Volume 4 Issue 1
Jun.  2020
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Hua Wei, Ying Cui, Yang Chen, Shijie Mu. The progress of abnormal expression of Lutheran blood group glycoprotein in cancers[J]. Blood&Genomics, 2020, 4(1): 39-44. doi: 10.46701/BG2020012020105
Citation: Hua Wei, Ying Cui, Yang Chen, Shijie Mu. The progress of abnormal expression of Lutheran blood group glycoprotein in cancers[J]. Blood&Genomics, 2020, 4(1): 39-44. doi: 10.46701/BG2020012020105

The progress of abnormal expression of Lutheran blood group glycoprotein in cancers

doi: 10.46701/BG2020012020105
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  • Corresponding author: Shijie Mu, Department of Blood Transfusion, Tangdu Hospital, the Second Affiliated Hospital of Air Force Military Medical University, 569 Xinsi Road, Baqiao District, Xi'an, Shaanxi 710032, China. Email: musj1963@fmmu.edu.cn. The authors declared no conflict of interests
  • Received Date: 2020-03-20
  • Accepted Date: 2020-06-04
  • Rev Recd Date: 2020-05-11
  • Available Online: 2021-07-01
  • Publish Date: 2020-06-30
  • Lutheran blood group glycoprotein (Lu-gp) is a specific α5 laminin receptor that is linked by binding to its receptor in the basement membrane matrix. Although the biological function of Lu-gp is unknown, its special affinity with laminin in the chain suggests that it plays an important role in human development and physiological processes. As the interaction between Lu-gp and laminin is further investigated, their expression may be found to play an important role in tumor invasion and metastasis. Laminin receptors help cells adhere, receive and conduct extracellular information into cells, mainly through MAPK pathways, including ERKs, p38MAPK, etc., affecting the degradation of the extracellular matrix and enhancing tumor cell infiltration and metastasis. Present researches in cancers mainly focus on aspects relating to laminin, but largely do not pay attention to the Lutheran blood group antigen, basal cell adhesion molecule. This paper focuses on the abnormal expression of the laminin receptor, that is, the Lutheran blood group antigen, in cancers, which is of great significance to the mechanism of cancer invasion and metastasis, and for finding effective treatment methods for cancers.


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  • [1]
    Zeng H, Chen W, Zheng R, et al. Changing cancer survival in China during 2003-15: a pooled analysis of 17 population-based cancer registries[J]. Lancet Glob Health, 2018, 6(5): 555-67. doi: 10.1016/S2214-109X(18)30127-X
    Chen W, Sun K, Zheng R, et al. Cancer incidence and mortality in China, 2014[J]. Chin J Cancer Res, 2018, 30(1): 1-12. doi: 10.21147/j.issn.1000-9604.2018.01.01
    Zhou B, Zong S, Zhong W, et al. Interaction between laminin-5γ2 and integrin β1 promotes the tumor budding of colorectal cancer via the activation of Yes-associated proteins[J]. Oncogene, 2019, 39(5): 1527-42. http://www.nature.com/articles/s41388-019-1082-1
    Chen W, Zheng R, Baade PD, et al. Cancer statistics in China, 2015[J]. CA Cancer J Clin, 2016, 66(2): 115-32. doi: 10.3322/caac.21338
    Torre LA, Siegel RL, Jemal A. Lung cancer statistics[J]. Adv Exp Med Biol, 2015, 893(12): 1-19.
    Islami F, Chen W, Yu XQ, et al. Cancer deaths and cases attributable to lifestyle factors and infections in China, 2013[J]. Ann Oncol, 2017, 28(10): 2567-74. doi: 10.1093/annonc/mdx342
    Willberg J, Hormia M, Takkunen M, et al. Lutheran blood group antigen as a receptor for α5 laminins in gingival epithelia[J]. J Periodontol, 2007, 78(9): 1810-8. doi: 10.1902/jop.2007.060482
    Manders DB, Kishore HA, Gazdar AF, et al. Dysregulation of fibulin-5 and matrix metalloproteases in epithelial ovarian cancer[J]. Oncotarget, 2018, 9(18): 14251-67. doi: 10.18632/oncotarget.24484
    Langer IBV, Visentainer JEL, Zacarias JMV, et al. Genotyping of Dombrock and Lutheran blood group systems in blood donors from the southwestern region of the state of Paraná, Southern Brazil[J]. Hematol Transfus Cell Ther, 2019, 41(1): 25-30. doi: 10.1016/j.htct.2018.06.001
    Kikkawa Y, Miner JH. Review: Lutheran/b-CAM: A lamin receptor on red blood cells and in various tissues[J]. Connect Tissue Res, 2005, 46(6): 193-9. http://europepmc.org/abstract/MED/16546822
    Gordon-Weeks A, Lim SY, Yuzhalin A, et al. Tumour-derived laminin α5 (LAMA5) promotes colorectal liver metastasis growth, branching angiogenesis and notch pathway inhibition[J]. Cancers, 2019, 11(5): 630. doi: 10.3390/cancers11050630
    Crew VK, Poole J, Banks J, et al. LU21: a new high-frequency antigen in the Lutheran blood group system[J]. Vox Sanguin, 2004, 87(9): 109-13. doi: 10.1111/j.1423-0410.2004.00542.x/full
    Lin Y, Ge X, Zhang X, et al. Protocadherin-8 promotes invasion and metastasis via laminin subunit γ2 in gastric cancer[J]. Cancer Sci, 2018, 109(3): 732-40. doi: 10.1111/cas.13502
    Daniels G. An update on the Lutheran blood group system[J]. Immunohematology, 2019, 35(1): 23-4. http://www.ncbi.nlm.nih.gov/pubmed/30908076
    Wang SG, Han BL, Chen YS, et al. Significance of laminin in tumor cell invasion in cholangiocarcinoma[J]. Acta Acdemiae Militaris Tertiae (in Chinese), 1995, 17(5): 389-92. http://en.cnki.com.cn/Article_en/ http://search.cnki.net/down/default.aspx?filename=DSDX505.005&dbcode=CJFD&year=1995&dflag=pdfdown
    Brocks DG, Strecker H, Neubauer HP, et al. Radioimmunoassay of laminin in serum and its application to cancer patients[J]. Clin Chem, 1986, 32(5): 787-91. doi: 10.1093/clinchem/32.5.787
    Parsons SF, Mallinson G, Holmes CH, et al. The Lutheran blood group glycoprotein, another member of the immunoglobulin superfamily is widely expressed in human tissues and is developmentally regulated in human liver[J]. Proc Natl Acad Sci USA, 2016, 92(12): 5496-500.
    Latini FR, Bastos AU, Arnoni CP, et al. DARC and BCAM (Lutheran) reduced expression in thyroid cancer[J]. Blood Cells Mol Dis, 2013, 50(2): 161-5. http://www.ncbi.nlm.nih.gov/pubmed/23168236
    Kikkawa Y, Ogawa T, Sudo R, et al. The lutheran/basal cell adhesion molecule promotes tumor cell migration by modulating integrin-mediated cell attachment to laminin-511 protein[J]. J Biol Chem, 2013, 288(43): 30990-1001. doi: 10.1074/jbc.M113.486456
    Murphy MM, Zayed MA, Evans A, et al. Role of Rap 1 in promoting sickle red blood cell adhesion to laminin via BCAM / LU[J]. Blood, 2005, 105(8): 3322-9. doi: 10.1182/blood-2004-07-2881
    Drewniok C, Wienrich BG, Schon M, et al. Molecular interactions of B-CAM (basal-cell adhesion molecule) and laminin in epithelial skin cancer[J]. Arch Dermatol Res, 2004, 296(2): 59-66. doi: 10.1007/s00403-004-0481-4
    Satoh K, Narumi K, Abe T, et al. Diminution of 37-kDa laminin binding protein expression reduces tumour formation of murine lung cancer cells[J]. Br J Cancer, 1999, 80(8): 1115-22. doi: 10.1038/sj.bjc.6690474
    Bernemann TM, Podda M, Wolter M, et al. Expression of the basal cell adhesion molecule (B-CAM) in normal and diseased human skin[J]. J Cutan Pathol, 2000, 27(3): 108-11. doi: 10.1034/j.1600-0560.2000.027003108.x
    Drewniok C, Wienrich BG, Schön M, et al. Molecular interactions of B-CAM (basal-cell adhesionmolecule) and laminin in epithelial skin cancer[J]. Dermatol Res, 2004, 296(2): 59-66. doi: 10.1007/s00403-004-0481-4
    Schön M, Klein CE, Hogenkamp V, et al. Basal-cell adhesion molecule (B-CAM) is induced in epithelial skin tumors and inflammatory epidermis, and is expressed at cell-cell and cell-substrate contact sites[J]. J Invest Dermatol, 2000, 115(6): 1047-53. doi: 10.1046/j.1523-1747.2000.00189.x
    Manders DB, Kishore HA, Gazdar AF, et al. Dysregulation of fibulin-5 and matrix metalloproteases in epithelial ovarian cancer[J]. Oncotarget, 2018, 9 (18): 14251-67. doi: 10.18632/oncotarget.24484
    Chang HY, Chang HM, Wu TJ, et al. The role of Lutheran/basal cell adhesion molecule in human bladder carcinogenesis[J]. J Biomed Sci, 2017, 24(1): 61. doi: 10.1186/s12929-017-0360-x
    Caires-Dos-Santos L, da Silva SV, Smuczek B, et al. Laminin derived peptide C16 regulates Tks expression and reactive oxygen species generation in human prostate cancer cells[J]. J Cell Physiol, 2020, 235(1): 587-98. doi: 10.1002/jcp.28997
    Yu KH, Barry CG, Austin D, et al., Stable isotope dilution multidimensional liquid chromatography–tandem mass spectrometry for pancreatic cancer serum biomarker discovery[J]. J Proteome Res, 2009 (8): 1565-76. http://new.med.wanfangdata.com.cn/Paper/Detail?id=PeriodicalPaper_JJ026974214
    Kikkawa Y, Miwa T, Tanimizu N, et al. Soluble Lutheran/basal cell adhesion molecule is detectable in plasma of hepatocellular carcinoma patients and modulates cellular interaction with laminin-511 in vitro[J]. Exp Cell Res, 2014, 328(2): 197-206. http://europepmc.org/abstract/MED/25051049
    Yellapurkar S, Natarajan S, Boaz K, et al. Expression of Laminin in oral squamous cell carcinomas[J]. Asian Pac J Cancer Prev, 2018, 19(2): 407-13.
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