The current status of anti-GPCR drugs against different cancers

Sana Usman; Maria Khawer; Shazia Rafique; Zara Naz; Komal Saleem

doi:10.1016/j.jpha.2020.01.001

Volume 10 Issue 6

Dec. 2020

Turn off MathJax

Article Contents

Article Navigation > Journal of Pharmaceutical Analysis > 2020 > 10(6): 517-521

Sana Usman, Maria Khawer, Shazia Rafique, Zara Naz, Komal Saleem. The current status of anti-GPCR drugs against different cancers[J]. Journal of Pharmaceutical Analysis, 2020, 10(6): 517-521. doi: 10.1016/j.jpha.2020.01.001

Citation:

Sana Usman, Maria Khawer, Shazia Rafique, Zara Naz, Komal Saleem. The current status of anti-GPCR drugs against different cancers[J]. Journal of Pharmaceutical Analysis, 2020, 10(6): 517-521. doi: 10.1016/j.jpha.2020.01.001

Citation:

PDF( 298 KB)

The current status of anti-GPCR drugs against different cancers

doi: 10.1016/j.jpha.2020.01.001

a. Centre for Applied Molecular Biology, 87-West Canal Bank Road Thokar Niaz Baig, University of the Punjab, Lahore, Pakistan;
b. Centre of Excellence in Molecular Biology, University of the Punjab, Lahore, Pakistan

Received Date: Apr. 19, 2019
Accepted Date: Jan. 10, 2020
Rev Recd Date: Jan. 06, 2020
Available Online: Jan. 24, 2022
Publish Date: Dec. 10, 2020

Abstract

Abstract

G protein coupled receptors (GPCRs) have emerged as the most potential target for a number of drug discovery programs ranging from control of blood pressure, diabetes, cure for genetic diseases to treatment of cancer. A panel of different ligands including hormones, peptides, ions and small molecules is responsible for activation of these receptors. Molecular genetics has identified key GPCRs, whose mutations or altered expressions are linked with tumorgenicity. In this review, we discussed recent advances regarding the involvement of GPCRs in the development of cancers and approaches to manipulating the mechanism behind GPCRs involved tumor growth and metastasis to treat different types of human cancer. This review provides an insight into the current scenario of GPCR-targeted therapy, progress to date and the challenges in the development of anticancer drugs.
- GPCRs,
- Anticancer therapy,
- Pancreatic cancer,
- Colon cancer,
- CLL,
- Prostate cancer,
- Melanoma

FullText(HTML)

References(58)

References

K. Lundstrom, Structural genomics of GPCRs, Trends Biotechnol. 23 (2005) 103-108

M. Rask-Andersen, M. S. Almen, H. B. Schioth, Trends in the exploitation of novel drug targets, Nat. Rev. Drug Discov. 10 (2011) 579-590

D. Young, G. Waitches, C. Birchmeier, et al, Isolation and characterization of a new cellular oncogene encoding a protein with multiple potential transmembrane domains, Cell 45 (1986) 711-719

K. Noguchi, D. Herr, T. Mutoh, et al, Lysophosphatidic acid (LPA) and its receptors, Curr. Opin. Pharmacol. 9 (2009) 15-23

B. E. Krumm, R. Grisshammer, Peptide ligand recognition by G protein-coupled receptors, Front Pharmacol. 6 (2015) 48

F. Balkwill, Cancer and the chemokine network, Nat. Rev. Cancer 4 (2004) 540-550

Y. Matsuo, M. Raimondo, T. A. Woodward, et al, CXC-chemokine/CXCR2 biological axis promotes angiogenesis in vitro and in vivo in pancreatic cancer, Int. J. Cancer 125 (2009) 1027-1037

J. Xu, C. Zhang, Y. He, et al, Lymphatic endothelial cell-secreted CXCL1 stimulates lymphangiogenesis and metastasis of gastric cancer, Int. J. Cancer 130 (2012) 787-797

J. Tang, Z. Li, L. Lu, et al, beta-Adrenergic system, a backstage manipulator regulating tumour progression and drug target in cancer therapy, Semin. Cancer Biol. 23 (2013) 533-542

F. Labrie, A. Belanger, V. Luu-The, et al, Gonadotropin-releasing hormone agonists in the treatment of prostate cancer, Endocr. Rev. 26 (2005) 361-379

T. Meyer, M. E. Caplin, D. H. Palmer, et al, A phase Ib/IIa trial to evaluate the CCK2 receptor antagonist Z-360 in combination with gemcitabine in patients with advanced pancreatic cancer, Eur. J. Cancer 46 (2010) 526-533

U S Food and Drug Administration, https://www.accessdata.fda.gov/scripts/cder/daf/index.cfm, (accessed Aug 10, 2018)

Y. Xiang, X. Yao, K. Chen, et al, The G-protein coupled chemoattractant receptor FPR2 promotes malignant phenotype of human colon cancer cells, Am. J. Cancer Res. 6 (2016) 2599-2610

L. D. Su, J. M. Peng, Y. B. Ge, Formyl peptide receptor 2 mediated chemotherapeutics drug resistance in colon cancer cells, Eur. Rev. Med. Pharmacol. Sci. 22 (2018) 95-100

H. M. Schuller, Regulatory role of G protein-coupled receptors in pancreatic cancer development and progression, Curr. Med. Chem. (2017)

L. Chow, L. Rezmann, K. Imamura, et al, Functional angiotensin II type 2 receptors inhibit growth factor signaling in LNCaP and PC3 prostate cancer cell lines, Prostate 68 (2008) 651-660

C. Zhou, X. Dai, Y. Chen, et al, G protein-coupled receptor GPR160 is associated with apoptosis and cell cycle arrest of prostate cancer cells, Oncotarget 7 (2016) 12823-12839

D. Maussang, A. Mujic-Delic, F. J. Descamps, et al, Llama-derived single variable domains (nanobodies) directed against chemokine receptor CXCR7 reduce head and neck cancer cell growth in vivo, J. Biol. Chem. 288 (2013) 29562-29572

M. Yang, W. W. Zhong, N. Srivastava, et al, G protein-coupled lysophosphatidic acid receptors stimulate proliferation of colon cancer cells through the {beta}-catenin pathway, Proc. Natl. Acad. Sci. U S A 102 (2005) 6027-6032

R. L. Siegel, K. D. Miller, A. Jemal, Cancer statistics, 2016, CA Cancer J. Clin. 66 (2016) 7-30

J. Wang, J. Weng, Y. Cai, et al, The prostate-specific G-protein coupled receptors PSGR and PSGR2 are prostate cancer biomarkers that are complementary to alpha-methylacyl-CoA racemase, Prostate 66 (2006) 847-857

E. M. Neuhaus, W. Zhang, L. Gelis, et al, Activation of an olfactory receptor inhibits proliferation of prostate cancer cells, J. Biol. Chem. 284 (2009) 16218-16225

M. Liu, Y. Y. Zhao, F. Yang, et al, Evidence for a role of GPRC6A in prostate cancer metastasis based on case-control and in vitro analyses, Eur. Rev. Med. Pharmacol. Sci. 20 (2016) 2235-2248

R. Ye, M. Pi, J. V. Cox, et al, CRISPR/Cas9 targeting of GPRC6A suppresses prostate cancer tumorigenesis in a human xenograft model, J. Exp. Clin. Cancer Res. 36 (2017) 90

S. Fung, T. Forte, R. Rahal, et al, Provincial rates and time trends in pancreatic cancer outcomes, Curr. Oncol. 20 (2013) 279-281

K. Kisfalvi, G. Eibl, J. Sinnett-Smith, et al, Metformin disrupts crosstalk between G protein-coupled receptor and insulin receptor signaling systems and inhibits pancreatic cancer growth, Cancer Res. 69 (2009) 6539-6545

J. P. Smith, L. K. Fonkoua, T. W. Moody, The Role of Gastrin and CCK Receptors in Pancreatic Cancer and other Malignancies, Int. J. Biol. Sci. 12 (2016) 283-291

Global, regional, and national incidence, prevalence, and years lived with disability for 310 diseases and injuries, 1990-2015: a systematic analysis for the Global Burden of Disease Study 2015, Lancet 388 (2016) 1545-1602

H. Sic, H. Kraus, J. Madl, et al, Sphingosine-1-phosphate receptors control B-cell migration through signaling components associated with primary immunodeficiencies, chronic lymphocytic leukemia, and multiple sclerosis, J. Allergy Clin. Immunol. 134 (2014) 420-428

G. Runarsson, A. Liu, Y. Mahshid, et al, Leukotriene B4 plays a pivotal role in CD40-dependent activation of chronic B lymphocytic leukemia cells, Blood 105 (2005) 1274-1279

S. Saada, P. Marget, A. L. Fauchais, et al, Differential expression of neurotensin and specific receptors, NTSR1 and NTSR2, in normal and malignant human B lymphocytes, J. Immunol. 189 (2012) 5293-5303

T. Kamp, B. Liebl, E. Haen, et al, Defects of beta 2-adrenergic signal transduction in chronic lymphocytic leukaemia: relationship to disease progression, Eur. J. Clin. Invest. 27 (1997) 121-127

M. Mamani-Matsuda, D. Moynet, M. Molimard, et al, Long-acting beta2-adrenergic formoterol and salmeterol induce the apoptosis of B-chronic lymphocytic leukaemia cells, Br. J. Haematol. 124 (2004) 141-150

S. Decker, J. Finter, A. J. Forde, et al, PIM kinases are essential for chronic lymphocytic leukemia cell survival (PIM2/3) and CXCR4-mediated microenvironmental interactions (PIM1), Mol. Cancer Ther. 13 (2014) 1231-1245

B. Stamatopoulos, N. Meuleman, C. De Bruyn, et al, The histone deacetylase inhibitor suberoylanilide hydroxamic acid (SAHA) induces apoptosis, downregulates the CXCR4 chemokine receptor and impairs migration of chronic lymphocytic leukemia cells, Haematol. Hematol. J. 95 (2010) 1136-1143

M. Buchner, P. Brantner, N. Stickel, et al, The microenvironment differentially impairs passive and active immunotherapy in chronic lymphocytic leukaemia - CXCR4 antagonists as potential adjuvants for monoclonal antibodies, Br. J. Haematol. 151 (2010) 167-178

M. Burger, T. Hartmann, M. Krome, et al, Small peptide inhibitors of the CXCR4 chemokine receptor (CD184) antagonize the activation, migration, and antiapoptotic responses of CXCL12 in chronic lymphocytic leukemia B cells, Blood 106 (2005) 1824-1830

M. Niedermeier, B. T. Hennessy, Z. A. Knight, et al, Isoform-selective phosphoinositide 3′-kinase inhibitors inhibit CXCR4 signaling and overcome stromal cell-mediated drug resistance in chronic lymphocytic leukemia: a novel therapeutic approach, Blood 113 (2009) 5549-5557

L. Patrussi, N. Capitani, V. Martini, et al, Enhanced Chemokine Receptor Recycling and Impaired S1P1 Expression Promote Leukemic Cell Infiltration of Lymph Nodes in Chronic Lymphocytic Leukemia, Cancer Res. 75 (2015) 4153-4163

O. Yoshie, R. Fujisawa, T. Nakayama, et al, Frequent expression of CCR4 in adult T-cell leukemia and human T-cell leukemia virus type 1-transformed T cells, Blood 99 (2002) 1505-1511

S. Makita, K. Tobinai, Mogamulizumab for the treatment of T-cell lymphoma, Expert. Opin. Biol. Ther. 17 (2017) 1145-1153

P. Boyle, B. Levin. World cancer report 2008. IARC Press, International Agency for Research on Cancer; 2008

A. McGuire, J. A. Brown, C. Malone, et al, Effects of age on the detection and management of breast cancer, Cancers 7 (2015) 908-929

G. P. Tuszynski, V. L. Rothman, X. Zheng, et al, G-protein coupled receptor-associated sorting protein 1 (GASP-1), a potential biomarker in breast cancer, Exp. Mol. Pathol. 91 (2011) 608-613

S. Hardy, G. G. St-Onge, E. Joly, et al, Oleate promotes the proliferation of breast cancer cells via the G protein-coupled receptor GPR40, J. Biol. Chem. 280 (2005) 13285-13291

J. Q. Chen, J. Russo, ERalpha-negative and triple negative breast cancer: molecular features and potential therapeutic approaches, Biochim. Biophys. Acta. 1796 (2009) 162-175

M. E. Feigin, B. Xue, M. C. Hammell, et al, G-protein-coupled receptor GPR161 is overexpressed in breast cancer and is a promoter of cell proliferation and invasion, PNAS 111 (2014) 4191-4196

Home-ClinicalTrials.gov, https://clinicaltrials.gov/ct2/home. Accessed on 8 August 2018

World Cancer Report 2014, Geneva, Switzerland: World Health Organization, International Agency for Research on Cancer, WHO Press, 2015

Y. Qin, E. M. Verdegaal, M. Siderius, et al, Quantitative expression profiling of G-protein-coupled receptors (GPCRs) in metastatic melanoma: the constitutively active orphan GPCR GPR18 as novel drug target, Pigment Cell Melanoma Res. 24 (2011) 207-218

L. Xu, S. Begum, M. Barry, et al, GPR56 plays varying roles in endogenous cancer progression, Clin. Exp. Metastasis 27 (2010) 241-249

L. Yang, G. Chen, S. Mohanty, et al, GPR56 Regulates VEGF production and angiogenesis during melanoma progression, Cancer Res. 71 (2011) 5558-5568

Z. Jin, R. Luo, X. Piao, GPR56 and its related diseases, Prog. Mol. Biol. Transl. Sci. 89 (2009) 1-13

E. Perez-Gomez, C. Andradas, J. M. Flores, et al, The orphan receptor GPR55 drives skin carcinogenesis and is upregulated in human squamous cell carcinomas, Oncogene 32 (2013) 2534

M. T. Bastiaens, J. A. ter Huurne, C. Kielich, et al, Melanocortin-1 receptor gene variants determine the risk of nonmelanoma skin cancer independently of fair skin and red hair, Am. J. Hum. Genet. 68 (2001) 884-894

D. L. Duffy, N. F. Box, W. Chen, et al, Interactive effects of MC1R and OCA2 on melanoma risk phenotypes, Hum. Mol. Genet. 13 (2004) 447-461

K. Loser, T. Brzoska, V. Oji, et al, The neuropeptide alpha-melanocyte-stimulating hormone is critically involved in the development of cytotoxic CD8+ T cells in mice and humans, PLOS ONE 5 (2010) e8958

T. H. Nasti, L. Timares, MC1R, eumelanin and pheomelanin: their role in determining the susceptibility to skin cancer, Photochem. Photobiol. 91 (2015) 188-200

Relative Articles

Supplements(0)

Cited By

Proportional views