Abstract
A variety of transcriptional and post-transcriptional mechanisms regulate the expression of the inducible nitric-oxide synthase (iNOS, or NOS2). Although neurons and endothelial cells express proteins that interact with and inhibit neuronal NOS and endothelial NOS, macrophage proteins that inhibit NOS2 have not been identified. We show that murine macrophages express a 110-kDa protein that interacts with NOS2, which we call NOS- associated protein-110 kDa (NAP110). NAP110 directly interacts with the amino terminus of NOS2, and inhibits NOS catalytic activity by preventing formation of NOS2 homodimers. Expression of NAP110 may be a mechanism by which macrophages expressing NOS2 protect themselves from cytotoxic levels of nitric oxide.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 30250-30257 |
| Number of pages | 8 |
| Journal | Journal of Biological Chemistry |
| Volume | 274 |
| Issue number | 42 |
| DOIs | |
| State | Published - Oct 15 1999 |
Fingerprint
ASJC Scopus subject areas
- Biochemistry
Cite this
An inducible nitric-oxide synthase (NOS)-associated protein inhibits NOS dimerization and activity. / Ratovitski, Edward A.; Bao, Clare; Quick, Richard A.; McMillan, Audrey; Kozlovsky, Chaim; Lowenstein, Charles J.
In: Journal of Biological Chemistry, Vol. 274, No. 42, 15.10.1999, p. 30250-30257.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - An inducible nitric-oxide synthase (NOS)-associated protein inhibits NOS dimerization and activity
AU - Ratovitski, Edward A.
AU - Bao, Clare
AU - Quick, Richard A.
AU - McMillan, Audrey
AU - Kozlovsky, Chaim
AU - Lowenstein, Charles J.
PY - 1999/10/15
Y1 - 1999/10/15
N2 - A variety of transcriptional and post-transcriptional mechanisms regulate the expression of the inducible nitric-oxide synthase (iNOS, or NOS2). Although neurons and endothelial cells express proteins that interact with and inhibit neuronal NOS and endothelial NOS, macrophage proteins that inhibit NOS2 have not been identified. We show that murine macrophages express a 110-kDa protein that interacts with NOS2, which we call NOS- associated protein-110 kDa (NAP110). NAP110 directly interacts with the amino terminus of NOS2, and inhibits NOS catalytic activity by preventing formation of NOS2 homodimers. Expression of NAP110 may be a mechanism by which macrophages expressing NOS2 protect themselves from cytotoxic levels of nitric oxide.
AB - A variety of transcriptional and post-transcriptional mechanisms regulate the expression of the inducible nitric-oxide synthase (iNOS, or NOS2). Although neurons and endothelial cells express proteins that interact with and inhibit neuronal NOS and endothelial NOS, macrophage proteins that inhibit NOS2 have not been identified. We show that murine macrophages express a 110-kDa protein that interacts with NOS2, which we call NOS- associated protein-110 kDa (NAP110). NAP110 directly interacts with the amino terminus of NOS2, and inhibits NOS catalytic activity by preventing formation of NOS2 homodimers. Expression of NAP110 may be a mechanism by which macrophages expressing NOS2 protect themselves from cytotoxic levels of nitric oxide.
UR - http://www.scopus.com/inward/record.url?scp=0033569879&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0033569879&partnerID=8YFLogxK
U2 - 10.1074/jbc.274.42.30250
DO - 10.1074/jbc.274.42.30250
M3 - Article
C2 - 10514518
AN - SCOPUS:0033569879
VL - 274
SP - 30250
EP - 30257
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 42
ER -