMID: 29658567
2. hepaCAM associates with connexin 43, a main component of gap junctions, and enhances connexin 43 localization to the plasma membrane at cellular junctions. PMID: 27819278
3. this study revealed that hepaCAM was downregulated in CRC tissues and cell lines. Overexpression of hepaCAM inhibited CRC cell proliferation, migration, and invasion in vitro. Furthermore, the tumorigenesis assay showed that increased expression of hepaCAM suppressed CRC tumor growth and metastasis in vivo. PMID: 28244854
4. In a group of Egyptian patients with megalencephalic leukoencephalopathy, novel mutations were identified in HEPACAM. PMID: 27389245
5. DNMT1 up-regulation induced by IL-6/STAT3 signaling was indispensable for IL-6-mediated hepaCAM loss in renal cell carcinoma (RCC) cell lines ACHN and 769-P, while DNMT3b up-regulation was crucial for hepaCAM loss in A498. PMID: 28093267
6. Out of 20 patients, macrocephaly, classic MRI features, motor development delay and cognitive impairment were detected in 20(100%), 20(100%), 17(85%) and 4(20%) patients, respectively. 20(100%) were clinically diagnosed with MLC. 19(95%) were genetically diagnosed with 10 novel mutations in MLC1, MLC1 and GlialCAM mutations were identified in 15 and 4 patients, respectively PMID: 27322623
7. HepaCAM depletion was discovered in bladder cancer tissues compared with adjacent normal tissues, and the decreased level was associated with the degradation of FoxO3. PMID: 28229220
8. HepaCAM proteins were significantly decreased in bladder carcinoma. Low hepaCAM was not statistically associated with clinicopathological characteristics of the patients. HepaCAM overexpression activated caspase 3/8/9, downregulated poly-ADP ribose polymerase and p-SMAD2/3, and decreased apoptosis. PMID: 26873485
9. The suppressive roles of HEPACAM in NSCLC. PMID: 26392113
10. Due to the ability to reactivate expression of hepaCAM and inhibit growth of bladder cancer cells, AZAC may represent an effective treatment for bladder cancer. PMID: 26677113
11. The extracellular domain of GlialCAM is necessary for cell junction targeting and for mediating interactions with itself or with MLC1 and ClC-2. PMID: 26033718
12. HepaCAM may prevent the translocation of PKCepsilon from cytosolic to particulate fractions, resulting in the inhibition of 786-0 cell proliferation. PMID: 24515280
13. GlialCAM is able to interact with all CLC channels tested in this study, targeting them to cell junctions and activating them by stabilizing the open configuration of the common gate PMID: 25185546
14. Results allow classifying the effect of HEPACAM gene mutations in different subtypes and authors indicate different cellular mechanisms that lead to megalencephalic leukoencephalopathy pathogenesis. PMID: 25044933
15. we demonstrate an evolutionary conserved role for MLC1 in regulating glial surface levels of GLIALCAM, and this interrelationship explains why patients with mutations in either gene (MLC1 or GLIALCAM) share the same clinical phenotype. PMID: 24824219
16. High expression of hepaCAM is associated with renal carcinoma. PMID: 24645843
17. analysis of mutations in GLIALCAM in patients with megalencephalic leukoencephalopathy with subcortical cysts [case report] PMID: 24202401
18. results suggested that HepaCAM acted as a tumor suppressor in prostate cancer PMID: 24811146
19. Re-activation of hepaCAM gene by 5-aza-CdR can inhibit growth of cancer cells and arrest cells at G0/G1 phase PMID: 24324362
20. results indicate GlialCAM is necessary for MLC1 protein expression, and its reduction affects the activity of volume-regulated anion currents (VRAC) which may cause astrocyte vacuolation; work extends the role of GlialCAM as a chaperone of MLC1 needed for proper VRAC activation PMID: 23793458
21. No clear association between GLIALCAM mutations and an autism-epilepsy phenotype. PMID: 24580998
22. Results suggest an important connection between HEPACAM and interferon-gamma, which may inhibit BIU-87 proliferation through HEPACAM re-expression and p21(WAF1) up-regulation to arrest cells at the G(0)/G(1) phase PMID: 22906662
23. Research implies that the decrease in c-Myc protein expression, resulting from ectopic expression of hepaCAM, may contribute to the inhibition of proliferation in these cells. PMID: 21618595
24. study presents more detailed characterization of the effect of mutations found in MLC1 and GLIALCAM megalencephalic leukoencephalopathy with subcortical cysts PMID: 21624973
25. Dominant HEPACAM mutations can cause either macrocephaly and mental retardation with or without autism or benign familial macrocephaly. PMID: 21419380
26. Downregulation of hepaCAM expression plays an important role in the tumorigenesis and development of bladder cancer PMID: 20628239
27. There is a close relationship between hepaCAM and VEGF in urothelial carcinoma PMID: 20593288
28. The truncation mutant of hepaCAM failed to promote cell-ECM adhesion and migration, and lost the inhibitory effects on cell growth, suggesting a regulatory role of the cleavage in hepaCAM functions. PMID: 20514407
29. HepaCAM is involved in cell adhesion and growth control, and its expression is frequently silenced in TCCB. The extracellular domain of hepaCAM is essential to its physiological and biological functions. PMID: 20205955
30. Observational study of gene-disease association. (HuGE Navigator) PMID: 20237496
31. HEPN1 is frequently silenced in HCC, and exogenous HEPN1 exhibits antiproliferative effect on HepG2 cells, suggesting that silencing of HEPN1 may be associated with carcinogenesis of hepatocytes. PMID: 12971969
32. encodes an Ig-like transmembrane glycoprotein and is involved in cell adhesion and growth control PMID: 15885354
33. the cytoplasmic domain of hepaCAM is essential to its function on cell-matrix interaction and cell motility PMID: 15917256
34. study examined the glycosylation of the GlialCAM (hepaCAM) extracellular domain expressed in HEK and CHO cells PMID: 18082421
35. GlialCAM, an immunoglobulin-like cell adhesion molecule is expressed in glial cells of the central nervous system. PMID: 18293412
36. the expression of hepaCAM in MCF7 cells not only inhibits cell growth but also induces cellular senescence through the p53/21 pathway PMID: 18845560
37. hepaCAM is partially localized in the lipid rafts/caveolae and interacts with Cav-1 through its first immunoglobulin domain. PMID: 19059381
38. The data suggest that an intact hepaCAM protein is critical for establishing a stable physical association with the actin cytoskeleton; and such association is important for modulating hepaCAM-mediated cell adhesion and motility. PMID: 19142852
39. high expression of hepaCAM significantly accelerated cell adhesion but inhibited cell proliferation and migration; cell differentiation was noticeably less apparent in cells expressing low-level hepaCAM PMID: 19507233

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HGNC: 26361

OMIM: 611642

KEGG: hsa:220296

STRING: 9606.ENSP00000298251

UniGene: Hs.745294