Document Detail


Heart-type fatty acid-binding protein is a useful marker for organ dysfunction and leptin alleviates sepsis-induced organ injuries by restraining its tissue levels.
MedLine Citation:
PMID:  19576209     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Heart-type fatty acid-binding protein (H-FABP) is widely distributed and has been used to diagnose certain diseases. However, its alteration during infection-evoked organ dysfunction, and the potential association between leptin and it in injury or infection has not been investigated. In the current study, serum H-FABP, leptin, C-reactive protein and interleukin-1beta in the patients with pulmonary infection-induced multiple organ dysfunction were detected. Moreover, a mouse model of sepsis was established, and serum alanine transaminase, uric acid, tissue H-FABP, myeloperoxidase, superoxide dismutase activity and histological alterations in lung and intestine were investigated. Serum H-FABP and leptin increased simultaneously and significantly in the patients, and leptin alleviated pulmonary and intestinal injuries by restraining tissue H-FABP secretions in the mouse model of sepsis. Other investigated variables showed different but independent alterations. In conclusion, H-FABP represents a useful diagnostic marker for organ dysfunction, and its association with leptin will be a novel target for emergency aid.
Authors:
Guang-tao Yan; Ji Lin; Xiu-hua Hao; Hui Xue; Kai Zhang; Lu-huan Wang
Related Documents :
9065749 - A fluorescence displacement assay for the measurement of arachidonoyl ethanolamide (ana...
17428609 - Flavonoids and their oxidation products protect efficiently albumin-bound linoleic acid...
486509 - Thermal stability of fatty acid-serum albumin complexes studied by differential scannin...
8043989 - Effect of taurine, l-glutamine and l-histidine addition in an amino acid glucose soluti...
22055419 - Adrenal ascorbic acid depletion as an index of preslaughter stress in pigs.
20095809 - Effect of solvent on cytotoxicity and bioavailability of fatty acids.
170979 - Phosphonopyruvic acid: a probable precursor of phosphonic acids in cell-free preparatio...
18961739 - The successive determination of chloride, fluoride and sodium in single samples of orth...
3997709 - Thrombin-induced alterations in lung fluid balance in awake sheep.
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2009-07-01
Journal Detail:
Title:  European journal of pharmacology     Volume:  616     ISSN:  1879-0712     ISO Abbreviation:  Eur. J. Pharmacol.     Publication Date:  2009 Aug 
Date Detail:
Created Date:  2009-08-03     Completed Date:  2009-10-19     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  1254354     Medline TA:  Eur J Pharmacol     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  244-50     Citation Subset:  IM    
Affiliation:
Research Laboratory of Biochemistry, Basic Medical Institute, Chinese PLA General Hospital, Beijing, PR China. yan301@263.net
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Adult
Alanine Transaminase / blood
Animals
Biological Markers / blood
C-Reactive Protein / metabolism
Fatty Acid-Binding Proteins / analysis,  blood*,  metabolism*
Female
Humans
Interleukin-1beta / blood
Leptin / blood,  pharmacology*
Male
Mice
Middle Aged
Multiple Organ Failure / blood,  etiology*,  pathology*,  physiopathology
Peroxidase / blood
Rabbits
Radioimmunoassay
Reproducibility of Results
Sepsis / complications*,  metabolism
Superoxide Dismutase / blood
Uric Acid / blood
Chemical
Reg. No./Substance:
0/Biological Markers; 0/FABP3 protein, human; 0/Fatty Acid-Binding Proteins; 0/Interleukin-1beta; 0/Leptin; 69-93-2/Uric Acid; 9007-41-4/C-Reactive Protein; EC 1.11.1.7/Peroxidase; EC 1.15.1.1/Superoxide Dismutase; EC 2.6.1.2/Alanine Transaminase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Molecular cloning and characterization of dog TRPA1 and AITC stimulate the gastrointestinal motility...
Next Document:  Toxic peptides in Frazer's fraction interact with the actin cytoskeleton and affect the targeting an...