Role of MARCKS in regulating endothelial cell proliferation

American Journal of Physiology - Cell Physiology

Volumn 279, Issue 5 48-5, 2000, Pages

  Zhao, Ying ^a   Neltner, Bonnie S ^a   Davis, Harold W ^a  

^a UNIVERSITY OF CINCINNATI MEDICAL CENTER   (United States)

Author keywords

Actin; Myosin light chain phosphorylation; Myristoylated alanine rich C kinase substrate; Vascular endothelial growth factor

Indexed keywords

CALMODULIN; F ACTIN; MARCKS PROTEIN; MYOSIN LIGHT CHAIN; PROTEIN KINASE C; VASCULOTROPIN;

ACTIN POLYMERIZATION; ARTICLE; CELL PROLIFERATION; CONTROLLED STUDY; ENDOTHELIUM CELL; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN PHOSPHORYLATION; SIGNAL TRANSDUCTION; VASCULAR ENDOTHELIUM;

BOVINAE;

EID: 0033680983     PISSN: 03636143     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpcell.2000.279.5.c1611     Document Type: Article

References (49)

1. Calmodulin-binding proteins in the nuclei of quiescent and proliferatively activated rat liver cells
2. The MARCKS family of cellular protein kinase C substrates
3. Unpolymerized actin in fibroblasts and brain
4. The role of 80K/MARCKS, a specific substrate of protein kinase C, in cell growth and tumor progression
5. MARCKS functions as a novel growth suppressor in cells of melanocyte origin
6. The expression of 80K/MARCKS, a major substrate of protein kinase C, is down-regulated through both PKC-dependent and -independent pathways
7. Dissociation of phosphorylation and translocation of a myristoylated protein kinase C substrate (MARCKS protein) in C6 glioma and N1E- 115 neuroblastoma cells
8. 2+ regulation
9. Myosin phosphorylation/dephosphorylation and regulation of airway smooth muscle contractility
10. Phosphorylation of the MARCKS protein, a major protein kinase C substrate, is not an obligatory step in the mitogenic signaling pathway of basic fibroblast growth factor in rat oligodendrocytes
11. VEGF stimulates MAPK through a pathway that is unique for receptor tyrosine kinases
12. Vascular endothelial growth factor
13. Angiogenesis
14. Regulation of endothelial cell gap formation and barrier dysfunction: Role of myosin light chain phosphorylation
15. Phosphorylation-regulated calmodulin binding to a prominent cellular substrate for protein kinase C
16. MARCKS is an actin filament crosslinking protein regulated by protein kinase C and calcium-calmodulin
17. Overexpression of the myristoylated alanine-rich C kinase substrate in Rat 1 cells increases sensitivity to calmodulin antagonists
18. 0
19. Control of capillary growth and differentiation by extracellular matrix: Use of a tensegrity (tensional integrity) mechanism for signal processing
20. Changes in the cytoskeletal structure of human platelets following thrombin activation
21. MARCKS protein is transcriptionally down-regulated in v-Sir-transformed BALB/c3T3 cells
22. Cleavage of structural proteins during the assembly of the head of bacteriophage T4
23. Regulation of the cell cycle by calcium and calmodulin
24. Overepression of the myristoylated alanine-rich C kinase substrate in human choroidal melanoma cells affects cell proliferation
25. Specific proteolytic cleavage of the myristoylated alanine-rich C kinase substrate between Asn 147 and Glu 148 also occurs in brain
26. Phosphorylation-dependent binding of a synthetic MARCKS peptide to calmodulin
27. p42/p44 MAP kinase module plays a key role in the transcriptional regulation of the vascular endothelial growth factor gene in fibroblasts
28. Decreased expression of the myristoylated alanine-rich C kinase substrate in transformed BALB/c3T3 mouse fibroblasts
29. Different phosphorylated forms of myosin in contracting tracheal smooth muscle
30. Transformed 3T3 cells have reduced levels and altered subcellular distribution of the major PKC substrate protein MARCKS
31. p42 MAPK phosphorylates 80 kDa MARCKS at Ser-113
32. Vascular endothelial growth factor governs endothelial nitric-oxide synthase expression via a KDR/Flk- 1 receptor and a protein kinase C signaling pathway
33. Protein kinase C-mediated phosphorylation of the myristoylated alanine-rich C-kinase substrate protects it from specific proteolytic cleavage
34. Evidence for the role of protein kinase C in astrocyte-induced proliferation of rat cerebromicrovascular endothelial cells
35. Protein kinase C phosphorylates caldesmon and vimentin and enhances albumin permeability across cultured bovine pulmonary artery endothelial cell monolayers
36. MARCKS deficiency in mice leads to abnormal brain development and perinatal death
37. Atherosclerosis and angiogenesis
38. Membrane association of the myristoylated alanine-rich C kinase substrate (MARCKS) protein. Mutational analysis provides evidence for complex interactions
39. VEGF activates protein kinase C-dependent, but Ras-independent Raf-MEKMAP kinase pathway for DNA synthesis in primary endothelial cells
40. Myristoylated alanine-rich C kinase substrate (MAECKS), a major protein kinase C substrate, is an in vivo substrate of proline-directed protein kinases
41. Regulation by phosphorylation of reversible association of a myristoylated protein kinase C substrate with the plasma membrane
42. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
43. Protein kinase C involvement in the regulation of angiogenesis
44. Density dependent change of myristoylated proteins in C3H10T1/ 2 fibroblasts and their transformants
45. Severely decreased MARCKS expression correlates with ras reversion but not with mitogenic responsiveness
46. Elevated levels of diacylglycerol and decreased phorbol ester sensitivity in ras-transformed fibroblasts
47. Phosphorylation of myristoylated alanine-rich C kinase substrate (MARCKS) by proline-directed protein kinases and its dephosphorylation
48. Protein kinase C lies on the signaling pathway for vascular endothelial growth factor-mediated tumor development and angiogenesis
49. Thrombin-induced phosphorylation of the myristoylated alanine-rich C kinase substrate (MARCKS) protein in bovine pulmonary artery endothelial cells