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Articles by S Miyamoto
Total Records ( 4 ) for S Miyamoto
  G. A Borillo , M Mason , P Quijada , M Volkers , C Cottage , M McGregor , S Din , K Fischer , N Gude , D Avitabile , S Barlow , R Alvarez , S Truffa , R Whittaker , M. S Glassy , A. B Gustafsson , S Miyamoto , C. C Glembotski , R. A Gottlieb , J. H Brown and M. A. Sussman

Rationale: Cardioprotective signaling mediates antiapoptotic actions through multiple mechanisms including maintenance of mitochondrial integrity. Pim-1 kinase is an essential downstream effector of AKT-mediated cardioprotection but the mechanistic basis for maintenance of mitochondrial integrity by Pim-1 remains unexplored. This study details antiapoptotic actions responsible for enhanced cell survival in cardiomyocytes with elevated Pim-1 activity.

Objective: The purpose of this study is to demonstrate that the cardioprotective kinase Pim-1 acts to inhibit cell death by preserving mitochondrial integrity in cardiomyocytes.

Methods and Results: A combination of biochemical, molecular, and microscopic analyses demonstrate beneficial effects of Pim-1 on mitochondrial integrity. Pim-1 protein level increases in the mitochondrial fraction with a corresponding decrease in the cytosolic fraction of myocardial lysates from hearts subjected to 30 minutes of ischemia followed by 30 minutes of reperfusion. Cardiac-specific overexpression of Pim-1 results in higher levels of antiapoptotic Bcl-XL and Bcl-2 compared to samples from normal hearts. In response to oxidative stress challenge, Pim-1 preserves the inner mitochondrial membrane potential. Ultrastructure of the mitochondria is maintained by Pim-1 activity, which prevents swelling induced by calcium overload. Finally, mitochondria isolated from hearts created with cardiac-specific overexpression of Pim-1 show inhibition of cytochrome c release triggered by a truncated form of proapoptotic Bid.

Conclusion: Cardioprotective action of Pim-1 kinase includes preservation of mitochondrial integrity during cardiomyopathic challenge conditions, thereby raising the potential for Pim-1 kinase activation as a therapeutic interventional approach to inhibit cell death by antagonizing proapoptotic Bcl-2 family members that regulate the intrinsic apoptotic pathway.

  S Miyamoto , N. H Purcell , J. M Smith , T Gao , R Whittaker , K Huang , R Castillo , C. C Glembotski , M. A Sussman , A. C Newton and J. H. Brown

The recently discovered PHLPP-1 (PH domain leucine-rich repeat protein phosphatase-1) selectively dephosphorylates Akt at Ser473 and terminates Akt signaling in cancer cells. The regulatory role of PHLPP-1 in the heart has not been considered.


To test the hypothesis that blockade/inhibition of PHLPP-1 could constitute a novel way to enhance Akt signals and provide cardioprotection.

Methods and Results:

PHLPP-1 is expressed in neonatal rat ventricular myocytes (NRVMs) and in adult mouse ventricular myocytes (AMVMs). PHLPP-1 knockdown by small interfering RNA significantly enhances phosphorylation of Akt (p-Akt) at Ser473, but not at Thr308, in NRVMs stimulated with leukemia inhibitory factor (LIF). The increased phosphorylation is accompanied by greater Akt catalytic activity. PHLPP-1 knockdown enhances LIF-mediated cardioprotection against doxorubicin and also protects cardiomyocytes against H2O2. Direct Akt effects at mitochondria have been implicated in cardioprotection and mitochondria/cytosol fractionation revealed a significant enrichment of PHLPP-1 at mitochondria. The ability of PHLPP-1 knockdown to potentiate LIF-mediated increases in p-Akt at mitochondria and an accompanying increase in mitochondrial hexokinase-II was demonstrated. We generated PHLPP-1 knockout (KO) mice and demonstrate that AMVMs isolated from KO mice show potentiated p-Akt at Ser473 in response to agonists. When isolated perfused hearts are subjected to ischemia/reperfusion, p-Akt in whole-heart homogenates and in the mitochondrial fraction is significantly increased. Additionally in PHLPP-1 KO hearts, the increase in p-Akt elicited by ischemia/reperfusion is potentiated and, concomitantly, infarct size is significantly reduced.


These results implicate PHLPP-1 as an endogenous negative regulator of Akt activity and cell survival in the heart.

  H Daiko , K Nagai , J Yoshida , M Nishimura , T Hishida , M Ebihara , M Miyazaki , T Shinozaki , S Miyamoto , M Sakuraba , M Saikawa and R. Hayashi

The purpose of this study was to determine the role of surgical treatment and to identify factors affecting the survival of patients undergoing pulmonary resection for tumors metastatic from head and neck carcinomas.


Thirty-three patients who had undergone resection of pulmonary tumors metastatic from head and neck carcinomas, other than thyroid cancers and sarcomas of the head and neck, were reviewed.


The operative morbidity rate was only 6%, no patients died within 30 days after resection and complete resection was achieved in 94% of patients. The overall 1- and 3-year survival rates were 76% and 43%, respectively, and the median survival time was 21 months. The factors found on univariate analysis to significantly affect survival were a disease-free interval of ≤2 years, tongue carcinoma and squamous cell carcinoma. The factor found, on multivariate analysis, to most strongly affect survival was tongue carcinoma. The most frequent pattern of initial recurrence after pulmonary resection was distant metastasis (64%).


The safety and effectiveness of surgical treatment for pulmonary tumors metastatic from head and neck carcinomas in adaptive criteria for resection are well demonstrated. The poor survival after surgical resection of pulmonary tumors metastatic from cancers of the tongue should be noted.

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