Jz. Nowak et al., ARYLAMINE AND ARYLALKYLAMINE N-ACETYLTRANSFERASES IN RETINA, PINEAL-GLAND, BRAIN AND LIVER OF CHICKS - A COMPARATIVE-STUDY, Neurochemistry international, 27(3), 1995, pp. 285-297
Regulation of arylamine N-acetyltransferase (A-NAT) and arylalkylamine
N-acetyltransferase (AA-NAT) was examined in retina, pineal gland, br
ain and liver of chicks. Enzyme activities were determined using as su
bstrates p-phenetidine and procainamide for A-NAT, tryptamine and phen
ethylamine for AA-NAT. The activity of A-NAT in all tissues studied do
es not appear to be regulated by a light-dark cycle. On the other hand
, AA-NAT showed distinct light-dark dependent changes (with high Value
s at night) in the retina and pineal gland, but not in brain and liver
. The nocturnal increase of retinal and pineal AA-NAT activity was pre
vented by cycloheximide; the drug did not affect A-NAT activity in the
se tissues. Treatment of light-adapted chicks with aminophylline signi
ficantly increased AA-NAT activity of the retina and pineal gland, wit
hout altering the enzyme activity in brain and liver. In these animals
, the activity of A-NAT (procainamide) did not change in any tissue st
udied, whereas the enzyme activity measured using p-phenetidine as a s
ubstrate did decrease but only in the retina. A similar pattern of cha
nges in retinal A-NAT and AA-NAT activities was observed after intraoc
ular injection of d,b-cAMP. The rate of inactivation at 4 degrees C wa
s significantly slower for AA-NAT than A-NAT. NATs from brain and live
r displayed the highest and lowest, respectively, lability in the cold
. The results indicate that the chick retina contains both A-NAT and A
A-NAT. The two enzymes have distinct characteristics and the regulatio
n of their activities is different. The retinal A-NAT is similar to A-
NAT present in other tested tissues; however, AA-NAT can be induced at
night only in the retina and pineal gland. It is suggested that there
are two forms of retinal A-NAT, and that, under specified conditions,
the activity of one form (A-NAT; p-pheneditine) may be regulated in a
n opposite manner to AA-NAT activity.