Source:http://linkedlifedata.com/resource/pubmed/id/18407667
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
18
|
pubmed:dateCreated |
2008-4-30
|
pubmed:abstractText |
Surfactant protein A (SP-A), a member of the collectin family that modulates innate immunity, has recently been involved in the physiology of reproduction. Consistent with the activation of ERK-1/2 and COX-2 induced by SP-A in myometrial cells, we reported previously the presence of two major proteins recognized by SP-A in these cells. Here we identify by mass spectrometry one of these SP-A targets as the intermediate filament (IF) desmin. In myometrial preparations derived from desmin-deficient mice, the absence of binding of SP-A to any 50 kDa protein confirmed the identity of this SP-A-binding site as desmin. Our data based on partial chymotrypsin digestion of pure desmin suggested that SP-A recognizes especially its rod domain, which is known to play an important role during the assembly of desmin into filaments. In line with that, electron microscopy experiments showed that SP-A inhibits in vitro the polymerization of desmin filaments. SP-A also recognized in vitro polymerized filaments in a calcium-dependent manner at a physiological ionic strength but not the C1q receptor gC1qR. Furthermore, Texas Red-labeled SP-A colocalized with desmin filaments in myometrial cells. Interestingly, vimentin, the IF characteristic of leukocytes, is one of the major proteins recognized by SP-A in protein extracts of U937 cells after PMA-induced differentiation of this monocytic cell line. Interaction of SP-A with vimentin was further confirmed using recombinant vimentin in solid-phase binding assays. The ability of SP-A to interact with desmin and vimentin, and to prevent polymerization of desmin monomers, shed light on unexpected and wider biological roles of this collectin.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Extracts,
http://linkedlifedata.com/resource/pubmed/chemical/Desmin,
http://linkedlifedata.com/resource/pubmed/chemical/Pulmonary Surfactant-Associated...,
http://linkedlifedata.com/resource/pubmed/chemical/Vimentin
|
pubmed:status |
MEDLINE
|
pubmed:month |
May
|
pubmed:issn |
1520-4995
|
pubmed:author | |
pubmed:issnType |
Electronic
|
pubmed:day |
6
|
pubmed:volume |
47
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
5127-38
|
pubmed:meshHeading |
pubmed-meshheading:18407667-Animals,
pubmed-meshheading:18407667-Calcium,
pubmed-meshheading:18407667-Cell Extracts,
pubmed-meshheading:18407667-Cells, Cultured,
pubmed-meshheading:18407667-Desmin,
pubmed-meshheading:18407667-Humans,
pubmed-meshheading:18407667-Intermediate Filaments,
pubmed-meshheading:18407667-Mice,
pubmed-meshheading:18407667-Mice, Inbred C57BL,
pubmed-meshheading:18407667-Mice, Knockout,
pubmed-meshheading:18407667-Microscopy, Electron,
pubmed-meshheading:18407667-Osmolar Concentration,
pubmed-meshheading:18407667-Protein Binding,
pubmed-meshheading:18407667-Pulmonary Surfactant-Associated Protein A,
pubmed-meshheading:18407667-Rats,
pubmed-meshheading:18407667-Tandem Mass Spectrometry,
pubmed-meshheading:18407667-Vimentin
|
pubmed:year |
2008
|
pubmed:articleTitle |
Interaction of surfactant protein A with the intermediate filaments desmin and vimentin.
|
pubmed:affiliation |
Institut de Biochimie et Biophysique Moléculaire et Cellulaire, UMR-8619 du CNRS, Université de Paris-Sud, 91400 Orsay, France. ignaciogarciaverdugo@yahoo.com
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|