PMID- 8589550
OWN - NLM
STAT- MEDLINE
DCOM- 19960327
LR  - 20131121
IS  - 1040-5704 (Print)
IS  - 1040-5704 (Linking)
VI  - 8
IP  - 5
DP  - 1995 Sep-Oct
TI  - Selective effects of charge on G protein activation by FSH-receptor residues 
      551-555 and 650-653.
PG  - 278-84
AB  - Two cytosolic regions of the rat testicular FSH receptor (FSHR), residues 533-555 
      and 645-653, have been identified as G protein-coupling domains. We localized the 
      activity in these domains to their C-terminal sequences, residues 551-555 (KIAKR, 
      net charge +3) and 650-653 (RKSH, net charge +3), and examined the effects of 
      charge on G protein activation by the C-terminal peptides, using synthetic 
      analogs containing additions, through alanine (A) linkages, of arginine (R, +), 
      histidine (H, +) or both. RA-KIAKR (net charge +4) mimicked the effect of 
      FSHR-(551-555) on guanine nucleotide exchange in rat testis membranes, but 
      reduced its ability to inhibit FSH-stimulated estradiol biosynthesis in cultured 
      rat Sertoli cells. Further increasing net charge by the addition of H 
      (HARA-KIAKR, net charge +5) increased guanosine 5'-triphosphate (GTP) binding, 
      but eliminated FSHR-(551-555) effects on FSH-stimulated steroidogenesis. HA-RKSH 
      (net charge +4) significantly inhibited guanine nucleotide exchange in rat testis 
      membranes, but stimulated basal and potentiated FSH-induced estradiol 
      biosynthesis in cultured rat Sertoli cells. Addition of two H residues 
      (HAHA-RKSH, net charge +5) restored GTP binding and further potentiated basal and 
      FSH-stimulated steroidogenesis. These results suggest that positive charges in G 
      protein-coupling domains of the FSHR play a role in modulating G protein 
      activation and postbinding effects of FSH, such as steroidogenesis.
FAU - Grasso, P
AU  - Grasso P
AD  - Albany Medical College, NY, USA.
FAU - Deziel, M R
AU  - Deziel MR
FAU - Reichert, L E Jr
AU  - Reichert LE Jr
LA  - eng
GR  - HD-13938/HD/NICHD NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Pept Res
JT  - Peptide research
JID - 8913494
RN  - 0 (Peptide Fragments)
RN  - 0 (Receptors, FSH)
RN  - 4TI98Z838E (Estradiol)
RN  - 86-01-1 (Guanosine Triphosphate)
RN  - 9002-68-0 (Follicle Stimulating Hormone)
RN  - EC 3.6.1.- (GTP-Binding Proteins)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Cells, Cultured
MH  - Electrochemistry
MH  - Estradiol/biosynthesis
MH  - Follicle Stimulating Hormone/pharmacology
MH  - GTP-Binding Proteins/*metabolism
MH  - Guanosine Triphosphate/metabolism
MH  - Male
MH  - Molecular Sequence Data
MH  - Peptide Fragments/*chemistry/pharmacology
MH  - Protein Structure, Secondary
MH  - Rats
MH  - Rats, Sprague-Dawley
MH  - Receptors, FSH/*chemistry
MH  - Sertoli Cells/drug effects/metabolism
MH  - Structure-Activity Relationship
EDAT- 1995/09/01 00:00
MHDA- 2001/03/28 10:01
CRDT- 1995/09/01 00:00
PHST- 1995/09/01 00:00 [pubmed]
PHST- 2001/03/28 10:01 [medline]
PHST- 1995/09/01 00:00 [entrez]
PST - ppublish
SO  - Pept Res. 1995 Sep-Oct;8(5):278-84.