The activation of phosphatidylinositol-specific phospholipase C by insulin in mammary epithelial cells of lactating mouse
β Scribed by Akio Yoshimoto; Keiko Nakanishi; Tadashi Anzai; Senichi Komine
- Publisher
- John Wiley and Sons
- Year
- 1990
- Tongue
- English
- Weight
- 342 KB
- Volume
- 8
- Category
- Article
- ISSN
- 0263-6484
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
The role(s) of protein kinases in the regulation of G protein-dependent activation of phosphatidylinositolspecific phospholipase C by tumor necrosis factor-alpha was investigated in the osteoblast cell line MC3T3-E1. We have previously reported the stimulatory effects of tumor necrosis factor-alpha
We investigated the regulatory mechanism of interleukin-6 (IL-6) synthesis induced by interleukin-1 (IL-1) in osteoblast-like MC3T3-E1 cells. IL-1 stimulated the secretion of IL-6 in a dose-dependent manner in the range between 0.1 and 100 ng/ml. Staurosporine and calphostin C, inhibitors of protein
Swiss 3T3 mouse fibroblasts were exposed to 10 microM colchicine to disrupt microtubules, then stimulated with insulin-like growth factor-I. Immunoprecipitation experiments showed that insulin-like growth factor-I receptor and insulin receptor substrate-1 were tyrosine phosphorylated to the same ext
Respiratory syncytial virus (RSV) infection induced programmed cell death or apoptosis in the cultured lung epithelial cell line, A549. The apoptotic cells underwent multiple changes, including fragmentation and degradation of genomic DNA, consistent with the activation of the DNA fragmentation fact
We have previously shown that CD4 ligands inhibit interleukin-2 (IL-2) production and T cell proliferation in human peripheral CD4 + T lymphocytes, in an MHC-independent way. Two major pathways implicated in T cell activation are inhibited by binding of CD4 ligands to the CD4 molecule, i. e. Ca 2+ s