Increased tryptophan decarboxylase and monoamine oxidase activities induce Sekiguchi lesion formation in rice infected with Magnaporthe grisea.

Sekiguchi lesion (sl)-mutant rice infected with Magnaporthe grisea showed increased light-dependent tryptophan decarboxylase (TDC) and monoamine oxidase (MAO) activities. TDC and MAO activities were observed before the penetration of M. grisea to rice cells and maintained high levels even after Sekiguchi lesion formation. Light-dependent expression of TDC gene was observed in leaves inoculated with M. grisea before Sekiguchi lesion formation. Spore germination fluid (SGF) of M. grisea also induced Sekiguchi lesion formation accompanied by increased enzymes activities and tryptamine accumulation. Sekiguchi lesion was also induced by treatments with tryptamine and beta-phenylethylamine, which are substrates for MAO, but was not induced by non-substrates such as indole-3-propionic acid, (+/-)-phenylethylamine and tryptophan under light. Light-dependent induction of Sekiguchi lesion by tryptamine was significantly inhibited in the presence of MAO inhibitors, metalaxyl and semicarbazide, and H2O2-scavengers, ascorbic acid and catalase. H2O2 in M. grisea-infected leaves with and without Sekiguchi lesions was demonstrated directly in situ by strong 3,3'-diaminobenzidine (DAB) staining. On the other hand, H2O2 induced Sekiguchi lesions on leaves of cv. Sekiguchi-asahi under light, but not in darkness. This difference was associated with the decrease of catalase activity in infected leaves under light and the absence of decrease in darkness. We hypothesize that the H2O2-induced breakdown of cellular organelles such as chloroplasts and mitochondria in mesophyll cells may cause high TDC and MAO activities and the development of Sekiguchi lesion, and that the sl gene products in wild-type rice may function as a suppressor of organelle breakdown caused by chemical or environmental stress.

Short-photoperiod exposure reduces L-aromatic-amino-acid decarboxylase immunostaining in the arcuate nucleus and median eminence of male Syrian hamsters.

In male hamsters, exposure to short photoperiod (SD) results in a decrease in median eminence and posterior pituitary dopamine (DA) concentrations. To determine if the SD-induced decline in DA is due to a decrease in the number of neurons synthesizing DA, immunocytochemistry was used to identify cells containing tyrosine hydroxylase (TH) and L-aromatic amino acid decarboxylase (AADC) in animals housed under long photoperiod (LD) or SD. Immunopositive cells were counted in the arcuate and caudal periventricular nuclei, regions where the DA neurons that project to the median eminence and posterior pituitary are located. AADC immunopositive (AADC +) cells were also counted in the median eminence. Photoperiod did not affect the number of TH immunopositive (TH+) or AADC + cells in the caudal periventricular nuclei. In the arcuate nuclei, SD exposure did not affect the number of TH+ neurons, but produced a significant decline in the number of AADC + cells. The number of AADC + cells was also reduced in the median eminence of SD-exposed animals. This decline in AADC+ cells may play a role in SD-induced changes in hypothalamic regulation of anterior pituitary hormone release, including the decline in median eminence DA concentrations.

Aromatic L-amino acid decarboxylase activity of the rat retina is modulated in vivo by environmental light.

Aromatic L-amino acid decarboxylase (AAAD) activity of rat retina is low in animals placed in the dark. When the room lights are turned on, activity rises for almost 3 h and reaches values that are about twice the values found in the dark. A study of the kinetics of the enzyme revealed that the apparent Km values for L-3,4-dihydroxyphenylalanine and pyridoxal-5'-phosphate were unchanged in light- and dark-exposed animals, whereas the Vmax increased in the light. Treating the animals with cycloheximide before exposure to light prevented the increase of enzyme activity. Immunotitration with antibodies to AAAD suggested that more enzyme molecules are present in the light than in the dark. When the room lights are turned off AAAD activity drops rapidly at first and then more slowly, suggesting that at least two processes are responsible for the fall of enzyme activity. Exposure to short periods of dark followed by light results in a rapid increase of AAAD activity. Mixing homogenates from light- and dark-exposed rats results in activity values that are less than expected, suggesting the presence of an endogenous inhibitor(s). These studies demonstrate that AAAD activity is modulated in vivo.

Dye-sensitized photo-oxidation of pig kidney Dopa decarboxylase.

The effects of irradiation of pig kidney Dopa decarboxylase by visible light absorbed by the intrinsic chromophore, pyridoxal-P, and by the externally added dyes, pyridoxal-P or proflavin, have been studied. In all cases inactivation was observed, even though to different extens, which seemed to be essentially correlated to tryptophanyl residues photodestruction. Kinetics of inactivation and oxidation of these amino acid residues revealed the presence of two distinct groups of tryptophan residues with different photooxidation rate constants. A different role for these classes of residues in the structure and function of Dopa decarboxylase has been suggested.