Please use this identifier to cite or link to this item:
Title: Calpain 1 and -2 play opposite roles in cord formation of lymphatic endothelial cells via eNOS regulation
Authors: Prangsaengtong O.
Senda K.
Doki Y.
Park J.Y.
Jo M.
Sakurai H.
Shibahara N.
Saiki I.
Koizumi K.
Keywords: calpain 1
calpain 2
endothelial nitric oxide synthase
heat shock protein 90
small interfering RNA
cell adhesion
cell function
cell migration
controlled study
endothelium cell
gene silencing
genetic transfection
human cell
microvascular endothelial cell
priority journal
protein degradation
protein phosphorylation
Western blotting
Cell Adhesion
Cell Movement
Cells, Cultured
Drug Combinations
Endothelial Cells
HSP90 Heat-Shock Proteins
Nitric Oxide Synthase Type III
Issue Date: 2012
Abstract: Calpains are a family of calcium-dependent proteases. Two isoforms, calpain 1 and 2, have been implicated in angiogenesis and endothelial cell adhesion and migration. Calpains regulate the function of eNOS; however, the relation of calpains and eNOS to lymphangiogenesis is still unclear. In the present study, we evaluated the role of calpain and eNOS in the formation of cords by lymphatic endothelial cells on Matrigel. Human lymphatic microvascular dermal-derived endothelial cells were transfected with siRNA against calpain 1 or 2. Calpain 2 knockdown, but not calpain 1 knockdown, significantly reduced cord formation, adhesion, and migration on Matrigel. These decreases correlated with a reduction in eNOS, and phosphorylated eNOS and Hsp90 levels, as assayed by immunoprecipitation and western blotting. In contrast, the knockdown of calpain 1, but not calpain 2, increased cell adhesion, enhanced migration, and stabilized late-stage cord formation by increasing cord length compared to the control. These differences correlated with an increase in the level of phosphorylated eNOS. The results indicated that the functions of calpains and eNOS are important for cord formation by lymphatic endothelial cells. For the first time, we have found different functions of calpain 1 and 2. Calpain 1 is involved in the degradation of eNOS and Hsp90 and the phosphorylation of eNOS, while calpain 2 regulates eNOS phosphorylation during cord formation by lymphatic endothelial cells on Matrigel. © 2012 Japan Human Cell Society and Springer.
ISSN: 9147470
Appears in Collections:Scopus 1983-2021

Files in This Item:
There are no files associated with this item.

Items in SWU repository are protected by copyright, with all rights reserved, unless otherwise indicated.