Simpkin, J.C., Yellon, D.M., Davidson, S.M., Lim, S.Y., Wynne, A.M. and Smith, C.C. (2007) Apelin-13 and apelin-36 exhibit direct cardioprotective activity against ischemia-reperfusion injury. Basic Research in Cardiology, 102, 518-528. doi:10.1007/s00395-007-0671-2

has been cited by the following article:

• TITLE: SCNH2 is a novel apelinergic family member acting as a potent mitogenic and chemotactic factor for both endothelial and epithelial cells

  AUTHORS: Changge Fang, Ingalill Avis, Caterina Bianco, Natalie Held, Jennifer Morris, Kris Ylaya, Stephen M. Hewitt, Alfred C. Aplin, Roberto F. Nicosia, Laura A. Fung, John D. Lewis, William G. Stetler-Stevenson, David S. Salomon, Frank Cuttitta

  KEYWORDS: Novel Apelinergic Member; SCNH2; Angiogenesis; Migration; Embryogenesis

  JOURNAL NAME: Open Journal of Clinical Diagnostics, Vol.3 No.2, June 25, 2013

  ABSTRACT: The gut hormone apelin is a major therapeutic focus for several diseases involving inflammation and aberrant cell growth. We investigated whether apelin-36 contained alternative bioactive peptides associated with normal physiology or disease. Amino acid sequence analysis of apelin-36 identified an amidation motif consistent with the formation of a secondary bioactive peptide (SCNH2). SCNH2 is proven to be mitogenic and chemotactic in normal/malignant cells and augments angiogenesis via a PTX-resistant/CT-X-sensitive G protein-coupled receptor (GPCR). Notably, SCNH2 is substantially more potent and sensitive than apelin-13 and vascular endothelial growth factor-A. Endogenous SCNH2 is highly expressed in human tumors and placenta and in mouse embryonic tissues. Our findings demonstrate that SCNH2 is a new apelinergic member with critical pluripotent roles in angiogenesis related diseases and embryogenesis via a non-APJ GPCR.