| http://purl.uniprot.org/citations/10670585 | http://purl.uniprot.org/core/author | "Cristiani S."xsd:string |
| http://purl.uniprot.org/citations/10670585 | http://purl.uniprot.org/core/title | "Antimicrobial effects of alpha-MSH peptides."xsd:string |
| http://purl.uniprot.org/citations/10670585 | http://purl.uniprot.org/core/name | "J Leukoc Biol"xsd:string |
| http://purl.uniprot.org/citations/10670585 | http://purl.uniprot.org/core/volume | "67"xsd:string |
| http://purl.uniprot.org/citations/10670585 | http://purl.uniprot.org/core/author | "Cutuli M."xsd:string |
| http://purl.uniprot.org/citations/10670585 | http://purl.uniprot.org/core/author | "Catania A."xsd:string |
| http://purl.uniprot.org/citations/10670585 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/10670585 |
| http://purl.uniprot.org/citations/10670585 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10670585 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10670585 |
| http://purl.uniprot.org/citations/10670585 | http://www.w3.org/2000/01/rdf-schema#comment | "The presence of the ancient anti-inflammatory peptide alpha-melanocyte-stimulating hormone [alpha-MSH (1-13), SYSMEHFRWGKPV] in barrier organs such as gut and skin suggests a role in the nonspecific (innate) host defense. alpha-MSH and and its carboxy-terminal tripeptide (11-13, KPV) were determined to have antimicrobial influences against two major and representative pathogens: Staphylococcus aureus and Candida albicans. alpha-MSH peptides significantly inhibited S. aureus colony formation and reversed the enhancing effect of urokinase on colony formation. Antimicrobial effects occurred over a broad range of concentrations including the physiological (picomolar) range. Small concentrations of alpha-MSH peptides likewise reduced viability and germ tube formation of the yeast C. albicans. Antimicrobial influences of alpha-MSH peptides could be mediated by their capacity to increase cellular cAMP. Indeed, this messenger was significantly augmented in peptide-treated yeast and the potent adenylyl cyclase inhibitor dideoxyadenosine (ddAdo) partly reversed the killing activity of alpha-MSH peptides. Reduced killing of pathogens is a detrimental consequence of therapy with anti-inflammatory drugs. Because alpha-MSH has potent anti-inflammatory effects we determined influences of alpha-MSH on C. albicans and S. aureus killing by human neutrophils. alpha-MSH peptides did not reduce killing but rather enhanced it, likely as a consequence of the direct antimicrobial activity. alpha-MSH peptides that combine antipyretic, anti-inflammatory, and antimicrobial effects could be useful in treatment of disorders in which infection and inflammation coexist."xsd:string |
| http://purl.uniprot.org/citations/10670585 | http://purl.org/dc/terms/identifier | "doi:10.1002/jlb.67.2.233"xsd:string |
| http://purl.uniprot.org/citations/10670585 | http://purl.uniprot.org/core/date | "2000"xsd:gYear |
| http://purl.uniprot.org/citations/10670585 | http://purl.uniprot.org/core/pages | "233-239"xsd:string |
| http://purl.uniprot.org/citations/10670585 | http://purl.uniprot.org/core/author | "Lipton J.M."xsd:string |