## Abstract The mechanisms of peroxisomal biogenesis remain incompletely understood, specially regarding the role of the endoplasmic reticulum (ER) in human cells, where genetic disorders of peroxisome biogenesis lead to Zellweger syndrome (ZS). The Pex3p peroxisomal membrane protein (PMP) required
oscillations in a model of energy-dependent uptake by the endoplasmic reticulum
β Scribed by B.K. Dellen; M.J. Barber; M.L. Ristig; J. Hescheler; H. Sauer; M. Wartenberg
- Publisher
- Elsevier Science
- Year
- 2005
- Tongue
- English
- Weight
- 455 KB
- Volume
- 237
- Category
- Article
- ISSN
- 0022-5193
No coin nor oath required. For personal study only.
β¦ Synopsis
Active Ca2+ transport in living cells necessitates controlled supply of metabolic energy. Direct coupling between sarco/endoplasmic reticulum (ER) Ca2+ ATPases (SERCA) and intracellular energy-generation sites has been well established experimentally. On the basis of these experimental findings we propose a pump-driven model to investigate complex dynamic properties of a cell system. The model describes the pump process both by the Ca2+ ATPase itself and by a suitable description of the glycolysis. The associated set of differential equations shows a rich behavior, the solutions ranging from simple periodic oscillations to complex patterns such as bursting and spiking. Recent experimental results on calcium oscillations in Xenopus laevis oocytes and on dynamic patterns of intracellular Ca2+ concentrations in electrically non-excitable cells are well described by corresponding theoretical results derived within the proposed model. The simulation results are further compared to spontaneous [Ca2+] oscillations in primitive endodermal cells.
π SIMILAR VOLUMES
The activity of ornithine decarboxylase, the key enzyme in the synthesis of polyamines, is essential for proliferation and differentiation of all living cells. Two inhibitors of ornithine decarboxylase, a-difluoromethylornithine (DFMO) and 1-aminooxy-3-aminopropane (APA), caused swelling of endoplas
## Abstract The primary intracellular site of localization of the estrogen receptor activation factor (EβRAF) is shown here to be the endoplasmic reticulum where the protein remains anchored through an estrogen dependent mechanism. The retention of EβRAF by the endoplasmic reticulum is facilitated