Publication:
Calpain 1 and -2 play opposite roles in cord formation of lymphatic endothelial cells via eNOS regulation

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0

Issued Date

2012

Resource Type

Article

File Type

application/pdf

ISSN

9147470

DOI

10.1007/s13577-012-0042-7

Other identifier(s)

2-s2.0-84862150972

Rights Holder(s)

Scopus

Bibliographic Citation

Human Cell. Vol 25, No.2 (2012), p.36-44

Suggested Citation

Prangsaengtong O., Senda K., Doki Y., Park J.Y., Jo M., Sakurai H., Shibahara N., Saiki I., Koizumi K. Calpain 1 and -2 play opposite roles in cord formation of lymphatic endothelial cells via eNOS regulation. Human Cell. Vol 25, No.2 (2012), p.36-44. doi:10.1007/s13577-012-0042-7 Retrieved from: https://hdl.handle.net/20.500.14740/7047

Title

Calpain 1 and -2 play opposite roles in cord formation of lymphatic endothelial cells via eNOS regulation

Author(s)

Prangsaengtong O.
 Senda K.
 Doki Y.
 Park J.Y.
 Jo M.
 Sakurai H.
 Shibahara N.
 Saiki I.
 Koizumi K.

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.

Subject(s)

Calpain 1
 Calpain 2
 Endothelial nitric oxide synthase
 Heat shock protein 90
 Matrigel
 Small interfering RNA
 Article
 Cell adhesion
 Cell function
 Cell migration
 Controlled study
 Endothelium cell
 Gene silencing
 Genetic transfection
 Human
 Human cell
 Immunoprecipitation
 Lymphangiogenesis
 Microvascular endothelial cell
 Priority journal
 Protein degradation
 Protein phosphorylation
 Western blotting
 Adult
 Calpain
 Cell Adhesion
 Cell Movement
 Cells, Cultured
 Collagen
 Drug Combinations
 Endothelial Cells
 Female
 HSP90 Heat-Shock Proteins
 Humans
 Isoenzymes
 Laminin
 Lymphangiogenesis
 Nitric Oxide Synthase Type III
 Phosphorylation
 Proteoglycans

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URI

https://hdl.handle.net/20.500.14740/7047

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Scopus: Year 1983-2021

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