Table 1. The possible relationship between RAS components and AMPK.

Components of RAS	Tissue or cell type	Relation to AMPK		Related studies
ACE	Heart	No direct relation was shown		[77–79]
	Vascular system endothelial cells	AMPKα2 suppresses endothelial ACE expression via the phosphorylation of p53 and up-regulation of miR-143/145		[75]
	Monocytes	ACE expression was reduced in spleen derived-monocytes from AMPKα1(−/−) mice versus their wild-type littermates		[74]
	White adipose tissue	AMPK may decrease ACE expression		[76]
AngII	Heart	Rat neonatal cardiomyocytes	AngII down-regulates AMPK (α-Thr172) may be by phosphorylating α-Ser485/491 or inhibiting LKB1	[78,84–86]
		Neonatal rat ventricular myocytes (NRVMs)	Activation of AMPK can ameliorate pathological damage induced by AngII	[103,108]
		H9C2 cells neonatal rat cardiomyocyte (NRCMs)	No direct relation was shown	[88,89]
		HL-1 atrial myocytes	Ang ІІ decreased oxygen consumption rate, which resulted in ROS generation, AngII-induced intracellular calcium production. The generated ROS and calcium stimulated AMPK phosphorylation. Inhibiting AMPK blocked AngII-mediated JNK and TGF-β signaling pathways	[90]
AngII	Vascular system	VSMCs	AngII-induced AMPK activation and that AMPK works as an inhibitor of the AngII proliferative pathway	[91]
		VSMCs	AngII led to minor activation of AMPK at a low concentration (0.1–1 μM), whereas AngII suppressed AMPKα activity at a high concentration (5 μM) AngII could elevate LKB1 expression in VSMCs, while the activity of LKB1 was not elevated with the expression of LKB1, even declined slightly	[92–94]
		VSMC human umbilical vein endothelial cells (HUVECs)	Activation of AMPK can ameliorate pathological damage induced by AngII	[104–107,109]
AngII	Skeletal muscle	AngII inhibits AMPK Thr172 and AngII might up-regulate the AMPK resistance		[97,109]
	Kidney	AngII inhibits AMPK by binding to AT1 p-AMPK increase after ARB application		[100–102,105]
AT1R	Heart	AT1 is negatively related to AMPK, ARB could phosphorylate AMPK		[112,113,117]
	Skeletal muscle	ARB can improve AMPK resistance and activate AMPK		[97–99]
AT2R	White adipocytes	AT2R may activate AMPK independent of AngII		[119]
	Pulmonary artery endothelial cells (PAECs)	By binding to AT2R, AngII induces apoptosis by phosphorylating AMPK β		[120,121]
	Chinese hamster ovary (CHO)-K1 cells	Both AT1R and AT2R overexpression activated AMPK		[120]
ACE2	Heart	ACE2 could activate AMPK		[85,123,124]
	Adipose tissue	Phosphorylation of AMPK is reduced when ACE2 is knocked out		[124]
	Huh7 (hepatocellular carcinoma-derived) cells	AMPK activation can increase ACE2 expression, but this effect requires sirtuin 1 (SIRT1) to participate		[76,125]
	HUVECs and human embryonic kidney 293 (HEK293T) cells	Phosphorylated ACE2 Ser680 by AMPK could enhance the ACE2 stability		[126]
Ang(1-7)	Vascular systemaortas versus aortic tissues	Ang(1-7) could activate AMPK		[124,131]
	White adipose tissue	Ang(1-7) could activate AMPK		[76]
MasR	Adipose tissue	MasR may be positively related to AMPK		[76,124]
MrgD	Ventricular cardiomyocytes	Almandine could activate AMPK by activating LKB1		[89]