Source:http://linkedlifedata.com/resource/pubmed/id/14675208
Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
6
|
| pubmed:dateCreated |
2003-12-16
|
| pubmed:abstractText |
Within the past years, an important role for nitric oxide (NO) in skin repair has been well defined. As NO is synthesized from L-arginine by NO synthases (NOS), the availability of L-arginine might be one rate-limiting factor of NO production at the wound site. Upon injury, arginase-1 and -2 mRNA, protein, and activity were strongly induced reaching a maximum between day 3 and day 7 postwounding. Immunohistochemistry colocalized both arginases and the inducible NOS (iNOS) at epithelial sites at the margins of the wound. Notably, diabetes-impaired skin repair in leptin-deficient mice (diabetes/diabetes, db/db; and obese/obese, ob/ob) was characterized by an abnormally elevated arginase activity in wound tissue in the absence of an expression of iNOS. Expression analyses demonstrated that arginase-1 contributed to increased arginase activities in impaired repair. Interestingly, an improved healing of chronic wound situations in leptin-supplemented ob/ob mice was strongly associated with an adjustment of the dysregulated expression of L-arginine-converting enzymes: an attenuated iNOS expression was upregulated early in repair and an augmented arginase-1 expression and activity was downregulated in the presence of markedly elevated numbers of macrophages during late repair. These data suggest a coordinated consumption of L-arginine by the NOS and arginase enzymatic pathways at the wound site as a prerequisite for a balanced NO (via iNOS) and polyamine (via arginases) synthesis that drives a normal skin repair.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Arginase,
http://linkedlifedata.com/resource/pubmed/chemical/Arginine,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Leptin,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide Synthase,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide Synthase Type II,
http://linkedlifedata.com/resource/pubmed/chemical/Nos2 protein, mouse
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Dec
|
| pubmed:issn |
0022-202X
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
121
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1544-51
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:14675208-Animals,
pubmed-meshheading:14675208-Arginase,
pubmed-meshheading:14675208-Arginine,
pubmed-meshheading:14675208-Chronic Disease,
pubmed-meshheading:14675208-Diabetes Complications,
pubmed-meshheading:14675208-Diabetes Mellitus,
pubmed-meshheading:14675208-Female,
pubmed-meshheading:14675208-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:14675208-Isoenzymes,
pubmed-meshheading:14675208-Leptin,
pubmed-meshheading:14675208-Mice,
pubmed-meshheading:14675208-Mice, Inbred BALB C,
pubmed-meshheading:14675208-Mice, Inbred C57BL,
pubmed-meshheading:14675208-Mice, Mutant Strains,
pubmed-meshheading:14675208-Nitric Oxide Synthase,
pubmed-meshheading:14675208-Nitric Oxide Synthase Type II,
pubmed-meshheading:14675208-Skin,
pubmed-meshheading:14675208-Wound Healing
|
| pubmed:year |
2003
|
| pubmed:articleTitle |
Expression and activity of arginase isoenzymes during normal and diabetes-impaired skin repair.
|
| pubmed:affiliation |
Pharmazentrum Frankfurt, Klinikum der Johann Wolfgang Goethe-Universität, Frankfurt am Main, Germany.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|