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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Ko, Soyoung Shi, Liheng Kim, Andy Jeesu Ko, Gladys Y-p Ko, Michael L. |
| Description | Author Affiliation: Shi L ( Department of Veterinary Integrative Biosciences, College of Veterinary Medicine and Biomedical Sciences, Texas A&M University, College Station, TX 77843-4458, USA.); Ko S ( Department of Medicine, Baylor College of Medicine, Houston, TX 77030, USA.); Ko ML ( Department of Veterinary Integrative Biosciences, College of Veterinary Medicine and Biomedical Sciences, Texas A&M University, College Station, TX 77843-4458, USA.); Kim AJ ( Department of Veterinary Integrative Biosciences, College of Veterinary Medicine and Biomedical Sciences, Texas A&M University, College Station, TX 77843-4458, USA.); Ko GY ( Department of Veterinary Integrative Biosciences, College of Veterinary Medicine and Biomedical Sciences, Texas A&M University, College Station, TX 77843-4458, USA) |
| Abstract | We previously identified peptide Lv, a novel bioactive peptide that enhances the activity of L-type voltage-gated calcium channels (L-VGCCs) in cone photoreceptors. In this study, we verified that peptide Lv was able to augment L-VGCC currents in cardiomyocytes, as well as promote proliferation of endothelial cells. We used a proteomics approach to determine the specific receptors and binding partners of peptide Lv and found that vascular endothelial growth factor receptor 2 (VEGFR2) interacted with peptide Lv. Peptide Lv treatment in embryonic cardiomyocytes stimulated tyrosine autophosphorylation of VEGFR2 and activated its downstream signaling. Peptide Lv activity was blocked by DMH4, a VEGFR2 specific blocker, but not by SCH202676, an allosteric inhibitor of G protein-coupled receptors, suggesting that the activity of peptide Lv was mediated through VEGFR2 signaling. Inhibition of VEGFR tyrosine kinase or its downstream signaling molecules abolished the augmentation of L-VGCCs elicited by peptide Lv in cardiomyocytes. In addition, peptide Lv promoted cell proliferation of cultured human endothelial cells. Calcium entry through L-VGCCs is essential for excitation-contraction coupling in cardiomyocytes. Since peptide Lv was able to augment L-VGCCs through activation of VEGF signaling in cardiomyocytes and promote proliferation of endothelial cells, peptide Lv may play an important role in regulating the cardiovascular system. |
| ISSN | 00063002 |
| Journal | Biochimica et Biophysica Acta (BBA) - Reviews on Cancer |
| Issue Number | 5 |
| Volume Number | 1853 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2015-05-01 |
| Publisher Place | Netherlands |
| Access Restriction | Open |
| Subject Keyword | Calcium Channels, L-Type Metabolism Peptides Pharmacology Signal Transduction Drug Effects Vascular Endothelial Growth Factor Receptor-2 Amino Acid Sequence Animals Cells, Cultured Chick Embryo Human Umbilical Vein Endothelial Cells Mice Molecular Sequence Data Myocytes, Cardiac Chemistry Phosphorylation Phosphotyrosine Protein Binding Protein Structure, Secondary Protein Structure, Tertiary Time Factors Vascular Endothelial Growth Factor A Antagonists & Inhibitors Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Biochemistry |
| Content Type | Text |
| Resource Type | Article |
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