Occurrence of the erythroid cell specific arachidonate 15-lipoxygenase in human reticulocytes

P Kroschwald, A Kroschwald, H Ku, P Ludwig… - Biochemical and …, 1989 - Elsevier
P Kroschwald, A Kroschwald, H Ku, P Ludwig, BJ Thiele, M Ho, T Schewe, SM Rapoport
Biochemical and biophysical research communications, 1989Elsevier
Human reticulocytes obtained from patients suffering from various haemolytic disorders
convert exogenous {1-14 C}-arachidonic acid to 15-hydroxy-5, 8, 11, 13 (Z, Z, Z, E)-
eicosatetraenoic acid (15-HETE). Immunological studies (dot blot, Western blot) indicated
that human reticulocytes contain a lipoxygenase which cross-reacts with a polyclonal
antiserum against the rabbit reticulocyte lipoxygenase. Northern blotting with a cloned
lipoxygenase cDNA probe shows that the specific mRNA is also present. Reaction of the …
Abstract
Human reticulocytes obtained from patients suffering from various haemolytic disorders convert exogenous {1-14C}-arachidonic acid to 15-hydroxy-5,8,11,13(Z,Z,Z,E)-eicosatetraenoic acid (15-HETE). Immunological studies (dot blot, Western blot) indicated that human reticulocytes contain a lipoxygenase which cross-reacts with a polyclonal antiserum against the rabbit reticulocyte lipoxygenase. Northern blotting with a cloned lipoxygenase cDNA probe shows that the specific mRNA is also present. Reaction of the lipoxygenase with submitochondrial particles caused inactivation of respiratory enzymes. The occurrence of an erythroid cell specific lipoxygenase of similar type in reticulocytes of various mammals and man suggests the general role of this enzyme in the maturational degradation of mitochondria.
Elsevier