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PKN2 deficiency leads both to prenatal 'congenital' cardiomyopathy and defective angiotensin II stress responses.
Marshall, Jacqueline J T; Cull, Joshua J; Alharbi, Hajed O; Zaw Thin, May; Cooper, Susanna T E; Barrington, Christopher; Vanyai, Hannah; Snoeks, Thomas; Siow, Bernard; Suáarez-Bonnet, Alejandro; Herbert, Eleanor; Stuckey, Daniel J; Cameron, Angus J M; Prin, Fabrice; Cook, Andrew C; Priestnall, Simon L; Chotani, Sonia; Rackham, Owen J L; Meijles, Daniel N; Mohun, Tim; Clerk, Angela; Parker, Peter J.
Affiliation
  • Marshall JJT; Protein Phosphorylation Laboratory, Francis Crick Institute, 1 Midland Road, London NW1 1AT, U.K.
  • Cull JJ; School of Biological Sciences, University of Reading, Reading RG6 2AS, U.K.
  • Alharbi HO; School of Biological Sciences, University of Reading, Reading RG6 2AS, U.K.
  • Zaw Thin M; UCL Centre for Advanced Biomedical Imaging, Division of Medicine, University College London, London WC1E 6DD, U.K.
  • Cooper STE; Molecular and Clinical Sciences Institute, St George's University of London, London SW17 0RE, U.K.
  • Barrington C; Bioinformatics and Biostatistics, Francis Crick Institute, 1 Midland Road, London NW1 1AT, U.K.
  • Vanyai H; Epithelial Biology Laboratory, Francis Crick Institute, 1 Midland Road, London London NE1 1AT, U.K.
  • Snoeks T; In Vivo Imaging, Francis Crick Institute, 1 Midland Road, London London NW1 1AT, U.K.
  • Siow B; In Vivo Imaging, Francis Crick Institute, 1 Midland Road, London London NW1 1AT, U.K.
  • Suáarez-Bonnet A; Experimental Histopathology, Francis Crick Institute, 1 Midland Road, London NW1 1AT, U.K.
  • Herbert E; Department of Pathobiology & Population Sciences, The Royal Veterinary College, North Mymms, Hatfield, Hertfordshire AL9 7TA, U.K.
  • Stuckey DJ; Experimental Histopathology, Francis Crick Institute, 1 Midland Road, London NW1 1AT, U.K.
  • Cameron AJM; Department of Pathobiology & Population Sciences, The Royal Veterinary College, North Mymms, Hatfield, Hertfordshire AL9 7TA, U.K.
  • Prin F; UCL Centre for Advanced Biomedical Imaging, Division of Medicine, University College London, London WC1E 6DD, U.K.
  • Cook AC; Kinase Biology Laboratory, John Vane Science Centre, Barts Cancer Institute, Queen Mary University of London, Charterhouse Square, London EC1M 6BQ, U.K.
  • Priestnall SL; Heart Formation in Vertebrates Laboratory, Francis Crick Institute, 1 Midland Road, London NW1 1AT, U.K.
  • Chotani S; Centre for Morphology and Structural Heart Disease, Institute of Institute of Cardiovascular Science, Zayed Centre for Research, 20 Guilford Street, London WC1N 1DZ, U.K.
  • Rackham OJL; Experimental Histopathology, Francis Crick Institute, 1 Midland Road, London NW1 1AT, U.K.
  • Meijles DN; Department of Pathobiology & Population Sciences, The Royal Veterinary College, North Mymms, Hatfield, Hertfordshire AL9 7TA, U.K.
  • Mohun T; Program in Cardiovascular and Metabolic Disorders, Duke-NUS Medical School, Singapore, Singapore.
  • Clerk A; Program in Cardiovascular and Metabolic Disorders, Duke-NUS Medical School, Singapore, Singapore.
  • Parker PJ; Molecular and Clinical Sciences Institute, St George's University of London, London SW17 0RE, U.K.
Biochem J ; 479(13): 1467-1486, 2022 07 15.
Article in En | MEDLINE | ID: mdl-35730579
The protein kinase PKN2 is required for embryonic development and PKN2 knockout mice die as a result of failure in the expansion of mesoderm, cardiac development and neural tube closure. In the adult, cardiomyocyte PKN2 and PKN1 (in combination) are required for cardiac adaptation to pressure-overload. The specific role of PKN2 in contractile cardiomyocytes during development and its role in the adult heart remain to be fully established. We used mice with cardiomyocyte-directed knockout of PKN2 or global PKN2 haploinsufficiency to assess cardiac development and function using high resolution episcopic microscopy, MRI, micro-CT and echocardiography. Biochemical and histological changes were also assessed. Cardiomyocyte-directed PKN2 knockout embryos displayed striking abnormalities in the compact myocardium, with frequent myocardial clefts and diverticula, ventricular septal defects and abnormal heart shape. The sub-Mendelian homozygous knockout survivors developed cardiac failure. RNASeq data showed up-regulation of PKN2 in patients with dilated cardiomyopathy, suggesting an involvement in adult heart disease. Given the rarity of homozygous survivors with cardiomyocyte-specific deletion of PKN2, the requirement for PKN2 in adult mice was explored using the constitutive heterozygous PKN2 knockout. Cardiac hypertrophy resulting from hypertension induced by angiotensin II was reduced in these haploinsufficient PKN2 mice relative to wild-type littermates, with suppression of cardiomyocyte hypertrophy and cardiac fibrosis. It is concluded that cardiomyocyte PKN2 is essential for heart development and the formation of compact myocardium and is also required for cardiac hypertrophy in hypertension. Thus, PKN signalling may offer therapeutic options for managing congenital and adult heart diseases.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Protein Kinase C / Hypertension / Cardiomyopathies Limits: Animals / Pregnancy Language: En Journal: Biochem J Year: 2022 Document type: Article Country of publication: United kingdom

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Protein Kinase C / Hypertension / Cardiomyopathies Limits: Animals / Pregnancy Language: En Journal: Biochem J Year: 2022 Document type: Article Country of publication: United kingdom