Phosphat ÄSE-1 and -2A activity and their regulation on apoptosis in ocular lens system

David W. Li, Uwe Pass, Isham Huizar

Research output: Contribution to journalArticle

Abstract

Protein phosphorylation and dephosphorylation play important roles in regulating cell signalling, proliferation, differentiation and apoptosis. In our previous studies, we have demonstrated that stress-induced lens epithelial cell apoptosis is a very important early event during stressinduced non-congenital cataract formation by various stress factors. In the present study, we have examined the distribution of the activity of protein phosphatase-1 and 2A in human, bovine and rat lenses and their function in regulating cell death in rabbit lens epithelial cells. Our results reveal that majority of the phosphatase activity (both PP-1 and PP-2A) is localized in the epithelial cells of all three different lenses. In the lens fiber cells, only cortex fibers immediately underlying the lens epithelial cell layer have some PP-1 and PP-2A activity. Other fiber sections essentially display no phosphatase activity. In the rabbit lens epithelial cells, inhibition of PP-2A has no effect on cell viability. In contrast, inhibition of PP-1 induces rapid lens epithelial cell apoptosis. This induced cell death is associated with up-regulation of p53 and box and can be inhibited by blocking protein synthesis. Our results suggest that PP-1 is an important signalling component regulating apoptosis in lens system. (Supported by a NIH grant EY 11372 to D. W-C. Li and Research to Prevent Blindness).

Original languageEnglish (US)
Pages (from-to)A1403
JournalFASEB Journal
Volume12
Issue number8
StatePublished - Dec 1 1998

Fingerprint

eye lens
Crystalline Lens
Lens
Lenses
apoptosis
Apoptosis
epithelial cells
Epithelial Cells
phosphoprotein phosphatase
Cell death
Phosphoric Monoester Hydrolases
Fibers
cell death
Cell Death
rabbits
Rabbits
Cell signaling
Protein Phosphatase 1
Protein Phosphatase 2
fiber cells

ASJC Scopus subject areas

  • Biotechnology
  • Biochemistry
  • Molecular Biology
  • Genetics

Cite this

Phosphat ÄSE-1 and -2A activity and their regulation on apoptosis in ocular lens system. / Li, David W.; Pass, Uwe; Huizar, Isham.

In: FASEB Journal, Vol. 12, No. 8, 01.12.1998, p. A1403.

Research output: Contribution to journalArticle

Li, David W. ; Pass, Uwe ; Huizar, Isham. / Phosphat ÄSE-1 and -2A activity and their regulation on apoptosis in ocular lens system. In: FASEB Journal. 1998 ; Vol. 12, No. 8. pp. A1403.
@article{2651be70264f418aa9bc0291970ef37d,
title = "Phosphat {\"A}SE-1 and -2A activity and their regulation on apoptosis in ocular lens system",
abstract = "Protein phosphorylation and dephosphorylation play important roles in regulating cell signalling, proliferation, differentiation and apoptosis. In our previous studies, we have demonstrated that stress-induced lens epithelial cell apoptosis is a very important early event during stressinduced non-congenital cataract formation by various stress factors. In the present study, we have examined the distribution of the activity of protein phosphatase-1 and 2A in human, bovine and rat lenses and their function in regulating cell death in rabbit lens epithelial cells. Our results reveal that majority of the phosphatase activity (both PP-1 and PP-2A) is localized in the epithelial cells of all three different lenses. In the lens fiber cells, only cortex fibers immediately underlying the lens epithelial cell layer have some PP-1 and PP-2A activity. Other fiber sections essentially display no phosphatase activity. In the rabbit lens epithelial cells, inhibition of PP-2A has no effect on cell viability. In contrast, inhibition of PP-1 induces rapid lens epithelial cell apoptosis. This induced cell death is associated with up-regulation of p53 and box and can be inhibited by blocking protein synthesis. Our results suggest that PP-1 is an important signalling component regulating apoptosis in lens system. (Supported by a NIH grant EY 11372 to D. W-C. Li and Research to Prevent Blindness).",
author = "Li, {David W.} and Uwe Pass and Isham Huizar",
year = "1998",
month = "12",
day = "1",
language = "English (US)",
volume = "12",
pages = "A1403",
journal = "FASEB Journal",
issn = "0892-6638",
publisher = "FASEB",
number = "8",

}

TY - JOUR

T1 - Phosphat ÄSE-1 and -2A activity and their regulation on apoptosis in ocular lens system

AU - Li, David W.

AU - Pass, Uwe

AU - Huizar, Isham

PY - 1998/12/1

Y1 - 1998/12/1

N2 - Protein phosphorylation and dephosphorylation play important roles in regulating cell signalling, proliferation, differentiation and apoptosis. In our previous studies, we have demonstrated that stress-induced lens epithelial cell apoptosis is a very important early event during stressinduced non-congenital cataract formation by various stress factors. In the present study, we have examined the distribution of the activity of protein phosphatase-1 and 2A in human, bovine and rat lenses and their function in regulating cell death in rabbit lens epithelial cells. Our results reveal that majority of the phosphatase activity (both PP-1 and PP-2A) is localized in the epithelial cells of all three different lenses. In the lens fiber cells, only cortex fibers immediately underlying the lens epithelial cell layer have some PP-1 and PP-2A activity. Other fiber sections essentially display no phosphatase activity. In the rabbit lens epithelial cells, inhibition of PP-2A has no effect on cell viability. In contrast, inhibition of PP-1 induces rapid lens epithelial cell apoptosis. This induced cell death is associated with up-regulation of p53 and box and can be inhibited by blocking protein synthesis. Our results suggest that PP-1 is an important signalling component regulating apoptosis in lens system. (Supported by a NIH grant EY 11372 to D. W-C. Li and Research to Prevent Blindness).

AB - Protein phosphorylation and dephosphorylation play important roles in regulating cell signalling, proliferation, differentiation and apoptosis. In our previous studies, we have demonstrated that stress-induced lens epithelial cell apoptosis is a very important early event during stressinduced non-congenital cataract formation by various stress factors. In the present study, we have examined the distribution of the activity of protein phosphatase-1 and 2A in human, bovine and rat lenses and their function in regulating cell death in rabbit lens epithelial cells. Our results reveal that majority of the phosphatase activity (both PP-1 and PP-2A) is localized in the epithelial cells of all three different lenses. In the lens fiber cells, only cortex fibers immediately underlying the lens epithelial cell layer have some PP-1 and PP-2A activity. Other fiber sections essentially display no phosphatase activity. In the rabbit lens epithelial cells, inhibition of PP-2A has no effect on cell viability. In contrast, inhibition of PP-1 induces rapid lens epithelial cell apoptosis. This induced cell death is associated with up-regulation of p53 and box and can be inhibited by blocking protein synthesis. Our results suggest that PP-1 is an important signalling component regulating apoptosis in lens system. (Supported by a NIH grant EY 11372 to D. W-C. Li and Research to Prevent Blindness).

UR - http://www.scopus.com/inward/record.url?scp=33749110262&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33749110262&partnerID=8YFLogxK

M3 - Article

AN - SCOPUS:33749110262

VL - 12

SP - A1403

JO - FASEB Journal

JF - FASEB Journal

SN - 0892-6638

IS - 8

ER -