Abstract
D-myo-inositol-1,4,5-trisphosphate (InsP3) is a putative intracellular second messenger for the mobilization of Ca2- from intracel-lular stores, in particular, the endoplasmic reticulum1-6. Specific binding sites on the endoplasmic reticulum may participate in the InsP3-induced release of Ca2- from the Ca2- pool6-8. To examine the specific binding sites on the endoplasmic reticulum, we synthesized an arylazide derivative of InsP3 for photoaffinity labelling; InsP3 coupled to p-azidobenzoic acid (InsP3-pAB) using N,N′-carbonyldiimidazole (GDI) was obtained at a 9-11% yield. Here, we report that InsP3-pAB, but not an arylazide derivative of inositol-1,4-bisphophate (Ins(1,4)P2), causes the irreversible inhibition of InsP3-induced release of Ca 2- in saponin-permeabilized photo-irradiated macrophages. The irreversible inhibition by InsP3-pAB after photo-irradiation was prevented by a 10-fold excess of unmodified InsP3.
| Original language | English |
|---|---|
| Pages (from-to) | 723-725 |
| Number of pages | 3 |
| Journal | Nature |
| Volume | 317 |
| Issue number | 6039 |
| DOIs | |
| Publication status | Published - Dec 1 1985 |
Fingerprint
All Science Journal Classification (ASJC) codes
- General
Cite this
Irreversible inhibition of Ca2+ release in saponin-Treated macrophages by the photoaffinity derivative of inositol-1,4,5-Trisphosphate. / Hirata, Masato; Sasaguri, Toshiyuki; Hamachi, Takafumi; Hashimoto, Toshihiko; Kukita, Masataka; Koga, Toshitaka.
In: Nature, Vol. 317, No. 6039, 01.12.1985, p. 723-725.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Irreversible inhibition of Ca2+ release in saponin-Treated macrophages by the photoaffinity derivative of inositol-1,4,5-Trisphosphate
AU - Hirata, Masato
AU - Sasaguri, Toshiyuki
AU - Hamachi, Takafumi
AU - Hashimoto, Toshihiko
AU - Kukita, Masataka
AU - Koga, Toshitaka
PY - 1985/12/1
Y1 - 1985/12/1
N2 - D-myo-inositol-1,4,5-trisphosphate (InsP3) is a putative intracellular second messenger for the mobilization of Ca2- from intracel-lular stores, in particular, the endoplasmic reticulum1-6. Specific binding sites on the endoplasmic reticulum may participate in the InsP3-induced release of Ca2- from the Ca2- pool6-8. To examine the specific binding sites on the endoplasmic reticulum, we synthesized an arylazide derivative of InsP3 for photoaffinity labelling; InsP3 coupled to p-azidobenzoic acid (InsP3-pAB) using N,N′-carbonyldiimidazole (GDI) was obtained at a 9-11% yield. Here, we report that InsP3-pAB, but not an arylazide derivative of inositol-1,4-bisphophate (Ins(1,4)P2), causes the irreversible inhibition of InsP3-induced release of Ca 2- in saponin-permeabilized photo-irradiated macrophages. The irreversible inhibition by InsP3-pAB after photo-irradiation was prevented by a 10-fold excess of unmodified InsP3.
AB - D-myo-inositol-1,4,5-trisphosphate (InsP3) is a putative intracellular second messenger for the mobilization of Ca2- from intracel-lular stores, in particular, the endoplasmic reticulum1-6. Specific binding sites on the endoplasmic reticulum may participate in the InsP3-induced release of Ca2- from the Ca2- pool6-8. To examine the specific binding sites on the endoplasmic reticulum, we synthesized an arylazide derivative of InsP3 for photoaffinity labelling; InsP3 coupled to p-azidobenzoic acid (InsP3-pAB) using N,N′-carbonyldiimidazole (GDI) was obtained at a 9-11% yield. Here, we report that InsP3-pAB, but not an arylazide derivative of inositol-1,4-bisphophate (Ins(1,4)P2), causes the irreversible inhibition of InsP3-induced release of Ca 2- in saponin-permeabilized photo-irradiated macrophages. The irreversible inhibition by InsP3-pAB after photo-irradiation was prevented by a 10-fold excess of unmodified InsP3.
UR - http://www.scopus.com/inward/record.url?scp=0022271082&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0022271082&partnerID=8YFLogxK
U2 - 10.1038/317723a0
DO - 10.1038/317723a0
M3 - Article
VL - 317
SP - 723
EP - 725
JO - Nature
JF - Nature
SN - 0028-0836
IS - 6039
ER -