0000000001120066
AUTHOR
Masaki Nakane
Nitric oxide synthase isozymes antibodies
Three isozymes of nitric oxide synthase (NOS) have been identified, cDNAs isolated and sequenced, and antibodies produced against each isozyme. Isozyme I (found primarily in central and peripheral neuronal cells), II (in cytokine-induced cells), and III (in endothelial cells) show less than 58% identity in the deduced amino acid sequences from humans. Many investigators have produced isozyme-specific antibodies and used these antibodies to locate these proteins in various cells and tissues. NOS-I is constitutively expressed, and the enzymatic activity is regulated by Ca2+ and calmodulin. The anti-NOS-I antibodies have allowed investigators to characterize non-adrenergic non-cholinergic neur…
[26] Isoforms of nitric-oxide synthase: Purification and regulation
Publisher Summary Nitric-oxide synthase (NOS) catalyzes the five-electron oxidation of L-arginine to the nitric oxide radical (.NO) and L-citrulline. Molecular oxygen is the cosubstrate of the enzyme. NO synthase activity has been found in a large variety of cells and tissues. The enzyme exists in several isoforms, three of which have been purified, characterized, and cloned. The activities of all three isoforms are found distributed between the soluble and particulate fractions of cells. Isoform I (from brain) and isoform II (from cytokine-induced macrophages) are mostly soluble proteins. Isoform III from endothelial cells is myristoylated and found predominantly in the particulate fractio…
Inducible NO synthase II and neuronal NO synthase I are constitutively expressed in different structures of guinea pig skeletal muscle: implications for contractile function
The expression of NOS isoforms was studied in guinea pig skeletal muscle at the mRNA and protein level, and the effect of NO on contractile response was examined. Ribonuclease protection analyses demonstrated NOS I and NOS II mRNAs in diaphragm and gastrocnemius muscle. In Western blots, NOS I and NOS II immunoreactivities were found in the particulate but not the soluble fraction of skeletal muscle. NOS activity was found almost exclusively in the particulate fraction. About 50% of this activity was Ca2+ independent. In immunohistochemistry, the anti-NOS I antibody stained distinct membrane regions of muscle fibers. The most intense staining was seen in neuromuscular endplates identified b…