PMID- 1566870
OWN - NLM
STAT- MEDLINE
DCOM- 19920521
LR  - 20171213
IS  - 0002-9513 (Print)
IS  - 0002-9513 (Linking)
VI  - 262
IP  - 4 Pt 2
DP  - 1992 Apr
TI  - Involvement of C3 exotoxin-sensitive G proteins (rho/rac) in PTH signal 
      transduction in OK cells.
PG  - F572-7
AB  - Parathyroid hormone (PTH) in opossum kidney (OK) cells leads to inhibition of 
      Na-Pi cotransport, to the generation of inositol trisphosphate (IP3) and 
      adenosine 3',5'-cyclic monophosphate (cAMP) and to a phosphorylation of proteins 
      present in an enriched apical membrane fraction (27, 28; for review see Ref. 23). 
      In the present report we have identified two of these phosphoproteins with 
      molecular weights of approximately 22,000 and approximately 24,000, respectively, 
      as guanosine 5'-triphosphate (GTP)-binding proteins, ADP-ribosylated by the 
      Clostridium botulinum exotoxin C3 and recognized by an anti-rho polyclonal 
      antibody but not by pan-ras monoclonal antibody; as suggested by Western-blot 
      analysis the content of the proteins recognized by the anti-rho antibody did not 
      alter in the membrane fraction as a function of treatment with PTH. Transient 
      permeabilization of OK cells using streptolysin O and including the C3 exotoxin 
      attenuated PTH-dependent inhibition of Na-Pi cotransport at hormone 
      concentrations higher than 10(-10) M; residual PTH-dependent inhibition is equal 
      to that observed after pharmacological activation of protein kinase A and protein 
      kinase C, respectively. C3 exotoxin did not alter PTH-dependent generation of 
      cAMP but modified production of IP3; it was increased at 10(-11) M and reduced at 
      10(-8) M PTH, respectively. It is suggested that protein kinase A may be involved 
      in the phosphorylation of C3 exotoxin-sensitive G proteins (rho/rac). These 
      proteins could be involved in PTH signal transduction.
FAU - Reshkin, S J
AU  - Reshkin SJ
AD  - Department of Physiology, University of Zurich, Switzerland.
FAU - Murer, H
AU  - Murer H
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Am J Physiol
JT  - The American journal of physiology
JID - 0370511
RN  - 0 (Carrier Proteins)
RN  - 0 (Membrane Proteins)
RN  - 0 (Parathyroid Hormone)
RN  - 0 (Sodium-Phosphate Cotransporter Proteins)
RN  - 0 (Symporters)
RN  - EC 2.4.2.- (ADP Ribose Transferases)
RN  - EC 2.4.2.- (exoenzyme C3, Clostridium botulinum)
RN  - EC 3.4.24.69 (Botulinum Toxins)
RN  - EC 3.6.1.- (GTP-Binding Proteins)
RN  - EC 3.6.5.2 (rhoB GTP-Binding Protein)
SB  - IM
MH  - ADP Ribose Transferases/*metabolism
MH  - Animals
MH  - *Botulinum Toxins
MH  - Carrier Proteins/antagonists & inhibitors
MH  - GTP-Binding Proteins/metabolism/*physiology
MH  - Kidney/cytology/metabolism/*physiology
MH  - Membrane Proteins/metabolism
MH  - Opossums
MH  - Parathyroid Hormone/pharmacology/*physiology
MH  - Permeability
MH  - Phosphorylation
MH  - Second Messenger Systems
MH  - *Signal Transduction
MH  - Sodium-Phosphate Cotransporter Proteins
MH  - *Symporters
MH  - rhoB GTP-Binding Protein
EDAT- 1992/04/01 00:00
MHDA- 1992/04/01 00:01
CRDT- 1992/04/01 00:00
PHST- 1992/04/01 00:00 [pubmed]
PHST- 1992/04/01 00:01 [medline]
PHST- 1992/04/01 00:00 [entrez]
AID - 10.1152/ajprenal.1992.262.4.F572 [doi]
PST - ppublish
SO  - Am J Physiol. 1992 Apr;262(4 Pt 2):F572-7. doi: 10.1152/ajprenal.1992.262.4.F572.