Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C0406810 (NAME)
 13,345 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The effects of interactions between N-methyl-D-aspartate (NMDA) and nitric oxide on ultrasonic vocalizations, motor activity and body temperature was investigated in 9-10-day-old rat pups. The competitive NMDA receptor antagonist, 3-((+/-)-2-carboxypiperazin-4-yl)-propyl-1-phosphonic acid (CPP), and the nitric oxide synthase inhibitor, nitro-L-arginine-methyl ester (L-NAME), decreased the emission of ultrasonic vocalizations while NMDA and the nitric oxide precursor, L-arginine, produced a trend toward increased emission of ultrasonic vocalizations. CCP also attenuated the geotaxic response. Co-administration of CPP with L-NAME virtually abolished the emission of ultrasonic vocalizations and the ability to show the geotaxic response while co-administration of NMDA with L-arginine increased the emission of ultrasonic vocalizations and decreased body temperature with no effect on the geotaxic response. NMDA and L-arginine reversed the effects of L-NAME, but not of CPP, on ultrasonic vocalizations. L-arginine but not NMDA antagonized the effect of CPP on the geotaxic response. Our results confirmed the functional coupling between NMDA receptor activation and nitric oxide in modulating anxiety-like behavior and motor coordination in infant rats.
 ...
PMID:Interactions between N-methyl-D-aspartate and nitric oxide in the modulation of ultrasonic vocalizations of infant rats. 1109 Jun 43

The enzyme nitric oxide synthase (NOS) oxidizes L-arginine to NO and citrulline. In this work, we characterise the NOS from the cyanobacteria Synechococcus PCC 7335 (SyNOS). SyNOS possesses a canonical mammalian NOS architecture consisting of oxygenase and reductase domains. In addition, SyNOS possesses an unusual globin domain at the N-terminus. Recombinant SyNOS expressed in bacteria is active, and its activity is suppressed by the NOS inhibitor L-NAME. SyNOS allows E. coli to grow in minimum media containing L-arginine as the sole N source, and has a higher growth rate during N deficiency. SyNOS is expressed in Synechococcus PCC 7335 where NO generation is dependent on L-arginine concentration. The growth of Synechococcus is dramatically inhibited by L-NAME, suggesting that SyNOS is essential for this cyanobacterium. Addition of arginine in Synechococcus increases the phycoerythrin content, an N reservoir. The role of the novel globin domain in SyNOS is discussed as an evolutionary advantage, conferring new functional capabilities for N metabolism.
 ...
PMID:A singular nitric oxide synthase with a globin domain found in Synechococcus PCC 7335 mobilizes N from arginine to nitrate. 3013 3