Adiponectin stimulates angiogenesis by promoting cross-talk between AMP-activated protein kinase and Akt signaling in endothelial cells
Open accessAbstract
Adiponectin is an adipocyte-specific adipocytokine with anti-atherogenic and anti-diabetic properties. Here, we investigated whether adiponectin regulates angiogenic processes in vitro and in vivo. Adiponectin stimulated the differentiation of human umbilical vein endothelium cells (HUVECs) into capillary-like structures in vitro and functioned as a chemoattractant in migration assays. Adiponectin promoted the phosphorylation of AMP-activated protein kinase (AMPK), protein kinase Akt/protein kinase B, and endothelial nitric oxide synthesis (eNOS) in HUVECs. Transduction with either dominant-negative AMPK or dominant-negative Akt abolished adiponectin-induced eNOS phosphorylation as well as adiponectin-stimulated HUVEC migration and differentiation. Dominant-negative AMPK also inhibited adiponectin-induced Akt phosphorylation, suggesting that AMPK is upstream of Akt. Dominant-negative Akt or the phosphatidylinositol 3-kinase inhibitor LY294002 blocked adiponectin-stimulated Akt and eNOS phosphorylation, migration, and differentiation without altering AMPK phosphorylation. Finally, adiponectin stimulated blood vessel growth in vivo in mouse Matrigel plug implantation and rabbit corneal models of angiogenesis. These data indicate that adiponectin can function to stimulate the new blood vessel growth by promoting cross-talk between AMP-activated protein kinase and Akt signaling within endothelial cells.
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AMPK lies upstream of the phosphatidylinositol-3-kinase-protein kinase B pathway, which also leads to eNOS activation and NO production.
“Further evidence also shows that AMPK lies upstream of the phosphatidylinositol-3-kinase-protein kinase B pathway, which also leads to eNOS activation and NO production [162,164,165].”
From AMPK, Mitochondrial Function, and Cardiovascular Disease (2020) · cites this paper as [164]
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Shibata, R., Ouchi, N., Kihara, S., Sato, K., Funahashi, T., & Walsh, K. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402558200 · Cited by 336 · see citing works
Self-citationOsteocalcin: Skeletal and extra‐skeletal effects
Neve, A., Corrado, A., & Cantatore, F. P. (2013) · Journal of Cellular Physiology · doi:10.1002/jcp.24278 · Cited by 335 · see citing works
“As adiponectin has been demonstrated to be able to induce angiogenesis (Ouchi et al., 2004), it appears conceivable that OC could also induce angiogenesis through adiponectin.”
BackgroundEndo, H., Niioka, M., Kobayashi, N., Tanaka, M., & Watanabe, T. (2013) · PLoS ONE · doi:10.1371/journal.pone.0063388 · Cited by 335 · see citing works
Adiponectin actions in the cardiovascular system
Hopkins, T. A., Ouchi, N., Shibata, R., & Walsh, K. X. (2006) · Cardiovascular Research · doi:10.1016/j.cardiores.2006.10.009 · Cited by 326 · see citing works
“Adiponectin supplementation has also been shown to stimulate blood vessel growth in both mouse Matrigel plug implantation and rabbit corneal models of angiogenesis [70].”
BackgroundAdiponectin action from head to toe
Brochu‐Gaudreau, K., Rehfeldt, C., Blouin, R., Bordignon, V., Murphy, B. D., & Palin, M. (2009) · Endocrine · doi:10.1007/s12020-009-9278-8 · Cited by 323 · see citing works
Cheng, K. K. Y., Lam, K. S. L., Wang, Y., Huang, Y., Carling, D., Wu, D., Wong, C., & Xu, A. (2007) · Diabetes · doi:10.2337/db06-1580 · Cited by 318 · see citing works
“Previous studies have shown that adiponectin stimulates NO production through activation of the AMPK/ eNOS signaling cascade (12,16).”
BackgroundResultInfluentialCardiac Energy Metabolism in Obesity
Lopaschuk, G. D., Folmes, C. D. L., & Stanley, W. C. (2007) · Circulation Research · doi:10.1161/circresaha.107.150417 · Cited by 302 · see citing works
Obesity, Diabetes, and Increased Cancer Progression
Kim, D.-S., & Scherer, P. E. (2021) · Diabetes & Metabolism Journal · doi:10.4093/dmj.2021.0077 · Cited by 312 · see citing works
“Activation of several metabolic signaling pathways including IKKβ/NF-κB and c-Jun N-terminal kinase (JNK) pathways by excess nutrients leads to initiation of obesity-associated inflammation and a subsequent chronic low-grade inflammatory response (Fig.”
BackgroundActivation and Signaling by the AMP-Activated Protein Kinase in Endothelial Cells
Fisslthaler, B., & Fleming, I. (2009) · Circulation Research · doi:10.1161/circresaha.109.201590 · Cited by 295 · see citing works
Role of adipokines in cardiovascular disease
Mattu, H. S., & Randeva, H. S. (2012) · Journal of Endocrinology · doi:10.1530/joe-12-0232 · Cited by 292 · see citing works
Vascular effects of adiponectin: molecular mechanisms and potential therapeutic intervention
Zhu, W., Cheng, K. K. Y., Vanhoutte, P. M., Lam, K. S. L., & Xu, A. (2008) · Clinical Science · doi:10.1042/cs20070347 · Cited by 285 · see citing works
APPL1: role in adiponectin signaling and beyond
Deepa, S. S., & Dong, L. (2008) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90731.2008 · Cited by 287 · see citing works
Protective vascular and myocardial effects of adiponectin
Goldstein, B. J., Scalia, R. G., & Ma, X. L. (2008) · Nature Clinical Practice Cardiovascular Medicine · doi:10.1038/ncpcardio1398 · Cited by 288 · see citing works
“AMP kinase also mediates at least some of the vascular effects of adiponectin in endothelial cells, especially those involving eNOS activation”
BackgroundAdiponectin and cardiovascular health: an update
Hui, X. H., Lam, K. S., Vanhoutte, P. M., & Xu, A. (2011) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2011.01395.x · Cited by 287 · see citing works
“Indeed, a crosstalk between PI3-Kinase/Akt and AMPK in endothelial cells has been implicated in adiponectin-induced angiogenesis (Ouchi et al., 2004).”
BackgroundAMPK, Mitochondrial Function, and Cardiovascular Disease
Wu, S., & Zou, M.-H. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21144987 · Cited by 286 · see citing works
“Further evidence also shows that AMPK lies upstream of the phosphatidylinositol‐3‐kinase‐protein kinase B pathway, which also leads to eNOS activation and NO production [162,164,165].”
BackgroundAdiponectin receptor signalling in the brain
Thundyil, J., Pavlovski, D., Sobey, C. G., & Arumugam, T. V. (2011) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2011.01560.x · Cited by 282 · see citing works
“AMPK activation is also involved in adiponectinmediated actions in vascular endothelial cells and the heart, in a manner that is reported to be beneficial in protection against cardiovascular diseases (Kobayashi et al., 2004; Ouchi et al., 2004).”
BackgroundStatins Activate AMP-Activated Protein Kinase In Vitro and In Vivo
Sun, W., Lee, T., Zhu, M., Gu, C., Wang, Y., Zhu, Y., & Shyy, J. Y.-J. (2006) · Circulation · doi:10.1161/circulationaha.106.630194 · Cited by 264 · see citing works
Recinella, L., Orlando, G., Ferrante, C., Chiavaroli, A., Brunetti, L., & Leone, S. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.578966 · Cited by 261 · see citing works
“The vasoprotective effects of adiponectin could be due to increased production of nitric oxide through activation of endothelial NO synthase (eNOS) via AMPKdependent (Kobayashi et al., 2004; Ouchi et al., 2004) as well as cyclooxygenase 2-dependent mechanisms (Ohashi et al., 2009).”
BackgroundOng, K. W., Hsu, A., & Tan, B. K. H. (2012) · PLoS ONE · doi:10.1371/journal.pone.0032718 · Cited by 270 · see citing works
Cardioprotection by Adiponectin
Ouchi, N., Shibata, R., & Walsh, K. X. (2006) · Trends in Cardiovascular Medicine · doi:10.1016/j.tcm.2006.03.001 · Cited by 257 · see citing works
“Consistent with its angiogenic actions, adiponectin stimulates endothelial cell migration and differentiation into capillary-like structures in vitro through activation of AMPK signaling (Ouchi et al. 2004).”
BackgroundAdiponectin Inhibits Endothelial Synthesis of Interleukin-8
Kobashi, C., Urakaze, M., Kishida, M., Kibayashi, E., Kobayashi, H., Kihara, S., Funahashi, T., Takata, M., Temaru, R., Sato, A., et al. (2005) · Circulation Research · doi:10.1161/01.res.0000194328.57164.36 · Cited by 255 · see citing works
Baratta, R., Amato, S., Degano, C., Farina, M. G., Patanè, G., Vigneri, R., & Frittitta, L. (2004) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2003-031777 · Cited by 253 · see citing works
Ouedraogo, R., Wu, X., Xu, S., Fuchsel, L., Motoshima, H., Mahadev, K., Hough, K., Scalia, R. G., & Goldstein, B. J. (2006) · Diabetes · doi:10.2337/db05-1174 · Cited by 250 · see citing works
“Adiponectin is known to activate AMPK in endothelial cells (15,31,32), and recently activation of AMPK has been shown to reduce ROS derived from mitochondria in high-glucose conditions (33).”
BackgroundAdiponectin: a versatile player of innate immunity
Luo, Y., & Liu, M. (2016) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjw012 · Cited by 244 · see citing works
“…(Scherer et al., 1995; Hu et al., 1996; Maeda et al., 1996; Pajvani et al., 2004), insulin resistance (Tomas et al., 2002; Gil-Campos et al., 2004; Haluzik et al., 2004; Hoffstedt et al., 2004), and cardiovascular diseases (Goldstein and Scalia, 2004; Ouchi et al., 2004; Shibata et al., 2005).”
BackgroundResveratrol inhibits cardiac hypertrophy via AMP-activated protein kinase and Akt
Chan, A. Y. M., Dolinsky, V. W., Soltys, C.-L. M., Viollet, B., Baksh, S., Light, P. E., & Dyck, J. R. B. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802869200 · Cited by 244 · see citing works
Igata, M., Motoshima, H., Tsuruzoe, K., Kojima, K., Matsumura, T., Kondo, T., Taguchi, T., Nakamaru, K., Yano, M., Kukidome, D., et al. (2005) · Circulation Research · doi:10.1161/01.res.0000185823.73556.06 · Cited by 244 · see citing works
Park, C.-E., Kim, M., Lee, J. H., Min, B.-I., Bae, H., Choe, W., Kim, S. S., & Ha, J. (2007) · Experimental & Molecular Medicine · doi:10.1038/emm.2007.25 · Cited by 239 · see citing works
“However, some other reports suggest that AMPK functions upstream of Akt signaling (Ouchi et al., 2004).”
BackgroundOuchi, N., Shibata, R., & Walsh, K. (2005) · Circulation Research · doi:10.1161/01.res.0000163633.10240.3b · Cited by 238 · see citing works
Transcriptional and post-translational regulation of adiponectin
Liu, M., & Liu, F. (2009) · Biochemical Journal · doi:10.1042/bj20091045 · Cited by 234 · see citing works
The autocrine and paracrine roles of adipokines
Karastergiou, K., & Mohamed-Ali, V. (2010) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2009.11.011 · Cited by 233 · see citing works
“Adiponectin, by activating AMP kinase in endothelial cells, is also able to induce angiogenesis (Ouchi et al., 2004), as shown in adiponectin-deficient mice, which have impaired responses to ischemia (Shibata et al., 2004).”
BackgroundAngiogenesis and development of adipose tissue
Christiaens, V., & LIJNEN, H. R. (2009) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2009.08.006 · Cited by 234 · see citing works
“However, adiponectin has also been reported to activate adenosine monophosphate kinase in endothelial cells, leading to enhanced in vivo angiogenesis in murine Matrigel plug and rabbit cornea assays and to inhibition of caspase 3-mediated apoptosis in HUVECs cultured in vitro (Kobayashi et al., 2004; Ouchi et al., 200…”
Wijesekara, N., Krishnamurthy, M., Bhattacharjee, A., Suhail, A., Sweeney, G., & Wheeler, M. B. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.085084 · Cited by 229 · see citing works
Anti-inflammatory and anti-atherogenic properties of adiponectin
Ohashi, K., Ouchi, N., & Matsuzawa, Y. (2012) · Biochimie · doi:10.1016/j.biochi.2012.06.008 · Cited by 224 · see citing works
“Adiponectin normalizes elevated blood pressure of APN-KO mice via an eNOS-dependent mechanism [32] Treatment of cultured endothelial cells with adiponectin protein enhances differentiation into capillary-like structures and migration, and reduces apoptosis in response to serum starvation partly through AMP activated p…”
BackgroundInfrapatellar fat pad features in osteoarthritis: a histopathological and molecular study
Favero, M., Hadi, H. E., Belluzzi, E., Granzotto, M., Porzionato, A., Sarasin, G., Rambaldo, A., Iacobellis, C., Cigolotti, A., Fontanella, C. G., et al. (2017) · Rheumatology · doi:10.1093/rheumatology/kex287 · Cited by 219 · see citing works
Adiponectin and Cardiovascular Disease
Shibata, R., Ouchi, N., & Murohara, T. (2009) · Circulation Journal · doi:10.1253/circj.cj-09-0057 · Cited by 214 · see citing works
Adipose tissue angiogenesis: Impact on obesity and type-2 diabetes
Corvera, S., & Gealekman, O. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.06.003 · Cited by 211 · see citing works
Stahmann, N., Woods, A., Carling, D., & Heller, R. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00383-06 · Cited by 214 · see citing works
“AMPK has been shown to mediate serine 1177 phosphorylation in response to hypoxia, peroxynitrite, and adiponectin (7, 33, 35, 49, 50).”
BackgroundResultInfluentialAdiponectin Deficiency Increases Allergic Airway Inflammation and Pulmonary Vascular Remodeling
Medoff, B. D., Okamoto, Y., Leyton, P., Weng, M., Sandall, B. P., Raher, M. J., Kihara, S., Bloch, K. D., Libby, P., & Luster, A. D. (2009) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2008-0415oc · Cited by 208 · see citing works
Adiponectin protects against the development of systolic dysfunction following myocardial infarction
Shibata, R., Izumiya, Y., Sato, K., Papanicolaou, K. N., Kihara, S., Colucci, W. S., Sam, F., Ouchi, N., & Walsh, K. X. (2007) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2007.03.808 · Cited by 213 · see citing works
“In accordance with these observations, we have previously shown that adiponectin can function as a survival factor for endothelial cells [41] and that APN-KO mice exhibit impaired angiogenic repair in ischemic hindlimbs whereas adiponectin overexpression stimulates blood vessel growth [14,42].”
Zhang, Y., Lee, T.-S., Kolb, E. M., Sun, K., Lu, X., Sladek, F. M., Kassab, G. S., Garland, T., & Shyy, J. Y.-J. (2006) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000221230.08596.98 · Cited by 212 · see citing works
Nishimura, M., Izumiya, Y., Higuchi, A., Shibata, R., Qiu, J., Kudo, C., Shin, H. K., Moskowitz, M. A., & Ouchi, N. (2007) · Circulation · doi:10.1161/circulationaha.107.725044 · Cited by 207 · see citing works
Agonist-modulated Regulation of AMP-activated Protein Kinase (AMPK) in Endothelial Cells
Levine, Y. C., Li, G. K., & Michel, T. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702182200 · Cited by 207 · see citing works
Han, S., Khuri, F. R., & Roman, J. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-2367 · Cited by 207 · see citing works
“AMPK has been shown to diminish protein synthesis by activating TSc2, leading to inhibition of mTOR and subsequent inhibition of p70S6K protein activity (20, 33).”
BackgroundZheng, Q., Yuan, Y., Yi, W., Lau, W. B., Wang, Y., Wang, X., Sun, Y., Lopez, B. L., Christopher, T. A., Peterson, J. M., et al. (2011) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.111.231050 · Cited by 202 · see citing works
Adiponectin Acts as an Endogenous Antithrombotic Factor
Kato, H., Kashiwagi, H., Shiraga, M., Tadokoro, S., Kamae, T., Ujiie, H., Honda, S., Miyata, S., Ijiri, Y., Yamamoto, J., et al. (2005) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000194076.84568.81 · Cited by 202 · see citing works
Guerre-Millo, M. (2008) · Diabetes & Metabolism · doi:10.1016/j.diabet.2007.08.002 · Cited by 198 · see citing works
Adiponectin: Anti-inflammatory and cardioprotective effects
Villarreal-Molina, M. T., & Antuna-Puente, B. (2012) · Biochimie · doi:10.1016/j.biochi.2012.06.030 · Cited by 197 · see citing works
Adiponectin, an adipocyte-derived protein
Nedvidkova, J., Smitka, K., Kopský, V., & Hainer, V. (2005) · Physiological Research · doi:10.33549/physiolres.930600 · Cited by 195 · see citing works
Walnuts (Juglans regia) Chemical Composition and Research in Human Health
Hayes, D., Angove, M. J., Tucci, J., & Dennis, C. (2015) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2012.760516 · Cited by 203 · see citing works
“These molecules are known for their anti-inflammatory (Ouchi et al., 2004; Ohashia et al., 2012) and insulin resistance properties (Yamauchi et al.”
BackgroundIdentification of Adiponectin as a Novel Hemopoietic Stem Cell Growth Factor
DiMascio, L. N., Voermans, C., Uqoezwa, M., Duncan, A. W., Lu, D., Wu, J., Sankar, U., & Reya, T. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.178.6.3511 · Cited by 192 · see citing works
“First, we cultured HSCs infected with either a wild-type or dominant-negative form of AMPK in the presence or absence of adiponectin.”
BackgroundResultInfluentialThe fat and the bad: Mature adipocytes, key actors in tumor progression and resistance
Duong, M. N., Geneste, A., Fallone, F., Li, X., Dumontet, C., & Muller, C. (2017) · OncoTarget · doi:10.18632/oncotarget.18038 · Cited by 178 · see citing works
“While some studies showed that adiponectin may be pro-angiogenesis [77, 115, 116, 119, 120], other studies reported an inhibition of angiogenesis both in vitro and in vivo [121, 122].”
BackgroundAdiponectin Induces Periovulatory Changes in Ovarian Follicular Cells
Ledoux, S., Campos, D. B., Lopes, F. L., Dobias-Goff, M., Palin, M., & Murphy, B. D. (2006) · Endocrinology · doi:10.1210/en.2006-0679 · Cited by 188 · see citing works
Yu, J., Deng, Y., Han, X., Ren, G., Cai, J., & Jiang, G. (2016) · Cardiovascular Diabetology · doi:10.1186/s12933-016-0408-3 · Cited by 188 · see citing works
Salt, I. P., & Hardie, D. G. (2017) · Circulation Research · doi:10.1161/circresaha.117.309633 · Cited by 186 · see citing works
Chabrolle, C., Tosca, L., & Dupont, J. (2007) · Reproduction · doi:10.1530/rep-06-0244 · Cited by 186 · see citing works
“…(2007) 133 719–731 Adiponectin activates various signalling pathways in rat granulosa cells Recombinant adiponectin is known to stimulate different signalling pathways including AMPK, MAPK and Akt in various cell types (Yamauchi et al. 2002, Wu et al. 2003, Ouchi et al. 2004, Luo et al. 2005).”
BackgroundRole of Adiponectin in Central Nervous System Disorders
Bloemer, J., Pinky, P. D., Govindarajulu, M., Hong, H., Judd, R. L., Amin, R., Moore, T., Dhanasekaran, M., Reed, M. N., & Suppiramaniam, V. D. (2018) · Neural Plasticity · doi:10.1155/2018/4593530 · Cited by 182 · see citing works
“AMPK signaling is also required for vascular endothelial growth factor -stimulated endothelial cell NO production, migration, and differentiation in response to hypoxic conditions and increased oxidative stress in stroke [76], which also promotes angiogenesis in vivo.”
BackgroundAdipokines, Myokines and Cardiovascular Disease
Walsh, K. X. (2008) · Circulation Journal · doi:10.1253/circj.cj-08-0961 · Cited by 177 · see citing works
Nonclassic Endogenous Novel Regulators of Angiogenesis
Ribatti, D., Conconi, M. T., & Nussdorfer, G. G. (2007) · Pharmacological Reviews · doi:10.1124/pr.59.2.3 · Cited by 178 · see citing works
“Adiponectin has been reported to activate adenosine monophosphate kinase in ECs, leading to enhanced in vivo angiogenesis in murine Matrigel plug and rabbit cornea assays and inhibition of caspase 3-mediated apoptosis in HUVECs cultured in vitro (Kobayashi et al., 2004; Ouchi et al., 2004).”
BackgroundRole of Adipokines in Cardiovascular Disease
Lau, W. B., Ohashi, K., Wang, Y., Ogawa, H., Murohara, T., Ma, X., & Ouchi, N. (2017) · Circulation Journal · doi:10.1253/circj.cj-17-0458 · Cited by 183 · see citing works
AMPK, metabolism, and vascular function
Rodríguez, C., Muñoz, M., Contreras, C., & Prieto, D. (2021) · FEBS Journal · doi:10.1111/febs.15863 · Cited by 178 · see citing works
Kim, H.-S., Kim, M.-J., Kim, E. J., Yang, Y. D., Lee, M., & Lim, J. (2011) · Biochemical Pharmacology · doi:10.1016/j.bcp.2011.11.008 · Cited by 175 · see citing works
“AMPK activation also increases human umbilical vein endothelial cell migration and contributes to transendothelial lymphocyte migration [39,40].”
BackgroundNicolai, A., Li, M., Kim, D. H., Peterson, S. J., Vanella, L., Positano, V., Gastaldelli, A., Rezzani, R., Rodella, L. F., Drummond, G., et al. (2009) · Hypertension · doi:10.1161/hypertensionaha.108.124701 · Cited by 170 · see citing works
T-cadherin Is Essential for Adiponectin-mediated Revascularization*
Parker, J., Nakamura, K., Silver, M., Kikuchi, R., Tigges, U., Yoshida, S., Denzel, M. S., Ranscht, B., & Walsh, K. X. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.454835 · Cited by 170 · see citing works
“It has been reported previously that adiponectin promotes endothelial cell migration and proliferation in vitro (9, 50, 51).”
BackgroundMaruyama, S., Shibata, R., Kikuchi, R., Izumiya, Y., Rokutanda, T., Araki, S., Kataoka, Y., Ohashi, K., Daida, H., Kihara, S., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.261818 · Cited by 167 · see citing works
Hebbard, L., Garlatti, M., Young, L. J. T., Cardiff, R. D., Oshima, R. G., & Ranscht, B. (2008) · Cancer Research · doi:10.1158/0008-5472.can-07-2953 · Cited by 166 · see citing works
“With T-cadherin regulating neovascularization in vivo , the primary question arising from our studies is ‘‘How does T-cadherin regulate blood vessel growth?’’ T-cadherin is a binding partner for the hexameric and high molecular weight forms of adiponectin (21) and adiponectin is implicated in vascular functions (32, 3…”
BackgroundHu, T., RamachandraRao, S., Siva, S., Valancius, C., Zhu, Y., Mahadev, K., Toh, I., Goldstein, B. J., Woolkalís, M. J., & Sharma, K. (2005) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00024.2005 · Cited by 166 · see citing works
“Transduction efficiency as measured by percent of cells expressing -galactosidase was 90–95%, similar to prior studies with adenoviral transduction efficiency in HUVEC (22, 24).”
Result
- Authors
- Ouchi, N., Kobayashi, H., Kihara, S., Kumada, M., Sato, K., Inoue, T., Funahashi, T., & Walsh, K.
- Affiliations
- Boston University (US)
- The University of Osaka (JP)
- Corresponding author
- Walsh, Kenneth
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2004-01
- Volume
- 279
- Issue
- 2
- Pages
- 1304-1309
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC4374490
- OpenAlex
- W2008967025
- Cited by
- 759
- References
- 49
- Citations by year
- 2026: 5 · 2025: 10 · 2024: 20 · 2023: 15 · 2022: 21 · 2021: 23 · 2020: 23 · 2019: 25 · 2018: 22 · 2017: 40 · 2016: 26 · 2015: 39 · 2014: 30 · 2013: 58 · 2012: 58
- FWCI
- 14.45
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Uehara Memorial Foundation
- National Institutes of Health (HD23681, AG15052)
- National Institute on Aging (R01AG015052, AG17241, R37AG015052, AG15052, R01AG017241)
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (AR-40197, R01AR040197)
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (P01HD023681, HD23681)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Angiogenesis and VEGF in Cancer
- Health Sciences › Medicine › Epidemiology › Adipokines, Inflammation, and Metabolic Diseases
- Health Sciences › Medicine › Physiology › Adipose Tissue and Metabolism
- Keywords
- adiponectin, angiogenesis, AMPK, Akt signaling, endothelial cells, endothelial nitric oxide synthase, endothelial cell migration, endothelial differentiation, capillary tube formation, phosphatidylinositol 3-kinase, signaling crosstalk, blood vessel development
- MeSH terms
- Adenoviridae, Animals, Cell Differentiation, Cell Movement, Cells, Cultured, Chromones, Collagen, Drug Combinations, Endothelium, Vascular, Enzyme Inhibitors, Genes, Dominant, Humans, Laminin, Models, Biological, Morpholines, Multienzyme Complexes, Neovascularization, Pathologic, Phosphorylation, Proteins, Proteoglycans, Rabbits, Recombinant Proteins, Time Factors, Umbilical Veins, Blotting, Western, Signal Transduction, Protein Serine-Threonine Kinases, Nitric Oxide Synthase, Phosphatidylinositol 3-Kinases, Intercellular Signaling Peptides and Proteins, Endothelial Cells, Mice, Adiponectin, Nitric Oxide Synthase Type II, Nitric Oxide Synthase Type III, AMP-Activated Protein Kinases
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