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Evidence for more than one Ca/sup 2 +/ transport mechanism in mitochondria

Journal Article · · Biochemistry; (United States)
OSTI ID:7353092
The active transport and internal binding of the Ca/sup 2 +/ analogue Mn/sup 2 +/ by rat liver mitochondria were monitored with electron paramagnetic resonance. The binding of transported Mn/sup 2 +/ depended strongly on internal pH over the range 7.7 - 8.9. Gradients of free Mn/sup 2 +/ were compared with K/sup +/ gradients measured on valinomycin-treated samples. In the steady state, the electrochemical Mn/sup 2 +/ activity was larger outside than inside the mitochondria. The observed gradients of free Mn/sup 2 +/ and of H/sup +/ could not be explained by a single ''passive'' uniport or antiport mechanism of divalent cation transport. This conclusion was further substantiated by observed changes in steady-state Ca/sup 2 +/ and Mn/sup 2 +/ distributions induced by La/sup 3 +/ and ruthenium red. Ruthenium red reduced total Ca/sup 2 +/ or Mn/sup 2 +/ uptake, and both inhibitors caused release of divalent cation from preloaded mitochondria. A model is proposed in which divalent cations are transported by at least two mechanisms: a passive uniport and an active pump, cation antiport or anion symport. The former is more sensitive to La/sup 3 +/ and ruthenium red. Under energized steady-state conditions, the net flux of Ca/sup 2 +/ or Mn/sup 2 +/ is inward over and outward over. The need for more than one transport system in regulating cytoplasmic Ca/sup 2 +/ is discussed.
Research Organization:
Univ. of Rochester, NY
OSTI ID:
7353092
Journal Information:
Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 15:17; ISSN BICHA
Country of Publication:
United States
Language:
English

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