Chemerin promotes the proliferation and migration of vascular smooth muscle and increases mouse blood pressure
Abstract
Blood chemerin concentration shows positive correlation not only with body mass index and serum triglyceride level but also with systolic blood pressure. While it seems likely that chemerin influences vascular smooth muscle cell (SMC) proliferation and migration, which are crucial to the development of hypertension, this remains to be clarified. In the present study, we investigated whether chemerin controls SMC proliferation and migration in vitro and also affects blood pressure in vivo. In vitro, chemerin significantly stimulated rat mesenteric arterial SMC proliferation and migration, as determined by a cell counting assay and Boyden chamber assay, respectively. The migratory effect of chemerin was confirmed in human aortic SMCs. Chemerin significantly increased ROS production in SMCs and phosphorylation of Akt (Ser 473) and ERK, as measured by fluorescent staining and Western blot analysis, respectively. Various inhibitors (ROS inhibitor: N-acetyl-l-cysteine, phosphatidylinositol 3-kinase inhibitor: LY-294002, MAPKK inhibitor: PD-98059, NADPH oxidase inhibitor: gp91 ds-tat, and xanthine oxidase inhibitor: allopurinol) as well as chemokine-like receptor 1 small interfering RNA significantly inhibited chemerin-induced SMC proliferation and migration. Furthermore, chemerin-neutralizing antibody prevented carotid neointimal hyperplasia in the mouse ligation model. In vivo, chronic chemerin treatment (6 μg/kg, 6 wk) increased systolic blood pressure as well as phosphorylation of Akt and ERK in the mouse isolated aorta. In summary, we, for the first time, demonstrate that chemerin/chemokine-like receptor 1 stimulates SMC proliferation and migration via ROS-dependent phosphorylation of Akt/ERK, which may lead to vascular structural remodeling and an increase in systolic blood pressure.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Chemerin shows vasoconstrictor activity in vitro and increases blood pressure in mice.
“Chemerin also shows vasoconstrictor activity in vitro and increases blood pressure in mice121.”
From Inflammation and its resolution in atherosclerosis: mediators and therapeutic opportunities (2019) · cites this paper as [121]
Cites
Mammalian Rho GTPases: new insights into their functions from in vivo studies
Heasman, S. J., & Ridley, A. J. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2476 · Cited by 1,871 · see citing works
Burridge, K., & Wennerberg, K. (2004) · Cell · doi:10.1016/s0092-8674(04)00003-0 · Cited by 1,790 · see citing works
Wittamer, V., Franssen, J.-D., Vulcano, M., Mirjolet, J.-F., Le Poul, E., Migeotte, I., Brézillon, S., Tyldesley, R., Blanpain, C., Detheux, M., et al. (2003) · The Journal of Experimental Medicine · doi:10.1084/jem.20030382 · Cited by 888 · see citing works
Chemerin Is a Novel Adipokine Associated with Obesity and Metabolic Syndrome
Bozaoglu, K., Bolton, K. A., McMillan, J. S., Zimmet, P., Jowett, J. B. M., Collier, G. R., Walder, K. R., & Segal, D. (2007) · Endocrinology · doi:10.1210/en.2007-0175 · Cited by 859 · see citing works
Chemerin, a Novel Adipokine That Regulates Adipogenesis and Adipocyte Metabolism
Goralski, K. B., McCarthy, T. C., Hanniman, E. A., Zabel, B. A., Butcher, E. C., Parlee, S. D., Muruganandan, S., & Sinal, C. J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700793200 · Cited by 851 · see citing works
Does superoxide underlie the pathogenesis of hypertension?
Nakazono, K., Watanabe, N., Matsuno, K., Sasaki, J., Sato, T., & Inoue, M. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.22.10045 · Cited by 746 · see citing works
The genetic design of signaling cascades to record receptor activation
Barnea, G., Strapps, W. R., Herrada, G., Berman, Y. L., Ong, J., Kloss, B., Axel, R., & Lee, K. J. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0710487105 · Cited by 673 · see citing works
S-Glutathiolation by peroxynitrite activates SERCA during arterial relaxation by nitric oxide
Adachi, T. K., Weisbrod, R. M., Pimentel, D. R., Ying, J., Sharov, V. S., Schöneich, C., & Cohen, R. A. (2004) · Nature Medicine · doi:10.1038/nm1119 · Cited by 662 · see citing works
Induction of Oxidative Stress by Glutathione Depletion Causes Severe Hypertension in Normal Rats
Vaziri, N. D., Wang, X. Q., Oveisi, F., & Rad, B. (2000) · Hypertension · doi:10.1161/01.hyp.36.1.142 · Cited by 400 · see citing works
Sell, H., Laurencikiene, J., Taube, A., Eckardt, K., Cramer, A., Horrighs, A., Arner, P., & Eckel, J. (2009) · Diabetes · doi:10.2337/db09-0277 · Cited by 389 · see citing works
Chemerin Activation by Serine Proteases of the Coagulation, Fibrinolytic, and Inflammatory Cascades
Zabel, B. A., Allen, S. J., Kulig, P., Allen, J. A., Cichy, J., Handel, T. M., & Butcher, E. C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504868200 · Cited by 369 · see citing works
Chemerin—A new adipokine that modulates adipogenesis via its own receptor
Roh, S., Song, S.-H., Choi, K.-C., Katoh, K., Wittamer, V., Parmentier, M., & Sasaki, S.-I. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.08.104 · Cited by 361 · see citing works
Kaur, J., Adya, R., Tan, B. K., Chen, J., & Randeva, H. S. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.12.150 · Cited by 349 · see citing works
Zabel, B. A., Nakae, S., Zuniga, L. A., Kim, J., Ohyama, T., Alt, C., Pan, J., Suto, H., Soler, D. F., Allen, S. J., et al. (2008) · The Journal of Experimental Medicine · doi:10.1084/jem.20080300 · Cited by 298 · see citing works
Role of the Pi3k Regulatory Subunit in the Control of Actin Organization and Cell Migration
Jiménez, C., Portela, R. A., Mellado, M., Rodrı́guez-Frade, J. M., Collard, J. G., Serrano, A., Martínez‐A, C., Ávila, J., & Carrera, A. C. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.151.2.249 · Cited by 255 · see citing works
Enomoto, T. (1996) · Cell Structure and Function · doi:10.1247/csf.21.317 · Cited by 218 · see citing works
Ho, K. J., Spite, M., Owens, C. D., Lancero, H., Kroemer, A. H. K., Pande, R., Creager, M. A., Serhan, C. N., & Conte, M. S. (2010) · The American Journal of Pathology · doi:10.2353/ajpath.2010.091082 · Cited by 204 · see citing works
Guo, F., Debidda, M., Yang, L. C., Williams, D. A., & Zheng, Y. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603508200 · Cited by 160 · see citing works
Chemerin Connects Fat to Arterial Contraction
Watts, S. W., Dorrance, A. M., Penfold, M. E. T., Rourke, J. L., Sinal, C. J., Seitz, B. M., Sullivan, T. J., Charvat, T. T., Thompson, J., Burnett, R. J., et al. (2013) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.113.301476 · Cited by 148 · see citing works
Chemoattractants, extracellular proteases, and the integrated host defense response
Zabel, B. A., Zuniga, L. A., Ohyama, T., Allen, S. J., Cichy, J., Handel, T. M., & Butcher, E. C. (2006) · Experimental Hematology · doi:10.1016/j.exphem.2006.05.003 · Cited by 142 · see citing works
Vascular Effects of Novel Adipocytokines: Focus on Vascular Contractility and Inflammatory Responses
Yamawaki, H. (2011) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.34.307 · Cited by 142 · see citing works
Self-citationExpression, Regulation, and Function of Atypical Chemerin Receptor CCRL2 on Endothelial Cells
Monnier, J., Lewén, S., O’Hara, E., Huang, K., Tu, H., Butcher, E. C., & Zabel, B. A. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1102871 · Cited by 139 · see citing works
Gpr1 is an active chemerin receptor influencing glucose homeostasis in obese mice
Rourke, J. L., Muruganandan, S., Dranse, H. J., McMullen, N. M., & Sinal, C. J. (2014) · Journal of Endocrinology · doi:10.1530/joe-14-0069 · Cited by 135 · see citing works
Drost, E., & MacNee, W. (2002) · European Journal of Immunology · doi:10.1002/1521-4141(200202)32:2 · Cited by 135 · see citing works
Molecular mechanisms of tazarotene action in psoriasis
Duvic, M. A., Nagpal, S., Asano, A. T., & Chandraratna, R. A. S. (1997) · Journal of the American Academy of Dermatology · doi:10.1016/s0190-9622(97)80396-9 · Cited by 134 · see citing works
Chemerin reveals its chimeric nature
Yoshimura, T., & Oppenheim, J. J. (2008) · The Journal of Experimental Medicine · doi:10.1084/jem.20081736 · Cited by 120 · see citing works
Carlino, C., Trotta, E., Stabile, H., Morrone, S., Bulla, R., Soriani, A., Iannitto, M. L., Agostinis, C., Mocci, C., Minozzi, M., et al. (2012) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2012-1102 · Cited by 90 · see citing works
Oxidative stress mediates chemerin-induced autophagy in endothelial cells
Shen, W., Tian, C., Chen, H., Yang, Y., Zhu, D., Gao, P., & Liu, J. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.11.011 · Cited by 83 · see citing works
Proteolytic regulatory mechanism of chemerin bioactivity
Du, X., & Leung, L. L. K. (2009) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmp091 · Cited by 83 · see citing works
Usui, T., Morita, T., Okada, M., & Yamawaki, H. (2013) · Hypertension · doi:10.1161/hypertensionaha.113.01843 · Cited by 81 · see citing works
Self-citationNeves, K. B., Lobato, N. S., Alves-Lopes, R., Filgueira, F. P., Zanotto, C. Z., de Oliveira, A. M., & Tostes, R. C. (2014) · Clinical Science · doi:10.1042/cs20130286 · Cited by 78 · see citing works
Patel, L., Charlton, S. J., Chambers, J. K., & Macphee, C. H. (2001) · Cytokine · doi:10.1006/cyto.2000.0851 · Cited by 77 · see citing works
Galligan, C. L., Matsuyama, W., Matsukawa, A., Mizuta, H., Hodge, D. R., Howard, O. M. Z., & Yoshimura, T. (2004) · Arthritis & Rheumatism · doi:10.1002/art.20275 · Cited by 71 · see citing works
Usui, T., Okada, M., Hara, Y., & Yamawaki, H. (2012) · Hypertension · doi:10.1161/hypertensionaha.112.200337 · Cited by 69 · see citing works
Self-citationLobato, N. S., Neves, K. B., Filgueira, F. P., Fortes, Z. B., de Carvalho, M. H. C., Webb, R. C., de Oliveira, A. M., & Tostes, R. C. (2012) · Life Sciences · doi:10.1016/j.lfs.2012.04.013 · Cited by 57 · see citing works
Yang, H., Li, F., Kong, X., Yuan, X., Wang, W., Huang, R., Li, T., Geng, M., Wu, G., & Yin, Y. (2012) · Cytokine · doi:10.1016/j.cyto.2012.07.033 · Cited by 56 · see citing works
Serum chemerin levels are associated with the presence and extent of coronary artery disease
Xiao-tao, L., Xiaoxia, Z., Yue, X., & Liye, W. (2012) · Coronary Artery Disease · doi:10.1097/mca.0b013e3283576a60 · Cited by 52 · see citing works
Kazama, K., Okada, M., & Yamawaki, H. (2014) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00048.2014 · Cited by 50 · see citing works
Self-citationBrouwer, N., Zuurman, M. W., Wei, T., Ransohoff, R. M., Boddeke, H. W. G. M., & Biber, K. P. H. (2004) · Glia · doi:10.1002/glia.10352 · Cited by 35 · see citing works
Usui, T., Niijima, R., Sakatsume, T., Otani, K., Kameshima, S., Okada, M., & Yamawaki, H. (2014) · Acta Physiologica · doi:10.1111/apha.12354 · Cited by 33 · see citing works
Self-citationMechanisms Underlying Pioglitazone-Mediated Relaxation in Isolated Blood Vessel
Nomura, H., Yamawaki, H., Mukohda, M., Okada, M., & Hara, Y. (2008) · Journal of Pharmacological Sciences · doi:10.1254/jphs.08117fp · Cited by 31 · see citing works
Self-citationUsui, T., Sakatsume, T., Niijima, R., Otani, K., Kazama, K., Morita, T., Kameshima, S., Okada, M., & Yamawaki, H. (2014) · Clinical Science · doi:10.1042/cs20130591 · Cited by 21 · see citing works
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Inflammation and its resolution in atherosclerosis: mediators and therapeutic opportunities
Bäck, M., Yurdagul, A., Tabas, I., Öörni, K., & Kovanen, P. T. (2019) · Nature Reviews Cardiology · doi:10.1038/s41569-019-0169-2 · Cited by 1,341 · see citing works
Chemerin: a multifaceted adipokine involved in metabolic disorders
Helfer, G., & Wu, Q. (2018) · Journal of Endocrinology · doi:10.1530/joe-18-0174 · Cited by 317 · see citing works
Mechanistic Links Between Obesity, Diabetes, and Blood Pressure: Role of Perivascular Adipose Tissue
Saxton, S. N., Clark, B., Withers, S., Eringa, E. C., & Heagerty, A. M. (2019) · Physiological Reviews · doi:10.1152/physrev.00034.2018 · Cited by 277 · see citing works
The Adipokine Hypothesis of Heart Failure With a Preserved Ejection Fraction
Packer, M. (2025) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2025.06.055 · Cited by 190 · see citing works
Kennedy, A. J., & Davenport, A. P. (2017) · Pharmacological Reviews · doi:10.1124/pr.116.013177 · Cited by 175 · see citing works
Chemerin Isoforms and Activity in Obesity
Buechler, C., Feder, S., Haberl, E. M., & Aslanidis, C. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20051128 · Cited by 170 · see citing works
Adipokines and Inflammation: Focus on Cardiovascular Diseases
Feijóo‐Bandín, S., Aragón‐Herrera, A., Moraña‐Fernández, S., Anido‐Varela, L., Tarazón, E., Roselló‐Lletí, E., Portolés, M., Moscoso, I., Gualillo, O., González‐Juanatey, J. R., et al. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21207711 · Cited by 122 · see citing works
Kennedy, A. J., Yang, P. B., Read, C., Kuc, R. E., Yang, L. L. H., Taylor, E. J. A., Taylor, C. W., Maguire, J. J., & Davenport, A. P. (2016) · Journal of the American Heart Association · doi:10.1161/jaha.116.004421 · Cited by 89 · see citing works
New drug targets for hypertension: A literature review
Gao, Q., Xu, L., & Cai, J. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2020.166037 · Cited by 62 · see citing works
Pro‐contractile effects of perivascular fat in health and disease
Ramirez, J. G., O’Malley, E. J., & Ho, W. ‐. V. (2017) · British Journal of Pharmacology · doi:10.1111/bph.13767 · Cited by 61 · see citing works
Chemerin as a Driver of Hypertension: A Consideration
Ferland, D. J., Mullick, A. E., & Watts, S. W. (2020) · American Journal of Hypertension · doi:10.1093/ajh/hpaa084 · Cited by 57 · see citing works
Zhang, J., Yin, Z., Xu, Y. Q., Wei, C., Peng, S., Zhao, M., Liu, J., Xu, S., Pan, W. D., Zheng, Z., et al. (2023) · Hypertension · doi:10.1161/hypertensionaha.123.21348 · Cited by 50 · see citing works
Chemerin-9, a potent agonist of chemerin receptor (ChemR23), prevents atherogenesis
Sato, K., Yoshizawa, H., Seki, T., Shirai, R., Yamashita, T., Okano, T., Shibata, K., Wakamatsu, M. J., Mori, Y., Morita, T., et al. (2019) · Clinical Science · doi:10.1042/cs20190336 · Cited by 50 · see citing works
Darios, E. S., Winner, B. M., Charvat, T. T., Krasinksi, A., Punna, S., & Watts, S. W. (2016) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00998.2015 · Cited by 49 · see citing works
Role of Chemerin in Cardiovascular Diseases
Mačvanin, M., Rizzo, M., Radovanović, J., Sönmez, A., Paneni, F., & Isenović, E. R. (2022) · Biomedicines · doi:10.3390/biomedicines10112970 · Cited by 43 · see citing works
Chemerin – exploring a versatile adipokine
Fischer, T. F., & Beck‐Sickinger, A. G. (2022) · Biological Chemistry · doi:10.1515/hsz-2021-0409 · Cited by 44 · see citing works
Sanges, S., Rice, L. M., Tu, L., Valenzi, E., Cracowski, J., Montani, D., Mantero, J. C., Ternynck, C., Marot, G., Bujor, A. M., et al. (2022) · Annals of the Rheumatic Diseases · doi:10.1136/ard-2022-223237 · Cited by 43 · see citing works
Chemerin-induced arterial contraction is Gi- and calcium-dependent
Ferland, D. J., Darios, E. S., Neubig, R. R., Sjögren, B., Truong, N., Torres, R., Dexheimer, T. S., Thompson, J., & Watts, S. W. (2016) · Vascular Pharmacology · doi:10.1016/j.vph.2016.11.009 · Cited by 43 · see citing works
Kumar, J. D., Aolymat, I., Tiszlavicz, L., Reisz, Z., Garalla, H. M., Beynon, R. J., Simpson, D. M., Dockray, G. J., & Varró, A. (2019) · Oncotarget · doi:10.18632/oncotarget.26414 · Cited by 42 · see citing works
Chemerin Forms: Their Generation and Activity
Zhao, L., Leung, L. L. K., & Morser, J. (2022) · Biomedicines · doi:10.3390/biomedicines10082018 · Cited by 42 · see citing works
Xie, Y., & Liu, L. (2022) · Journal of Translational Medicine · doi:10.1186/s12967-021-03220-7 · Cited by 41 · see citing works
Prochemerin cleavage by factor XIa links coagulation and inflammation
Ge, X., Yamaguchi, Y., Zhao, L., Bury, L., Gresele, P., Berube, C., Leung, L. L. K., & Morser, J. (2017) · Blood · doi:10.1182/blood-2017-07-792580 · Cited by 40 · see citing works
Association of Chemerin and Vascular Endothelial Growth Factor (VEGF) with Diabetic Nephropathy
Lin, S., Teng, J., Li, J., Sun, F., Yuan, D., & Chang, J. (2016) · Medical Science Monitor · doi:10.12659/msm.896781 · Cited by 37 · see citing works
Abais‐Battad, J. M., Lund, H., Fehrenbach, D. J., Dasinger, J. H., Alsheikh, A. J., & Mattson, D. L. (2018) · Hypertension · doi:10.1161/hypertensionaha.118.11994 · Cited by 33 · see citing works
Sun, J.-X., Zhang, C., Cheng, Z.-B., Tang, M.-Y., Liu, Y., Jiang, J.-F., Xiao, X., & Huang, L. (2021) · Clinica Chimica Acta · doi:10.1016/j.cca.2021.05.015 · Cited by 34 · see citing works
Wen, J., Wang, J., Guo, L. P., Cai, W., Wu, Y., Chen, W., & Tang, X. (2019) · Europe PMC (PubMed Central) · Cited by 31 · see citing works
Adipokine Chemerin Stimulates Progression of Atherosclerosis in ApoE−/− Mice
Liu, H., Xiong, W., Luo, Y., Chen, H., He, Y., Cao, Y., & Dong, S. (2019) · BioMed Research International · doi:10.1155/2019/7157865 · Cited by 29 · see citing works
Watts, S. W., Darios, E. S., Mullick, A. E., Garver, H. S., Saunders, T. L., Hughes, E. D., Filipiak, W. E., Zeidler, M. G., McMullen, N. M., Sinal, C. J., et al. (2018) · The FASEB Journal · doi:10.1096/fj.201800479 · Cited by 28 · see citing works
Adipocytokine Involvement in Innate Immune Mechanisms
Żelechowska, P., Kozłowska, E., Pastwińska, J., Agier, J., & Brzezińska‐Błaszczyk, E. (2018) · Journal of Interferon & Cytokine Research · doi:10.1089/jir.2018.0102 · Cited by 28 · see citing works
Kameshima, S., Sakamoto, Y., Okada, M., & Yamawaki, H. (2015) · Acta Physiologica · doi:10.1111/apha.12636 · Cited by 27 · see citing works
Self-citationAssociation of Circulating Chemerin With Subclinical Parameters of Atherosclerosis
Zylla, S., Dörr, M., Völzke, H., Schminke, U., Felix, S. B., Nauck, M. A., & Friedrich, N. (2018) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.118.311219 · Cited by 25 · see citing works
Immunometabolic Regulation of Vascular Redox State: The Role of Adipose Tissue
Oikonomou, E. K., & Antoniades, C. A. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7017 · Cited by 24 · see citing works
Chen, Y., Liu, Z., Gong, P., Zhang, H., Chen, Y., Yao, S., Li, W., Zhang, Y., & Yu, Y. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23169041 · Cited by 25 · see citing works
Omori, A., Goshima, M., Kakuda, C., Kodama, T., Otani, K., Okada, M., & Yamawaki, H. (2020) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-019-02345-5 · Cited by 23 · see citing works
Self-citationChou, H., Teng, M., Hsu, L., Er, L., Wu, S., & Ko, Y. (2021) · Clinical Endocrinology · doi:10.1111/cen.14441 · Cited by 22 · see citing works
Xiong, W. G., Luo, Y., Wu, L., Liu, F., Liu, H., Li, J., Liao, B., & Dong, S. (2016) · PLoS ONE · doi:10.1371/journal.pone.0165305 · Cited by 22 · see citing works
Okada, M., Murata, N., & Yamawaki, H. (2016) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00329.2015 · Cited by 21 · see citing works
Self-citationChemerin influences endothelin- and serotonin-induced pulmonary artery vasoconstriction in rats
Hanthazi, A., Jespers, P., Vegh, G., Degroot, G.-N., Springael, J., Lybaert, P., Dewachter, L., & Entee, K. M. (2019) · Life Sciences · doi:10.1016/j.lfs.2019.116580 · Cited by 21 · see citing works
Okamura, Y., Otani, K., Sekiguchi, A., Kogane, T., Kakuda, C., Sakamoto, Y., Kodama, T., Okada, M., & Yamawaki, H. (2017) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-017-1976-0 · Cited by 19 · see citing works
Self-citationPeng, L., Chen, Y., Li, Y., Feng, P., Zheng, Y., Dong, Y., Yang, Y., Wang, R., Li, A., Yan, J., et al. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.767705 · Cited by 19 · see citing works
Man, A. W. C., Xia, N., & Li, H. (2025) · Cardiovascular Diabetology · doi:10.1186/s12933-025-02814-5 · Cited by 18 · see citing works
Wabel, E., Krieger-Burke, T., & Watts, S. W. (2024) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00475.2024 · Cited by 18 · see citing works
Wójcik, M., Kozioł-Kozakowska, A., Januś, D., Furtak, A., Małek, A., Sztefko, K., & Starzyk, J. (2020) · Journal of Pediatric Endocrinology and Metabolism · doi:10.1515/jpem-2019-0460 · Cited by 18 · see citing works
Increased circulating chemerin in patients with advanced carotid stenosis
Kammerer, A., Staab, H., Herberg, M., Kerner, C., Klöting, N., & Aust, G. (2018) · BMC Cardiovascular Disorders · doi:10.1186/s12872-018-0803-7 · Cited by 18 · see citing works
Flood, E. D., & Watts, S. W. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21176392 · Cited by 16 · see citing works
Chemerin-9 stimulates migration in rat cardiac fibroblasts in vitro
Yamamoto, A., Sagara, A., Otani, K., Okada, M., & Yamawaki, H. (2021) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2021.174566 · Cited by 15 · see citing works
Self-citationNordquist, E., LaHaye, S., Nagel, C., & Lincoln, J. (2018) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2018.00030 · Cited by 15 · see citing works
Chemerin as a Driver of Cardiovascular Diseases: New Perspectives and Future Directions
Imiela, A. M., Stępnicki, J., Zawadzka, P. S., Bursa, A., & Pruszczyk, P. (2025) · Biomedicines · doi:10.3390/biomedicines13061481 · Cited by 13 · see citing works
Hanthazi, A., Jespers, P., Vegh, G., Dubois, C., Hubesch, G., Springael, J., Dewachter, L., & Entee, K. M. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00926 · Cited by 13 · see citing works
Understanding the Role of Chemerin in the Pathophysiology of Pre-Eclampsia
Pankiewicz, K., & Issat, T. (2023) · Antioxidants · doi:10.3390/antiox12040830 · Cited by 13 · see citing works
Yamamoto, A., Matsumoto, K., Hori, K., Kameshima, S., Yamaguchi, N., Okada, S., Okada, M., & Yamawaki, H. (2020) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-020-02391-4 · Cited by 13 · see citing works
Self-citationHsu, L., Chou, H., Teng, M., Wu, S., & Ko, Y. (2021) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2021.01.014 · Cited by 12 · see citing works
Novel Targets for Hypertension Drug Discovery
Bhatt, L. K., Selokar, I., Raut, D., & Hussain, T. (2021) · Current Hypertension Reports · doi:10.1007/s11906-021-01137-6 · Cited by 11 · see citing works
Chemerin is resident to vascular tunicas and contributes to vascular tone
Wabel, E., Orr, A., Flood, E. D., Thompson, J., Xie, H., Demireva, E. Y., Abolibdeh, B., Hulbert, D. H., Mullick, A. E., Garver, H. S., et al. (2023) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00239.2023 · Cited by 11 · see citing works
Kazama, K., Hoshino, K., Kodama, T., Okada, M., & Yamawaki, H. (2016) · Acta Physiologica · doi:10.1111/apha.12739 · Cited by 11 · see citing works
Self-citationChemerin in the Spotlight: Revealing Its Multifaceted Role in Acute Myocardial Infarction
Mitsis, A., Khattab, E., Myrianthefs, M. M., Tzikas, S., Kadoglou, N. P. E., Fragakis, N., Ziakas, A., & Kassimis, G. (2024) · Biomedicines · doi:10.3390/biomedicines12092133 · Cited by 9 · see citing works
Arterial Hypertension: Novel Pharmacological Targets and Future Perspectives
Popa, I. P., Clim, A., Pînzariu, A. C., Lazăr, C. I., Popa, Ș., Tudorancea, I. M., Moscalu, M., Șerban, D. N., Șerban, I. L., Costache-Enache, I.-I., et al. (2024) · Journal of Clinical Medicine · doi:10.3390/jcm13195927 · Cited by 10 · see citing works
MicroRNA-7 overexpression positively regulates the CD8+ SP cell development via targeting PIK3R1
Hu, L. T., Zhou, Y., Yang, J., Zhao, X., Mao, L., Zheng, W., Zhao, J., Guo, M., Chen, C., He, Z., et al. (2021) · Experimental Cell Research · doi:10.1016/j.yexcr.2021.112824 · Cited by 9 · see citing works
Chemokine-like Receptor 1 in Brain of Spontaneously Hypertensive Rats Mediates Systemic Hypertension
Yamamoto, A., Otani, K., Okada, M., & Yamawaki, H. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111812 · Cited by 9 · see citing works
Self-citationChemokine-Like Receptor 1 Regulates the Proliferation and Migration of Vascular Smooth Muscle Cells
Liu, H., Xiong, W. G., Liu, Q., Zhang, J., & Dong, S. (2016) · Medical Science Monitor · doi:10.12659/msm.897832 · Cited by 9 · see citing works
Chemerin as a Mediator of Hypertension and Cardiometabolic Diseases (A Comprehensive Review)
McMillan, R. K., & Kirabo, A. (2025) · Current Hypertension Reports · doi:10.1007/s11906-025-01354-3 · Cited by 8 · see citing works
Chemerin Regulates Epithelial Barrier Function of Mammary Glands in Dairy Cows
Suzuki, Y., Chiba, S., Nishihara, K., Nakajima, K., Hagino, A., Kim, W.-S., Lee, H., Nochi, T., Suzuki, T., & Roh, S. (2021) · Animals · doi:10.3390/ani11113194 · Cited by 7 · see citing works
Wang, J., Xuan, B., Song, B., Wang, T., Lan, C., Guo, W., Yang, Y., & Sun, X. (2025) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-025-05217-y · Cited by 5 · see citing works
Prognostic Utility Of Novel Biomarkers in Aortic Valve Stenosis
Tretjakovs, P., Hofmanis, J., Hofmane, D., Krieviņa, G., Blumfelds, L., Mackēvičs, V., Lejnieks, A., & Bahs, G. (2019) · Proceedings of the Latvian Academy of Sciences Section B Natural Exact and Applied Sciences · doi:10.2478/prolas-2019-0016 · Cited by 4 · see citing works
Zheng, C., Zheng, Y., Chen, X., Zhong, X.-Y., Zheng, X., Yang, S., & Zheng, Z. (2023) · BMC Endocrine Disorders · doi:10.1186/s12902-023-01267-9 · Cited by 4 · see citing works
Li, J., Song, L., & Hui, S. (2021) · Europe PMC (PubMed Central) · Cited by 4 · see citing works
Ahmed, N. A., Hussein, A. A., Khalil, R. G., Yassin, N. Y. S., Abdelaziz, M. A., Geddawy, A., & Ahmed, O. M. (2026) · Biochemistry Research International · doi:10.1155/bri/1761697 · Cited by 3 · see citing works
Wabel, E., Garver, H. S., Krieger-Burke, T., Xie, F., Zeng, L., Mullick, A. E., Fink, G. D., & Watts, S. W. (2026) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00152.2026 · Cited by 2 · see citing works
Chemerin/ChemerinR1 axis and inflammation-related diseases
Li, J., Mao, C., Li, K., Huang, Y., Yang, Y., Li, K., Li, S., & Wen, L. (2026) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2026.1785693 · Cited by 1 · see citing works
The Role of Perivascular Fat in Raising Blood Pressure in Obesity and Diabetes
Aghamohammadzadeh, R., & Heagerty, A. M. (2018) · Updates in hypertension and cardiovascular protection · doi:10.1007/978-3-319-75310-2_20
Pathophysiological Mechanisms Implicated in Organ Damage and Cardiovascular Events
Aghamohammadzadeh, R., & Heagerty, A. M. (2020) · Updates in hypertension and cardiovascular protection · doi:10.1007/978-3-030-47801-8_14
Españoles durante la Segunda Guerra Mundial en Francia
Chaussec, D. (2013) · UCrea (University of Cantabria)
Yamamoto, A., Kodama, T., Otani, K., Okada, M., & Yamawaki, H. (2022) · Journal of Veterinary Medical Science · doi:10.1292/jvms.22-0301
Self-citationClinical Predictive Value and Research Progress of Serum Chemerin
江, 倩. (2024) · Advances in Clinical Medicine · doi:10.12677/acm.2024.1441341
CMKLR-1 Expression in Human Aorta Is Dominated by Smooth Muscle Cell Positivity
Öster, H., Chen, T., Mennander, A., Paavonen, T., & Kholová, I. (2025) · Journal of Histochemistry & Cytochemistry · doi:10.1369/00221554251350743
Sówka, A., Balatskyi, V. V., Navrulin, V. O., Ntambi, J. M., & Dobrzyń, P. (2025) · Biochemical Pharmacology · doi:10.1016/j.bcp.2025.117633
Chemerin, hypertension, and the imperative of sex-based analysis: lessons from Wabel et al.
Webb, R. C. (2026) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00486.2026
Wen, L., Li, S., Xia, X., Huang, Y., Yang, Y., Li, K., Li, J., Xu, M., Liu, C., Liu, G., et al. (2026) · Biomaterials · doi:10.1016/j.biomaterials.2026.124613
Tissue-Specific Chemerin in Atherosclerosis
Chen, M., Li, Y., Linling, F., & Liu, L. (2026) · Biomolecules · doi:10.3390/biom16091327
- Authors
- Kunimoto, H., Kazama, K., Takai, M., Oda, M., Okada, M., & Yamawaki, H.
- Affiliations
- Kitasato University (JP)
- Corresponding author
- Yamawaki, Hideyuki
- Venue
- American Journal of Physiology-Heart and Circulatory Physiology
- Publisher
- American Physiological Society
- Published
- 2015-09
- Volume
- 309
- Issue
- 5
- Pages
- H1017-H1028
- ISSN
- 0363-6135 (ISSN-L)
- 1522-1539
- OpenAlex
- W2134650938
- Cited by
- 79
- References
- 42
- Citations by year
- 2026: 6 · 2025: 7 · 2024: 4 · 2023: 4 · 2022: 8 · 2021: 9 · 2020: 9 · 2019: 9 · 2018: 8 · 2017: 5 · 2016: 8 · 2015: 1 · 2013: 1
- FWCI
- 3.20
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- American Journal of Physiology-Heart and Circulatory Physiology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Japan Society for the Promotion of Science (25292175)
- Topics
- Health Sciences › Medicine › Oncology › Chemokine receptors and signaling
- Life Sciences › Immunology and Microbiology › Immunology › Atherosclerosis and Cardiovascular Diseases
- Health Sciences › Medicine › Surgery › Cardiovascular, Neuropeptides, and Oxidative Stress Research
- Keywords
- chemerin, CMKLR1, vascular smooth muscle cells, cell proliferation, cell migration, hypertension, blood pressure, reactive oxygen species, Akt phosphorylation, ERK1/2 phosphorylation, intimal hyperplasia, vascular remodeling, NADPH oxidase, xanthine oxidase
- MeSH terms
- Animals, Arteries, Blood Pressure, Cell Movement, Cells, Cultured, Humans, Male, Mice, Inbred BALB C, Mice, Inbred C57BL, Muscle, Smooth, Vascular, Rats, Wistar, Reactive Oxygen Species, Chemokines, Myocytes, Smooth Muscle, Intercellular Signaling Peptides and Proteins, Receptors, G-Protein-Coupled, Extracellular Signal-Regulated MAP Kinases, Cell Proliferation, Proto-Oncogene Proteins c-akt, Mice, Rats
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review