Abstract
Tissue transglutaminase (tTG) is a novel G-protein that previous studies showed can couple ligand-bound activated α(1B) adrenoreceptors to phospholipase C-δ, resulting in phosphoinositide (PI) hydrolysis. In human neuroblastoma SH-SY5Y cells we found that although endogenous tTG can facilitate α(1B) adrenoreceptor-stimulated PI hydrolysis, its contribution is minor compared with the classical heterotrimeric G-protein G(q/11). Further, we show that the α(1B) adrenoreceptor recruits tTG to the membrane and that this recruitment is enhanced by agonist occupancy of the receptor. In addition, the effects of tTG on signalling are bimodal. At low expression levels, tTG enhanced α(1B) adrenoreceptor-stimulated PI hydrolysis, whereas at higher expression levels tTG attenuated significantly this response. These findings are the first to demonstrate that a protein can both facilitate and attenuate receptor-stimulated PI hydrolysis.
| Original language | English |
|---|---|
| Pages (from-to) | 541-549 |
| Number of pages | 9 |
| Journal | Biochemical Journal |
| Volume | 343 |
| Issue number | 3 |
| DOIs | |
| State | Published - Nov 1 1999 |
| Externally published | Yes |
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Keywords
- α(1B) adrenoreceptors
- Phosphoinositide hydrolysis
- Phospholipase C
- SH-SY5Y cells
ASJC Scopus subject areas
- Biochemistry
Cite this
Novel bimodal effects of the G-protein tissue transglutaminase on adrenoreceptor signalling. / Zhang, Jianwen; Tucholski, Janusz; Lesort, Mathieu; Jope, Richard S; Johnson, Gail V W.
In: Biochemical Journal, Vol. 343, No. 3, 01.11.1999, p. 541-549.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Novel bimodal effects of the G-protein tissue transglutaminase on adrenoreceptor signalling
AU - Zhang, Jianwen
AU - Tucholski, Janusz
AU - Lesort, Mathieu
AU - Jope, Richard S
AU - Johnson, Gail V W
PY - 1999/11/1
Y1 - 1999/11/1
N2 - Tissue transglutaminase (tTG) is a novel G-protein that previous studies showed can couple ligand-bound activated α(1B) adrenoreceptors to phospholipase C-δ, resulting in phosphoinositide (PI) hydrolysis. In human neuroblastoma SH-SY5Y cells we found that although endogenous tTG can facilitate α(1B) adrenoreceptor-stimulated PI hydrolysis, its contribution is minor compared with the classical heterotrimeric G-protein G(q/11). Further, we show that the α(1B) adrenoreceptor recruits tTG to the membrane and that this recruitment is enhanced by agonist occupancy of the receptor. In addition, the effects of tTG on signalling are bimodal. At low expression levels, tTG enhanced α(1B) adrenoreceptor-stimulated PI hydrolysis, whereas at higher expression levels tTG attenuated significantly this response. These findings are the first to demonstrate that a protein can both facilitate and attenuate receptor-stimulated PI hydrolysis.
AB - Tissue transglutaminase (tTG) is a novel G-protein that previous studies showed can couple ligand-bound activated α(1B) adrenoreceptors to phospholipase C-δ, resulting in phosphoinositide (PI) hydrolysis. In human neuroblastoma SH-SY5Y cells we found that although endogenous tTG can facilitate α(1B) adrenoreceptor-stimulated PI hydrolysis, its contribution is minor compared with the classical heterotrimeric G-protein G(q/11). Further, we show that the α(1B) adrenoreceptor recruits tTG to the membrane and that this recruitment is enhanced by agonist occupancy of the receptor. In addition, the effects of tTG on signalling are bimodal. At low expression levels, tTG enhanced α(1B) adrenoreceptor-stimulated PI hydrolysis, whereas at higher expression levels tTG attenuated significantly this response. These findings are the first to demonstrate that a protein can both facilitate and attenuate receptor-stimulated PI hydrolysis.
KW - α(1B) adrenoreceptors
KW - Phosphoinositide hydrolysis
KW - Phospholipase C
KW - SH-SY5Y cells
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UR - http://www.scopus.com/inward/citedby.url?scp=0033231277&partnerID=8YFLogxK
U2 - 10.1042/0264-6021:3430541
DO - 10.1042/0264-6021:3430541
M3 - Article
C2 - 10527931
AN - SCOPUS:0033231277
VL - 343
SP - 541
EP - 549
JO - Biochemical Journal
JF - Biochemical Journal
SN - 0264-6021
IS - 3
ER -