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Gas6 and protein S. Vitamin K-dependent ligands for the Axl receptor tyrosine kinase subfamily.

Hafizi, Sassan LU and Dahlbäck, Björn LU (2006) In The FEBS Journal 273(23). p.5231-5244
Abstract
Gas6 and protein S are two homologous secreted proteins that depend on vitamin K for their execution of a range of biological functions. A discrete subset of these functions is mediated through their binding to and activation of the receptor tyrosine kinases Axl, Sky and Mer. Furthermore, a hallmark of the Gas6-Axl system is the unique ability of Gas6 and protein S to tether their non receptor-binding regions to the negatively charged membranes of apoptotic cells. Numerous studies have shown the Gas6-Axl system to regulate cell survival, proliferation, migration, adhesion and phagocytosis. Consequently, altered activity/expression of its components has been detected in a variety of pathologies such as cancer and vascular, autoimmune and... (More)
Gas6 and protein S are two homologous secreted proteins that depend on vitamin K for their execution of a range of biological functions. A discrete subset of these functions is mediated through their binding to and activation of the receptor tyrosine kinases Axl, Sky and Mer. Furthermore, a hallmark of the Gas6-Axl system is the unique ability of Gas6 and protein S to tether their non receptor-binding regions to the negatively charged membranes of apoptotic cells. Numerous studies have shown the Gas6-Axl system to regulate cell survival, proliferation, migration, adhesion and phagocytosis. Consequently, altered activity/expression of its components has been detected in a variety of pathologies such as cancer and vascular, autoimmune and kidney disorders. Moreover, Axl overactivation can equally occur without ligand binding, which has implications for tumorigenesis. Further knowledge of this exquisite ligand-receptor system and the circumstances of its activation should provide the basis for development of novel therapies for the above diseases. (Less)
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author
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organization
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type
Contribution to journal
publication status
published
subject
keywords
receptor tyrosine kinase, vitamin K, Axl, apoptosis, phagocytosis, cell adhesion
in
The FEBS Journal
volume
273
issue
23
pages
5231 - 5244
publisher
Wiley-Blackwell
external identifiers
  • wos:000242112100001
  • scopus:33751079330
ISSN
1742-464X
DOI
10.1111/j.1742-4658.2006.05529.x
language
English
LU publication?
yes
id
9f91d392-4a49-4d45-a4a7-f242e5874a1f (old id 162158)
alternative location
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=17064312&dopt=Abstract
date added to LUP
2016-04-01 16:55:11
date last changed
2021-08-18 04:48:03
@article{9f91d392-4a49-4d45-a4a7-f242e5874a1f,
  abstract     = {Gas6 and protein S are two homologous secreted proteins that depend on vitamin K for their execution of a range of biological functions. A discrete subset of these functions is mediated through their binding to and activation of the receptor tyrosine kinases Axl, Sky and Mer. Furthermore, a hallmark of the Gas6-Axl system is the unique ability of Gas6 and protein S to tether their non receptor-binding regions to the negatively charged membranes of apoptotic cells. Numerous studies have shown the Gas6-Axl system to regulate cell survival, proliferation, migration, adhesion and phagocytosis. Consequently, altered activity/expression of its components has been detected in a variety of pathologies such as cancer and vascular, autoimmune and kidney disorders. Moreover, Axl overactivation can equally occur without ligand binding, which has implications for tumorigenesis. Further knowledge of this exquisite ligand-receptor system and the circumstances of its activation should provide the basis for development of novel therapies for the above diseases.},
  author       = {Hafizi, Sassan and Dahlbäck, Björn},
  issn         = {1742-464X},
  language     = {eng},
  number       = {23},
  pages        = {5231--5244},
  publisher    = {Wiley-Blackwell},
  series       = {The FEBS Journal},
  title        = {Gas6 and protein S. Vitamin K-dependent ligands for the Axl receptor tyrosine kinase subfamily.},
  url          = {https://lup.lub.lu.se/search/ws/files/4819250/625695.pdf},
  doi          = {10.1111/j.1742-4658.2006.05529.x},
  volume       = {273},
  year         = {2006},
}