CendR

From Wikipedia, the free encyclopedia

CendR is a protein motif that regulates vascular permeability. The mechanism is activated through neuropilin-1 receptor, which mediates a , dubbed the C-end Rule, or CendR pathway.[1]

Mechanism of action[]

A protease cleavage event - normally through furin type proteases - reveals the c-terminal CendR motif (R/KXXR/K), able to bind to neuropilin-1, leading to an increased permeability in vasculature and other tissues. This is at least partly mediated by an endocytotic/exocytotic transport pathway.[2]

Clinical significance[]

The CendR pathway can be used for an enhanced transport of coupled and coadministered anti-cancer drugs into tumors. Several solid tumors are difficult to access due to a thick fibrotic stroma. Peptides that are based on iRGD are utilized to make such tumors temporarily more accessible to circulating anti-cancer drugs. Several viruses are also using the CendR system activated by , and it is known that viruses that have the system are more virulent and deadly.[3]

References[]

  1. ^ Ruoslahti E (February 2017). "Tumor penetrating peptides for improved drug delivery". Advanced Drug Delivery Reviews. 110–111 (Supplement C): 3–12. doi:10.1016/j.addr.2016.03.008. PMC 5045823. PMID 27040947.
  2. ^ Teesalu T, Sugahara KN, Kotamraju VR, Ruoslahti E (September 2009). "C-end rule peptides mediate neuropilin-1-dependent cell, vascular, and tissue penetration". Proceedings of the National Academy of Sciences of the United States of America. 106 (38): 16157–62. doi:10.1073/pnas.0908201106. PMC 2752543. PMID 19805273.
  3. ^ Balistreri G, Yamauchi Y, Teesalu T (November 2021). "A widespread viral entry mechanism: The C-end Rule motif–neuropilin receptor interaction". Proceedings of the National Academy of Sciences of the United States of America. 118 (49): e2112457118. doi:10.1073/pnas.2112457118. PMID 34772761.
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