PMID- 9013447
OWN - NLM
STAT- MEDLINE
DCOM- 19970417
LR  - 20211203
IS  - 1046-6673 (Print)
IS  - 1046-6673 (Linking)
VI  - 8
IP  - 1
DP  - 1997 Jan
TI  - Differential regulation of the dual-specificity protein-tyrosine phosphatases 
      CL100, B23, and PAC1 in mesangial cells.
PG  - 40-50
AB  - The extracellular-signal-regulated kinase (ERK), the best described MAP kinase 
      cascade, is a major signaling system by which cells transduce extracellular cues 
      into intracellular responses. ERK is activated by phosphorylation both on 
      tyrosine and threonine residues. Therefore, a new clas of protein-tyrosine 
      phosphatases (PTPases) that exhibit dual catalytic activity toward both 
      regulatory sites on ERK is of special interest in the control of intracellular 
      signaling. This study examined the expression and regulation of the 
      dual-specificity PTPases CL100, B23, and PAC1. Findings included differential 
      expression of these phosphatases in diverse cell lines and an expression of all 
      three dual-specificity PTPases in human mesangial cells (HMC), thereby allowing 
      investigation of their regulation in a single cell line. The MEK antagonist PD 
      098059 and selective extracellular agonists of ERK were used to demonstrate the 
      induction of CL100, PAC1, and B23 in response to activation of the ERK cascade. 
      In contrast, anisomycin, an agonist of the recently described MAP kinases 
      stress-activated protein kinase (SAPK) and p38 MAP kinase, stimulated CL100 gene 
      expression but had little effect on PAC1 and B23. This effect of anisomycin was 
      partly inhibited in the presence of the p38 MAP kinase antagonist SB 203580. This 
      study suggests a potential mechanism to regulate ERK activity through feedback 
      inhibition by demonstrating the ERK cascade's induction of the dual-specificity 
      PTPases CL100, PAC1, and B23. Moreover, this study suggests an ERK-independent 
      induction of CL100 following stimulation of SAPK and p38 MAP kinase. This mode of 
      induction of a phosphatase capable of inactivating ERK may play an important role 
      in the cellular stress response.
FAU - Bokemeyer, D
AU  - Bokemeyer D
AD  - Department of Medicine, Medical College of Wisconsin, Milwaukee 53226-0509, USA.
FAU - Sorokin, A
AU  - Sorokin A
FAU - Dunn, M J
AU  - Dunn MJ
LA  - eng
GR  - DK 41684/DK/NIDDK NIH HHS/United States
GR  - HL 22563/HL/NHLBI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Am Soc Nephrol
JT  - Journal of the American Society of Nephrology : JASN
JID - 9013836
RN  - 0 (Cell Cycle Proteins)
RN  - 0 (Enzyme Inhibitors)
RN  - 0 (Flavonoids)
RN  - 0 (Imidazoles)
RN  - 0 (Immediate-Early Proteins)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Pyridines)
RN  - 0 (RNA, Messenger)
RN  - 117896-08-9 (Nucleophosmin)
RN  - 6C74YM2NGI (Anisomycin)
RN  - EC 3.1.3.16 (Phosphoprotein Phosphatases)
RN  - EC 3.1.3.16 (Protein Phosphatase 1)
RN  - EC 3.1.3.16 (Protein Phosphatase 2)
RN  - EC 3.1.3.48 (DUSP1 protein, human)
RN  - EC 3.1.3.48 (DUSP2 protein, human)
RN  - EC 3.1.3.48 (Dual Specificity Phosphatase 1)
RN  - EC 3.1.3.48 (Dual Specificity Phosphatase 2)
RN  - EC 3.1.3.48 (Dusp1 protein, rat)
RN  - EC 3.1.3.48 (Dusp2 protein, rat)
RN  - EC 3.1.3.48 (Protein Tyrosine Phosphatases)
RN  - OU13V1EYWQ (SB 203580)
RN  - SJE1IO5E3I (2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one)
SB  - IM
MH  - Animals
MH  - Anisomycin/pharmacology
MH  - *Cell Cycle Proteins
MH  - Cell Line
MH  - Dual Specificity Phosphatase 1
MH  - Dual Specificity Phosphatase 2
MH  - Enzyme Inhibitors/pharmacology
MH  - Flavonoids/pharmacology
MH  - Gene Expression Regulation, Enzymologic
MH  - Glomerular Mesangium/cytology/*enzymology
MH  - Humans
MH  - Imidazoles/pharmacology
MH  - Immediate-Early Proteins/antagonists & inhibitors/genetics/*metabolism
MH  - Male
MH  - Nuclear Proteins/antagonists & inhibitors/genetics/*metabolism
MH  - Nucleophosmin
MH  - *Phosphoprotein Phosphatases
MH  - Protein Phosphatase 1
MH  - Protein Phosphatase 2
MH  - Protein Tyrosine Phosphatases/antagonists & inhibitors/genetics/*metabolism
MH  - Pyridines/pharmacology
MH  - RNA, Messenger/analysis
MH  - Rats
MH  - Rats, Sprague-Dawley
MH  - Signal Transduction/physiology
EDAT- 1997/01/01 00:00
MHDA- 1997/01/01 00:01
CRDT- 1997/01/01 00:00
PHST- 1997/01/01 00:00 [pubmed]
PHST- 1997/01/01 00:01 [medline]
PHST- 1997/01/01 00:00 [entrez]
AID - 10.1681/ASN.V8140 [doi]
PST - ppublish
SO  - J Am Soc Nephrol. 1997 Jan;8(1):40-50. doi: 10.1681/ASN.V8140.