Abstract
Phosphorylation of proteins on tyrosine acts as a reversible and specific trigger mechanism, forming or disrupting regulatory connections between proteins. Tyrosine kinases and phosphatases participate in multiple cellular processes, and considerable evidence now supports a role for tyrosine phosphorylation in vascular permeability. A semipermeable barrier between the vascular compartment and the interstitium is maintained by the integrity of endothelial monolayer, controlling movement of fluids, macromolecules and leucocytes. Barrier function is regulated by the adjustment of paracellular gaps between endothelial cells (ECs) by two antagonistic forces, centripetal cytoskeletal tension and opposing cell-cell and cell-matrix adhesion forces. Both cytoskeletal filaments and adhesion sites are intimately linked in complex machinery which is regulated by multiple signaling events including protein phosphorylation and/or protein translocation to specific intracellular positions. Tyrosine kinases occupy key positions in the mechanism controlling cell responses mediated through various cell surface receptors, which use tyrosine phosphorylation to transduce extracellular signal.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 201-212 |
| Number of pages | 12 |
| Journal | Vascular Pharmacology |
| Volume | 39 |
| Issue number | 4-5 |
| DOIs | |
| State | Published - Nov 1 2002 |
| Externally published | Yes |
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Keywords
- Cell barrier
- Phosphorylation
- Tyrosine kinase
ASJC Scopus subject areas
- Physiology
- Molecular Medicine
- Pharmacology
Cite this
Role of tyrosine kinase signaling in endothelial cell barrier regulation. / Bogatcheva, Natalia V.; Garcia, Joe G.N.; Verin, Alexander Dmitriyevich.
In: Vascular Pharmacology, Vol. 39, No. 4-5, 01.11.2002, p. 201-212.Research output: Contribution to journal › Review article
}
TY - JOUR
T1 - Role of tyrosine kinase signaling in endothelial cell barrier regulation
AU - Bogatcheva, Natalia V.
AU - Garcia, Joe G.N.
AU - Verin, Alexander Dmitriyevich
PY - 2002/11/1
Y1 - 2002/11/1
N2 - Phosphorylation of proteins on tyrosine acts as a reversible and specific trigger mechanism, forming or disrupting regulatory connections between proteins. Tyrosine kinases and phosphatases participate in multiple cellular processes, and considerable evidence now supports a role for tyrosine phosphorylation in vascular permeability. A semipermeable barrier between the vascular compartment and the interstitium is maintained by the integrity of endothelial monolayer, controlling movement of fluids, macromolecules and leucocytes. Barrier function is regulated by the adjustment of paracellular gaps between endothelial cells (ECs) by two antagonistic forces, centripetal cytoskeletal tension and opposing cell-cell and cell-matrix adhesion forces. Both cytoskeletal filaments and adhesion sites are intimately linked in complex machinery which is regulated by multiple signaling events including protein phosphorylation and/or protein translocation to specific intracellular positions. Tyrosine kinases occupy key positions in the mechanism controlling cell responses mediated through various cell surface receptors, which use tyrosine phosphorylation to transduce extracellular signal.
AB - Phosphorylation of proteins on tyrosine acts as a reversible and specific trigger mechanism, forming or disrupting regulatory connections between proteins. Tyrosine kinases and phosphatases participate in multiple cellular processes, and considerable evidence now supports a role for tyrosine phosphorylation in vascular permeability. A semipermeable barrier between the vascular compartment and the interstitium is maintained by the integrity of endothelial monolayer, controlling movement of fluids, macromolecules and leucocytes. Barrier function is regulated by the adjustment of paracellular gaps between endothelial cells (ECs) by two antagonistic forces, centripetal cytoskeletal tension and opposing cell-cell and cell-matrix adhesion forces. Both cytoskeletal filaments and adhesion sites are intimately linked in complex machinery which is regulated by multiple signaling events including protein phosphorylation and/or protein translocation to specific intracellular positions. Tyrosine kinases occupy key positions in the mechanism controlling cell responses mediated through various cell surface receptors, which use tyrosine phosphorylation to transduce extracellular signal.
KW - Cell barrier
KW - Phosphorylation
KW - Tyrosine kinase
UR - http://www.scopus.com/inward/record.url?scp=0042845701&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0042845701&partnerID=8YFLogxK
U2 - 10.1016/S1537-1891(03)00009-0
DO - 10.1016/S1537-1891(03)00009-0
M3 - Review article
C2 - 12747960
AN - SCOPUS:0042845701
VL - 39
SP - 201
EP - 212
JO - Vascular Pharmacology
JF - Vascular Pharmacology
SN - 1537-1891
IS - 4-5
ER -