Effects of gangliosides on the activity of the plasma membrane Ca2+-ATPase.
نویسندگان
چکیده
Control of intracellular calcium concentrations ([Ca(2+)]i) is essential for neuronal function, and the plasma membrane Ca(2+)-ATPase (PMCA) is crucial for the maintenance of low [Ca(2+)]i. We previously reported on loss of PMCA activity in brain synaptic membranes during aging. Gangliosides are known to modulate Ca(2+) homeostasis and signal transduction in neurons. In the present study, we observed age-related changes in the ganglioside composition of synaptic plasma membranes. This led us to hypothesize that alterations in ganglioside species might contribute to the age-associated loss of PMCA activity. To probe the relationship between changes in endogenous ganglioside content or composition and PMCA activity in membranes of cortical neurons, we induced depletion of gangliosides by treating neurons with d-threo-1-phenyl-2-decanoylamino-3-morpholino-1-propanol (d-PDMP). This caused a marked decrease in the activity of PMCA, which suggested a direct correlation between ganglioside content and PMCA activity. Neurons treated with neuraminidase exhibited an increase in GM1 content, a loss in poly-sialoganglioside content, and a decrease in PMCA activity that was greater than that produced by d-PDMP treatment. Thus, it appeared that poly-sialogangliosides had a stimulatory effect whereas mono-sialogangliosides had the opposite effect. Our observations add support to previous reports of PMCA regulation by gangliosides by demonstrating that manipulations of endogenous ganglioside content and species affect the activity of PMCA in neuronal membranes. Furthermore, our studies suggest that age-associated loss in PMCA activity may result in part from changes in the lipid environment of this Ca(2+) transporter.
منابع مشابه
Gangliosides activate the phosphatase activity of the erythrocyte plasma membrane Ca2+-ATPase.
The previous studies showed that gangliosides modulated the ATPase activity of the PMCA from porcine brain synaptosomes [Yongfang Zhao, Xiaoxuan Fan, Fuyu Yang, Xujia Zhang, Arch. Biochem. Biophys. 427 (2004) 204-212]. The effects of gangliosides on the hydrolysis of p-nitrophenyl phosphate (pNPP) catalyzed by the erythrocyte plasma membrane Ca(2+)-ATPase, which was characterized as E(2) confor...
متن کاملUp-regulation of plasma membrane H+-ATPase under salt stress may enable Aeluropus littoralis to cope with stress
Plasma membrane H+-ATPase is a major integral membrane protein with a role in various physiological processes including abiotic stress response. To study the effect of NaCl on the expression pattern of a gene encoding the plasma membrane H+-ATPase, an experiment was carried out in a completely random design with three replications. A pair of specific primers was designed based on the sequence o...
متن کاملHeavy metal regulation of plasma membrane H+-ATPase gene expression in halophyte Aeluropus littoralis
The present study was conducted to find the effect of three heavy metals, Ag, Hg and Pb on the expression level of a gene encoding plasma membrane H+-ATPase in Aeluropus littoralis. The experiment was laid out in a completely random design with three replications. The expression of the main gene was normalized to the expression of the housekeeping gene actin. Two 259 and 187 bp fragments were a...
متن کاملMethanol extract and fraction of Anchomanes difformis root tuber modulate liver mitochondrial membrane permeability transition pore opening in rats
Objective: Extracts of Anchomanes difformis (AD) are used in folkloric medicine to treat several diseases and infections. However, their roles in mitochondrial permeability transition pore opening are not known. Material and Methods: The viability of mitochondria isolated from Wistar rat liver used in this experiment, was assessed by monitoring their swel...
متن کاملThe rat liver plasma membrane high affinity (Ca2+-Mg2+)-ATPase is not a calcium pump. Comparison with ATP-dependent calcium transporter.
The high affinity (Ca2+-Mg2+)-ATPase purified from rat liver plasma membrane (Lin, S.-H., and Fain, J. N. (1984) J. Biol. Chem. 259, 3016-3020) has been further characterized. This enzyme also possesses Mg2+-stimulated ATPase activity with K0.5 of 0.16 microM free Mg2+. However, the Vm of the Mg2+-stimulated activity is only half that of the Ca2+-stimulated ATPase activity. The effects of Ca2+ ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Biochimica et biophysica acta
دوره 1838 5 شماره
صفحات -
تاریخ انتشار 2014