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Testosterone can affect cardiovascular disease, but its effects on mitochondrial dynamics in the post-infarct myocardium remain unclear. To observe the effects of testosterone replacement, a rat model of castration-myocardial infarction (MI) was established by ligating the left anterior descending coronary artery 2 weeks after castration with or without testosterone treatment. Expression of mitochondrial fission and fusion proteins was detected by western blot and immunofluorescence 14 days after MI. Cardiac function, myocardial inflammatory infiltration and fibrosis, cardiomyocyte apoptosis, mitochondrial microstructure, and ATP levels were also assessed. Compared with MI rats, castrated rats showed aggravated mitochondrial and myocardial insults, including mitochondrial swelling and disordered arrangement; loss of cristae, reduced mitochondrial length; decreased ATP levels; cardiomyocyte apoptosis; and impaired cardiac function. Results of western blotting analyses indicated that castration downregulated peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC1A) and mitofusin 2, but upregulated dynamin-related protein 1. The results were also supported by results obtained using immunofluorescence. However, these detrimental effects were reversed by testosterone supplementation, which also elevated the upstream AMP-activated protein kinase (AMPK) activation of PGC1A. Thus, testosterone can protect mitochondria in the post-infarct myocardium, partly via the AMPK–PGC1A pathway, thereby decreasing mitochondrial dysfunction and cardiomyocyte apoptosis. The effects of testosterone were confirmed by the results of ELISA analyses.
Search for other papers by Wanbao Yang in
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Glucagon promotes hepatic glucose production maintaining glucose homeostasis in the fasting state. Glucagon maintains at high level in both diabetic animals and human, contributing to hyperglycemia. Mitochondria, a major place for glucose oxidation, are dysfunctional in diabetic condition. However, whether hepatic mitochondrial function can be affected by glucagon remains unknown. Recently, we reported that FOXO1 is an important mediator in glucagon signaling in control of glucose homeostasis. In this study, we further assessed the role of FOXO1 in the action of glucagon in the regulation of hepatic mitochondrial function. We found that glucagon decreased the heme production in a FOXO1-dependent manner, suppressed heme-dependent complex III (UQCRC1) and complex IV (MT-CO1) and inhibited hepatic mitochondrial function. However, the suppression of mitochondrial function by glucagon was largely rescued by deleting the Foxo1 gene in hepatocytes. Glucagon tends to reduce hepatic mitochondrial biogenesis by attenuating the expression of NRF1, TFAM and MFN2, which is mediated by FOXO1. In db/db mice, we found that hepatic mitochondrial function was suppressed and expression levels of UQCRC1, MT-CO1, NRF1 and TFAM were downregulated in the liver. These findings suggest that hepatic mitochondrial function can be impaired when hyperglucagonemia occurs in the patients with diabetes mellitus, resulting in organ failure.
Department of Immunology, School of Medicine, Shandong University, Jinan, Shandong 250012, People’s Republic of China
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Department of Immunology, School of Medicine, Shandong University, Jinan, Shandong 250012, People’s Republic of China
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Department of Immunology, School of Medicine, Shandong University, Jinan, Shandong 250012, People’s Republic of China
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Department of Immunology, School of Medicine, Shandong University, Jinan, Shandong 250012, People’s Republic of China
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Department of Immunology, School of Medicine, Shandong University, Jinan, Shandong 250012, People’s Republic of China
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Department of Immunology, School of Medicine, Shandong University, Jinan, Shandong 250012, People’s Republic of China
Search for other papers by Yun Zhang in
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Department of Immunology, School of Medicine, Shandong University, Jinan, Shandong 250012, People’s Republic of China
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In this study, we investigated the in vivo role of adiponectin, an adipocytokine, on the development of atherosclerosis in rabbits mainly using adenovirus expressing adiponectin gene (Ad-APN) and intravascular ultrasonography. Serum adiponectin concentrations in rabbits after Ad-APN local transfer to abdominal aortas increased about nine times as much as those before transfer (P < 0.01), about ten times as much as the levels of endogenous adiponectin in adenovirus expressing β-galactosidase gene (Ad-β gal) treated rabbits (P < 0.01), and about four times as much as those in the aorta of non-injured rabbits on a normal cholesterol diet (P < 0.01). Ultrasonography revealed a significantly reduced atherosclerotic plaque area in abdominal aortas of rabbits infected through intima with Ad-APN, by 35.2% compared with the area before treatment (P < 0.01), and by 35.8% compared with that in Ad-β gal-treated rabbits (P < 0.01). In rabbits infected through adventitia, Ad-APN treatment reduced plaque area by 28.9% as compared with the area before treatment (P < 0.01) and 25.6% compared with that in Ad-β gal-treated rabbits (P < 0.01). Adiponectin significantly suppressed the mRNA expression of vascular cell adhesion molecule-1 (VCAM-1) by 18.5% through intima transfer (P < 0.05) and 26.9% through adventitia transfer (P < 0.01), and intercellular adhesion molecule-1 (ICAM-1) by 40.7% through intima transfer (P < 0.01), and 30.7% through adventitia transfer (P < 0.01). However, adiponectin had no effect on the expression of types I and III collagen. These results suggest that local adiponectin treatment suppresses the development of atherosclerosis in vivo in part by attenuating the expression of VCAM-1 and ICAM-1 in vascular walls.
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Cysteamine (an aminothiol), which is derived from coenzyme A degradation and metabolized into taurine, has beneficial effects against cystinosis and neurodegenerative diseases; however, its role in diabetic complications is unknown. Thus, we sought to determine the preventive effect of cysteamine against hyperglycemia-induced vascular leakage in the retinas of diabetic mice. Cysteamine and ethanolamine, the sulfhydryl group-free cysteamine analogue, inhibited vascular endothelial growth factor (VEGF)-induced stress fiber formation and vascular endothelial (VE)-cadherin disruption in endothelial cells, which play a critical role in modulating endothelial permeability. Intravitreal injection of the amine compounds prevented hyperglycemia-induced vascular leakage in the retinas of streptozotocin-induced diabetic mice. We then investigated the potential roles of reactive oxygen species (ROS) and transglutaminase (TGase) in the cysteamine prevention of VEGF-induced vascular leakage. Cysteamine, but not ethanolamine, inhibited VEGF-induced ROS generation in endothelial cells and diabetic retinas. In contrast, VEGF-induced TGase activation was prevented by both cysteamine and ethanolamine. Our findings suggest that cysteamine protects against vascular leakage through inhibiting VEGF-induced TGase activation rather than ROS generation in diabetic retinas.
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C-peptide exerts protective effects against diabetic complications; however, its role in inhibiting hyperglycemic memory (HGM) has not been elucidated. We investigated the beneficial effect of C-peptide on HGM-induced vascular damage in vitro and in vivo using human umbilical vein endothelial cells and diabetic mice. HGM induced apoptosis by persistent generation of intracellular ROS and sustained formation of ONOO− and nitrotyrosine. These HGM-induced intracellular events were normalized by treatment with C-peptide, but not insulin, in endothelial cells. C-peptide also inhibited persistent upregulation of p53 and activation of mitochondrial adaptor p66shc after glucose normalization. Further, C-peptide replacement therapy prevented persistent generation of ROS and ONOO− in the aorta of diabetic mice whose glucose levels were normalized by the administration of insulin. C-peptide, but not insulin, also prevented HGM-induced endothelial apoptosis in the murine diabetic aorta. This study highlights a promising role for C-peptide in preventing HGM-induced intracellular events and diabetic vascular damage.
State Key Laboratory of Stem Cell and Reproductive Biology, Institute of Zoology, Chinese Academy of Sciences, Beijing, China
Institute of Reproductive Sciences, Key Laboratory of Animal Reproduction and Germplasm Enhancement in Universities of Shandong, College of Animal Science and Technology, Qingdao Agricultural University, Qingdao, China
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Institute of Reproductive Sciences, Key Laboratory of Animal Reproduction and Germplasm Enhancement in Universities of Shandong, College of Animal Science and Technology, Qingdao Agricultural University, Qingdao, China
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State Key Laboratory of Stem Cell and Reproductive Biology, Institute of Zoology, Chinese Academy of Sciences, Beijing, China
Institute of Reproductive Sciences, Key Laboratory of Animal Reproduction and Germplasm Enhancement in Universities of Shandong, College of Animal Science and Technology, Qingdao Agricultural University, Qingdao, China
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State Key Laboratory of Stem Cell and Reproductive Biology, Institute of Zoology, Chinese Academy of Sciences, Beijing, China
Institute of Reproductive Sciences, Key Laboratory of Animal Reproduction and Germplasm Enhancement in Universities of Shandong, College of Animal Science and Technology, Qingdao Agricultural University, Qingdao, China
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As a fat storage organ, adipose tissue is distributed widely all over the body and is important for energy supply, body temperature maintenance, organ protection, immune regulation and so on. In humans, both underweight and overweight women find it hard to become pregnant, which suggests that appropriate fat storage can guarantee the female reproductive capacity. In fact, a large mass of adipose tissue distributes around the reproductive system both in the male and female. However, the functions of ovary fat pad (the nearest adipose tissue to ovary) are not known. In our study, we found that the ovary fat pad-removed female mice showed decreased fertility and less ovulated mature eggs. We further identified that only a small proportion of follicles developed to antral follicle, and many follicles were blocked at the secondary follicle stage. The overall secretion levels of estrogen and FSH were lower in the whole estrus cycle (especially at proestrus); however, the LH level was higher in ovary fat pad-removed mice than that in control groups. Moreover, the estrus cycle of ovary fat pad-removed mice showed significant disorder. Besides, the expression of FSH receptor decreased, but the LH receptor increased in ovary fat pad-removed mice. These results suggest that ovary fat pad is important for mouse reproduction.
Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, Massachusetts, USA
St Francis Hospital and Medical Center, Hartford, Connecticut, USA
Yale University School of Medicine, New Haven, Connecticut, USA
Mattel Hospital for Children, Los Angeles California, USA
The Department of Animal Science, Cornell University, Ithaca, New York, USA
The Jackson Laboratory, Bar Harbor, Maine, USA
Maine Center for Osteoporosis Research and Education, St Joseph Hospital, Maine, USA
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Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, Massachusetts, USA
St Francis Hospital and Medical Center, Hartford, Connecticut, USA
Yale University School of Medicine, New Haven, Connecticut, USA
Mattel Hospital for Children, Los Angeles California, USA
The Department of Animal Science, Cornell University, Ithaca, New York, USA
The Jackson Laboratory, Bar Harbor, Maine, USA
Maine Center for Osteoporosis Research and Education, St Joseph Hospital, Maine, USA
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Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, Massachusetts, USA
St Francis Hospital and Medical Center, Hartford, Connecticut, USA
Yale University School of Medicine, New Haven, Connecticut, USA
Mattel Hospital for Children, Los Angeles California, USA
The Department of Animal Science, Cornell University, Ithaca, New York, USA
The Jackson Laboratory, Bar Harbor, Maine, USA
Maine Center for Osteoporosis Research and Education, St Joseph Hospital, Maine, USA
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Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, Massachusetts, USA
St Francis Hospital and Medical Center, Hartford, Connecticut, USA
Yale University School of Medicine, New Haven, Connecticut, USA
Mattel Hospital for Children, Los Angeles California, USA
The Department of Animal Science, Cornell University, Ithaca, New York, USA
The Jackson Laboratory, Bar Harbor, Maine, USA
Maine Center for Osteoporosis Research and Education, St Joseph Hospital, Maine, USA
Search for other papers by Hui Sun in
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Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, Massachusetts, USA
St Francis Hospital and Medical Center, Hartford, Connecticut, USA
Yale University School of Medicine, New Haven, Connecticut, USA
Mattel Hospital for Children, Los Angeles California, USA
The Department of Animal Science, Cornell University, Ithaca, New York, USA
The Jackson Laboratory, Bar Harbor, Maine, USA
Maine Center for Osteoporosis Research and Education, St Joseph Hospital, Maine, USA
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Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, Massachusetts, USA
St Francis Hospital and Medical Center, Hartford, Connecticut, USA
Yale University School of Medicine, New Haven, Connecticut, USA
Mattel Hospital for Children, Los Angeles California, USA
The Department of Animal Science, Cornell University, Ithaca, New York, USA
The Jackson Laboratory, Bar Harbor, Maine, USA
Maine Center for Osteoporosis Research and Education, St Joseph Hospital, Maine, USA
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Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, Massachusetts, USA
St Francis Hospital and Medical Center, Hartford, Connecticut, USA
Yale University School of Medicine, New Haven, Connecticut, USA
Mattel Hospital for Children, Los Angeles California, USA
The Department of Animal Science, Cornell University, Ithaca, New York, USA
The Jackson Laboratory, Bar Harbor, Maine, USA
Maine Center for Osteoporosis Research and Education, St Joseph Hospital, Maine, USA
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Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, Massachusetts, USA
St Francis Hospital and Medical Center, Hartford, Connecticut, USA
Yale University School of Medicine, New Haven, Connecticut, USA
Mattel Hospital for Children, Los Angeles California, USA
The Department of Animal Science, Cornell University, Ithaca, New York, USA
The Jackson Laboratory, Bar Harbor, Maine, USA
Maine Center for Osteoporosis Research and Education, St Joseph Hospital, Maine, USA
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Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, Massachusetts, USA
St Francis Hospital and Medical Center, Hartford, Connecticut, USA
Yale University School of Medicine, New Haven, Connecticut, USA
Mattel Hospital for Children, Los Angeles California, USA
The Department of Animal Science, Cornell University, Ithaca, New York, USA
The Jackson Laboratory, Bar Harbor, Maine, USA
Maine Center for Osteoporosis Research and Education, St Joseph Hospital, Maine, USA
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Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, Massachusetts, USA
St Francis Hospital and Medical Center, Hartford, Connecticut, USA
Yale University School of Medicine, New Haven, Connecticut, USA
Mattel Hospital for Children, Los Angeles California, USA
The Department of Animal Science, Cornell University, Ithaca, New York, USA
The Jackson Laboratory, Bar Harbor, Maine, USA
Maine Center for Osteoporosis Research and Education, St Joseph Hospital, Maine, USA
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Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, Massachusetts, USA
St Francis Hospital and Medical Center, Hartford, Connecticut, USA
Yale University School of Medicine, New Haven, Connecticut, USA
Mattel Hospital for Children, Los Angeles California, USA
The Department of Animal Science, Cornell University, Ithaca, New York, USA
The Jackson Laboratory, Bar Harbor, Maine, USA
Maine Center for Osteoporosis Research and Education, St Joseph Hospital, Maine, USA
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The role of circulating IGF-I in skeletal acquisition and the anabolic response to PTH is not well understood. We generated IGF-I-deficient mice by gene deletions of IGF ternary complex components including: (1) liver-specific deletion of the IGF-I gene (LID), (2) global deletion of the acid-labile (ALS) gene (ALSKO), and (3) both liver IGF-I and ALS inactivated genes (LA). Twelve-week-old male control (CTL), LID, ALSKO, and LA mice were treated with vehicle (VEH) or human PTH(1–34) for 4 weeks. VEH-treated IGF-I-deficient mice (i.e. LID, ALSKO and LA mice) exhibited reduced cortical cross-sectional area (P = 0.001) compared with CTL mice; in contrast, femoral trabecular bone volume fractions (BV/TV) of the IGF-I-deficient mice were consistently greater than CTL (P<0.01). ALSKO mice exhibited markedly reduced osteoblast number and surface (P<0.05), as well as mineral apposition rate compared with other IGF-I-deficient and CTL mice. Adherent bone marrow stromal cells, cultured in β-glycerol phosphate and ascorbic acid, showed no strain differences in secreted IGF-I. In response to PTH, there were both compartment- and strain-specific effects. Cortical bone area was increased by PTH in CTL and ALSKO mice, but not in LID or LA mice. In the trabecular compartment, PTH increased femoral and vertebral BV/TV in LID, but not in ALSKO or LA mice. In conclusion, we demonstrated that the presentation of IGF-I as a circulating complex is essential for skeletal remodeling and the anabolic response to PTH. We postulate that the ternary complex itself, rather than IGF-I alone, influences bone acquisition in a compartment-specific manner (i.e. cortical vs trabecular bone).
