Photodynamic action of porphyrin on Ca2+ influx in endoplasmic reticulum: a comparison with mitochondria.
نویسندگان
چکیده
We have studied the distribution properties of haematoporphyrin (HP) and protoporphyrin (PP) in mitochondria and endoplasmic reticulum after isolation from rat liver. The photosensitizing efficiency of porphyrin on the Ca2+ influx function of microsomes has been compared with that obtained on Ca2+ uptake in mitochondria. HP and PP are accumulated in microsomes to a greater extent than in mitochondria, both porphyrins binding to membrane protein sites. The Ca2+ influx functions of mitochondria and microsomes, before and after irradiation in the presence of HP or PP, were studied by following the changes in the free Ca2+ concentration in the medium as revealed by the variations in fluorescence intensity of the Ca2+ indicator Calcium Green-1. For the same amount of incorporated porphyrin, the Ca2+ influx function of microsomes is degraded by irradiation more rapidly than that of mitochondria. The protective effect of dithiothreitol suggests that thiol groups in the Ca2+-transporting enzyme are the preferential targets of the photodynamic effect. These results suggest that intracellular Ca2+ movements are altered primarily by the endoplasmic reticulum rather than by mitochondrial damage, in good agreement with other observations made in porphyrin-loaded irradiated cells.
منابع مشابه
Ca2+-induced Ca2+ release in Aplysia bag cell neurons requires interaction between mitochondrial and endoplasmic reticulum stores.
Intracellular Ca2+ is influenced by both Ca2+ influx and release. We examined intracellular Ca2+ following action potential firing in the bag cell neurons of Aplysia californica. Following brief synaptic input, these neuroendocrine cells undergo an afterdischarge, resulting in elevated Ca2+ and the secretion of neuropeptides to initiate reproduction. Cultured bag cell neurons were injected with...
متن کاملEvidences on the existence of a new potassium channel in the rough endoplasmic reticulum (RER) of rat hepatocytes
Introduction: we have recently reported the presence of two potassium currents with 598 and 368 pS conductance in the rough endoplasmic reticulum (RER) membrane. The 598 pS channel was voltage dependent and ATP sensitive. However, the 368 pS channel was rarely observed and its identity remained obscure. Since cationic channels in intracellular organelles such as mitochondria and RER play imp...
متن کاملSubplasmalemmal mitochondria modulate the activity of plasma membrane Ca 2 +
Mitochondria are dynamic organelles that modulate cellular Ca2+ signals by interacting with Ca2+ transporters on the plasma membrane or the endoplasmic reticulum (ER). To study how mitochondria dynamics affects cell Ca2+ homeostasis, we overexpressed two mitochondrial fission proteins, hFis1 and Drp1, and measured Ca2+ changes within the cytosol and the ER in HeLa cells. Both proteins fragmente...
متن کاملA molecular study on the endoplasmic reticulum potassium channels in hepatocytes
Introduction: It has recently been suggested that the KATP channel subunits Kir6.x and BKCa channels exist in the endoplasmic reticulum of cardiomyocytes and neurons. Our previous studies showed the electrophysiological behavior of cation channels in the rough endoplasmic reticulum (RER) of rat hepatocytes. Therefore, we hypothesized that KATP channels and Ca2+-activated potassium channels m...
متن کاملNitric oxide inhibits capacitative cation influx in human platelets by promoting sarcoplasmic/endoplasmic reticulum Ca2+-ATPase-dependent refilling of Ca2+ stores.
Nitric oxide (NO) is a potent inhibitor of thrombin-induced increase in cytoplasmic free Ca2+ concentration and aggregation in platelets, but the precise mechanism of this inhibition is unclear. To measure Ca2+/Mn2+ influx in intact platelets and to monitor Ca2+ uptake into the stores in permeabilized platelets, fura-2 was used. In intact platelets, maximal capacitative Ca2+ and Mn2+ influx dev...
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:
- The Biochemical journal
دوره 338 ( Pt 1) شماره
صفحات -
تاریخ انتشار 1999