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J. Biol. Chem., Vol. 263, Issue 2, 799-805, Jan, 1988
DE Hartter and A Barnea
We characterized the mechanism of copper accumulation by the brain, using
rat hypothalamic tissue slices incubated with 67Cu as a model system. Two
ligand-dependent saturable processes were discerned: a high affinity, low
capacity process and a low affinity, high capacity process. Vo versus [S]
for the high affinity process was a hyperbolic function having an apparent
Km and Vmax of 6 microM copper and 23 pmol/min/mg protein, respectively. Vo
versus [S] for the low affinity process was a sigmoidal function having an
"apparent Km" (So5) and maximal velocity at saturating [S] of 40 microM
copper and 425 pmol/min/mg protein, respectively. The two processes were
similar in that each exhibited: (a) a requirement for complexing of copper
for optimal 67Cu accumulation; (b) a broad ligand specificity with respect
to amino acids (histidine, cysteine, threonine, glycine) and peptides
(Gly-His-Lys, glutathione) and ineffectiveness of albumin in serving as a
facilitatory ligand; (c) a requirement for thermic but not metabolic
energy. In spite of these similarities, a 50- or 1000-fold molar excess of
ligand (histidine) inhibited 67Cu accumulation by the low affinity process
by 60 and 85%, respectively, whereas excess histidine facilitated 67Cu
accumulation by the high affinity process by 1.6-4- fold. These results are
consistent with 1) a carrier-mediated facilitated diffusion, analogous to
that of neutral amino acids, as a means of transporting complexed copper
into brain tissue, and 2) the existence of two distinct carrier sites
interacting in a positive cooperative manner: a high and a low affinity
site.
Brain tissue accumulates 67copper by two ligand-dependent saturable processes. A high affinity, low capacity and a low affinity, high capacity process
Department of Obstetrics and Gynecology, University of Texas Health Science Center, Dallas 75235.
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