PMID- 1464505
OWN - NLM
STAT- MEDLINE
DCOM- 19930115
LR  - 20151119
IS  - 0146-0404 (Print)
IS  - 0146-0404 (Linking)
VI  - 33
IP  - 13
DP  - 1992 Dec
TI  - Guanine nucleotide binding proteins in the dual regulation of lacrimal function.
PG  - 3592-600
AB  - The purpose of this study was to identify and characterize functional G proteins 
      that couple regulatory peptides with lacrimal secretory functions. Membranes were 
      prepared from isolated rat exorbital lacrimal gland acini, and guanosine 
      5'-triphosphate (GTP)-dependence of adenylyl cyclase activity, known to be 
      coupled with regulation of secretion, was measured. The guanine nucleotide GTP 
      produced a biphasic response in the activity of membrane-bound adenylyl cyclase 
      during a 10 min incubation with a maximum stimulation at 10(-5) mol/l GTP. 
      Significant inhibition occurred at a dose of 10(-3) mol/l GTP, with cyclic 
      adenosine monophosphate (cAMP) production reduced to less than basal levels. The 
      effect of ADP-ribosylation of membrane proteins by the toxins produced by Vibrio 
      cholera or Bordetella pertussis on lacrimal adenylyl cyclase was assessed by 
      sodium dodecyl sulfate-polyacrylamide gel electrophoresis, autoradiography, and 
      laser densitometry. Cholera toxin treatment of membranes resulted in 
      dose-(0.5-100 micrograms/ml) and time-dependent (0-45 min) adenosine diphosphate 
      (ADP)-ribosylation of two membrane proteins with M(r) values of 42,000 and 
      45,000. Pertussis toxin treatment resulted in the specific ADP-ribosylation of a 
      single protein that migrates with an M(r) value of 41,000. This also was dose 
      (0.5-25 micrograms/ml) and time dependent (0-30 min). Incorporation of 32P into 
      the 45,000 M(r) and 42,000 M(r) proteins in the presence of 50 micrograms/ml 
      cholera toxin was guanine nucleotide dependent, with a two- to threefold increase 
      in labeling when the membranes were incubated with 1 or 0.5 mmol/l GTP. This 
      effect was enhanced in the presence of the nonhydrolyzable GTP analog GTP gamma 
      S.(ABSTRACT TRUNCATED AT 250 WORDS)
FAU - Cripps, M M
AU  - Cripps MM
AD  - Department of Physiology, Louisiana State University Medical Center, New Orleans 
      70119-2799.
FAU - Bennett, D J
AU  - Bennett DJ
LA  - eng
GR  - EY07380/EY/NEI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Invest Ophthalmol Vis Sci
JT  - Investigative ophthalmology & visual science
JID - 7703701
RN  - 0 (Adenylate Cyclase Toxin)
RN  - 0 (Eye Proteins)
RN  - 0 (Guanine Nucleotides)
RN  - 0 (Membrane Proteins)
RN  - 0 (Virulence Factors, Bordetella)
RN  - 20762-30-5 (Adenosine Diphosphate Ribose)
RN  - 27YLU75U4W (Phosphorus)
RN  - 9012-63-9 (Cholera Toxin)
RN  - EC 2.4.2.31 (Pertussis Toxin)
RN  - EC 3.6.1.- (GTP-Binding Proteins)
RN  - EC 4.6.1.1 (Adenylyl Cyclases)
SB  - IM
MH  - Adenosine Diphosphate Ribose/metabolism
MH  - Adenylate Cyclase Toxin
MH  - Adenylyl Cyclases/metabolism
MH  - Animals
MH  - Cholera Toxin/pharmacology
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Eye Proteins/metabolism
MH  - GTP-Binding Proteins/*metabolism
MH  - Guanine Nucleotides/pharmacology
MH  - Lacrimal Apparatus/*metabolism
MH  - Male
MH  - Membrane Proteins/metabolism
MH  - Pertussis Toxin
MH  - Phosphorus/metabolism
MH  - Rats
MH  - Rats, Sprague-Dawley
MH  - Virulence Factors, Bordetella/pharmacology
EDAT- 1992/12/01 00:00
MHDA- 1992/12/01 00:01
CRDT- 1992/12/01 00:00
PHST- 1992/12/01 00:00 [pubmed]
PHST- 1992/12/01 00:01 [medline]
PHST- 1992/12/01 00:00 [entrez]
PST - ppublish
SO  - Invest Ophthalmol Vis Sci. 1992 Dec;33(13):3592-600.