By C. Nathan (auth.), Hilary Koprowski, Hiroshi Maeda (eds.)
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Additional resources for The Role of Nitric Oxide in Physiology and Pathophysiology
Example text
From AKAIKE et al. 1993, with permission) 42 H. Maeda et al. 59~ 5 min Ach '-I ~ ~ r~ d t L-Arginine PE NNA Fig. 5a-d. Effects of imidazolineoxyl N-oxide (PTlO) on acetylcholine (Ach) induced vasorelaxation of rabbit thoracic aorta. 0 mM with or without PTIO and PT/. a Control without PTIO; b with 300 11M PTIO; c with 300 11M PTI; d effect of L-arginine (5 mMJ on inhibition by 100 11M PTIO (upper tracing) or 100 11M N"'-nitro-L-arginine (NNA) (lower tracing) of Achinduced vasorelaxation. (From AKAIKE et al.
In fact, reports by MORRIS and HANSEN firmly establish that the antimicrobial action of RS-NO results from covalent modification of bacterial membrane sulfhydryl groups (MORRIS et al. 1984; MORRIS and HANSEN 1981), and direct inhibition of sulfhydryl-dependent enzymes, such as glyceraldehyde phosphate dehydrogenase, may further contribute to their bacteriostatic activity (O'LEARY and SOLBERG 1976). Moreover, cell impermeable RS-NO potently inhibits S-Nitrosothiols and the Bioregulatory Actions of Nitrogen Oxides 25 growth of the malarial parasite, Plasmodium falciparum, whereas a saturated solution of NO' does not (ROCKETT et al.
1994), the latter event also associated with an ADP-ribosylation-like modification (MOLINA Y VEDIA et al. 1992; STAMLER 1994) in vivo. Studies on the mechanism of GAPDH modification reveal that S-nitrosylation of an active site thiol is requisite for subsequent modification by nicotine adenine dinucleotide phosphate (NAD+) (MOHR et al. 1994). Thus, the formation of protein RS-NO serves a catalytic function. Interestingly, the S-NO intermediate of GAPDH formed during labelling with NAD is devoid of enzymatic activity (MOLINA Y VEDIA et al.