A H+/Ca2+ Antiporter in Membranes of Microsomal Vesicles from Maize Coleoptiles, a Secondary Energized Ca2+ Pump

نویسنده

  • A. Hager
چکیده

Ca2+ Pump, H+-ATPase, Membrane Vesicles, Coleoptile, Zea mays Microsomal vesicles prepared from the ER and the Golgi apparatus of maize coleoptiles possess an ATP-fueled, Cl_-dependent proton pump which can cause an intravesicular acidifica­ tion of the vesicles (A. Hager and M. Heimle, Z. Naturforsch. 36 c, 997 (1981); A. Hager et al., Z. Naturforsch. 35 c, 783-793 (1980)). This acidification is very specifically inhibited by Ca2+. The inhibition is already distinct at concentrations of 30 hm. While 10-fold higher concentrations of La3+ produce similar effects, Mg2+ remains ineffective even at very high concentrations. If Ca2+ is added after acidification of the vesicles, a rapid H+-efflux proportional to the amount of Ca2+ added characterizes the first reaction phase. In the second reaction phase acidification within the vesicles commences anew, however, at a reduced rate. If Ca2+ is added to vesicles whose proton pump has been inhibited by DCCD, the first reaction phase remains unchanged, while the acidification in the second reaction phase does not set in, and only a leak out of protons is observed. These results give support for a H+/C a2+-antiporter mechanism which can function as a secondary energized Ca2+-pump and regulate the Ca2+-concentration in the cytoplasm.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

ATP-dependent proton transport into vesicles of microsomal membranes of Zea mays coleoptiles.

ATP-dependent proton pumps were found in the vesicles of microsomal membrane fractions of maize coleoptiles. Two membrane fractions isolated by density gradient centrifugation were identified by the aid of marker enzymes and electron microscopic analysis. Membrane fraction A largely consisted of vesicles of smooth ER and of the Golgi complex, fraction B predominantly of vesicles of plasmalemma ...

متن کامل

Active transport of calcium in Neurospora plasma membrane vesicles.

Functionally inverted plasma membrane vesicles isolated from the eukaryotic microorganism Neurospora crassa catalyze Mg2+/ATP-dependent Ca2+ uptake. Inhibitors induced efflux studies and isotope-exchange experiments indicate that the Ca2+ is accumulated inside the vesicles against a concentration gradient of about 40-fold, and that the majority of the transported Ca2+ is present essentially in ...

متن کامل

Ca2+-H+ antiport activity in synaptic vesicles isolated from sheep brain cortex.

Synaptic vesicles isolated from sheep brain cortex exhibit an ATP-dependent Ca2+ accumulation that is inhibited by the protonophore uncoupler carbonyl cyanide m-chorophenylhydrazone (CCCP) and completely released by the Ca2+ ionophore ionomycin. This transport activity was sensitive to the V-type ATPase inhibitor, bafilomycin, but not to the P-type ATPase inhibitor, vanadate. We also observed t...

متن کامل

A sodium-calcium exchange mechanism in plasma membrane vesicles isolated from ram sperm flagella.

The ability of mature mammalian spermatozoa to maintain a co-ordinated and forward motility is dependent upon intracellular free Ca2+ being maintained within anarrow concentration range [l]. At the level of the flagellar plasma membrane this could be achieved by two systems: (a) an ATP requiring Ca2’pump; or (b) a Na+/Ca2+ antiporter. Although such plasma membrane Ca2+extrusion mechanisms have ...

متن کامل

Energized Ca2+ transport by hepatopancreatic basolateral plasma membranes of Homarus americanus.

Ca2+ transport by hepatopancreatic basolateral membrane vesicles of Atlantic lobster (Homarus americanus) occurred by at least two independent processes: (1) an ATP-dependent carrier transport system, and (2) a Na+-gradient-dependent carrier mechanism. The sensitivity of ATP-dependent Ca2+ transport to vanadate indicated that it was probably due to a P-type ATPase. This system exhibited an extr...

متن کامل

ذخیره 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 نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2013