SUBCELLULAR-DISTRIBUTION OF PROTEIN-KINASE-C (PKC) IN ERYTHROCYTES AND CONCENTRATION OF D-MYO-INOSITOL-1,4,5-TRISPHOSPHATE (IP3) IN PLATELETS AND MONOCYTES OF FORCE-FED ZINC-DEFICIENT RATS
Hp. Roth et al., SUBCELLULAR-DISTRIBUTION OF PROTEIN-KINASE-C (PKC) IN ERYTHROCYTES AND CONCENTRATION OF D-MYO-INOSITOL-1,4,5-TRISPHOSPHATE (IP3) IN PLATELETS AND MONOCYTES OF FORCE-FED ZINC-DEFICIENT RATS, Biological trace element research, 53(1-3), 1996, pp. 225-234
The purpose of the present study was to investigate whether alimentary
zinc (Zn) deficiency affects the activities of the Zn metalloenzymes
protein kinase C (pKC) and the phosphatidylinositol-specific phospholi
pase C (PLC) in force-fed Zn-deficient rats. The in vivo activity of p
KC was determined by measuring the subcellular distribution of the enz
yme between the cytosolic and the particulate fraction of erythrocytes
, whereas the activity of PLC was measured indirectly through the conc
entration of its metabolite inositol-1,4,5-trisphosphate (IP3) in plat
elets and monocytes. For this purpose, 24 male Sprague-Dawley rats wit
h an average live mass of 126 g were divided into 2 groups of 12 anima
ls each. The Zn-deficient and the control rats received a semisyntheti
c casein diet with a Zn content of 1.2 and 24.1 ppm, respectively. All
animals were fed the same amount of the diet (10.8 g dry matter [DM]/
d and rat) four times daily by gastric tube. After 12 d, the depleted
rats were in a state of severe Zn deficiency, as demonstrated by a 70%
lower Zn concentration and a 66% reduction in the serum activity of a
lkaline phosphatase. The radioimmunologically determined concentration
of IP3 was reduced by a significant 55% in the platelets of the Zn-de
ficient rats (8.4 pmol IP3/5.10(8)) as compared with the control rats
(18.8 pmol IP3/5.10(8)), whereas the IP3 concentration in the monocyte
s was not affected by the alimentary Zn supply (1.4 vs 1.2 pmol IP3/10
(6)), nor was there any difference between the Zn-deficient and the co
ntrol rats with regard to the radioenzymatically determined specific a
ctivity of pKC, either in the cytosolic fraction (32.7 vs 32.5 pmol P/
min/mg protein) or in the particulate fraction (38.1 vs 36.5 pmol P/mi
n/mg protein) of the erythrocytes.