Aim:To examine the inhibitory effect of FAK-related nonkinase(FRNK)in cardiachypertrophy in vitro and investigate the possible mechanisms.Methods:A func-tional fragment of FRNK cDNA was amplified by reverse transcription-polymerasechain reaction and cloned into the vector pcDNA3.1.Hypertrophy in neonatal ratcardiac myocytes was established with angiotensin-Ⅱ stimulation.The pcDNA3.1-FRNK or pcDNA3.1 was respectively transfected into cardiomyocytes byLipofectamine 2000.The surface area and mRNA expression of atrial natriureticpeptide(ANP)of myocytes were employed to detect cardiac hypertrophy.NF-κBp65 protein in nuclear extracts,phosphorylation levels of ERK1/2(p-ERK 1/2)andAKT(p-AKT),as well as total ERK1/2,and AKT in variant treated cardiomyocyteswere determined by Western blot.Results:Under the stimulation of angiotensin Ⅱ,the surface area of myocytes and levels ofANP mRNA were significantly increased.But transient transfection with pcDNA3.1-FRNK in advance may reduce the sur-face area and expression of ANP mRNA of hypertrophic myocytes.The proteinlevels of NF-κB p65 in nuclear extracts and p-ERKI/2,p-AKT in FRNK treatedcardiomyocytes were significantly decreased compared with that in angiotensin-Ⅱ induced cardiomyocytes,while different treatments had little effect on totalERK1/2 and AKT.Conclusion:FRNK may inhibit angiotensin-Ⅱ-inducedcardiomyocyte hypertrophy via decreasing phosphorylation levels at ERK1/2 andAKT,consequently downregulating nuclear translocation of NF-κB p65. Aim: To examine the inhibitory effect of FAK-related nonkinase (FRNK) in cardiachypertrophy in vitro and investigate the possible mechanisms. Methods: A func-tional fragment of FRNK cDNA was amplified by reverse transcription-polymerase chain reaction and cloned into the vector pcDNA3. 1. Hypertrophy in neonatal rat cardiac myocytes was established with angiotensin-II stimulation. The pcDNA3.1-FRNK or pcDNA3.1 was respectively transfected into cardiomyocytes by Lipofectamine 2000. The surface area and mRNA expression of atrial natriuretic peptide (ANP) of myocytes were employed to detect cardiac hypertrophy.NF-κBp65 protein in nuclear extracts, phosphorylation levels of ERK1 / 2 (p-ERK 1/2) and AKT (p-AKT), as well as total ERK1 / 2, and AKT in variant treated cardiomyocyteswere determined by Western blot. Results: Under the stimulation of angiotensin II, the surface area of ​​myocytes and levels of ANP mRNA were significantly increased. By transient transfection with pcDNA3.1-FRNK in advance may reduce the sur-fa ce area and expression of ANP mRNA of hypertrophic myocytes. Protein fractions of NF-κB p65 in nuclear extracts and p-ERKI / 2, p-AKT in FRNK treated cardiomyocytes were significantly decreased compared with that in angiotensin-Ⅱ induced cardiomyocytes, while different different treatments had little effect on total ERK1 / 2 and AKT.Conclusion: FRNK may inhibit angiotensin-Ⅱ-induced cardiomyocyte hypertrophy via decreasing phosphorylation levels at ERK1 / 2 and AKT, down downregulating nuclear translocation of NF-κB p65.