Linked Life Data

7642568

Source:http://linkedlifedata.com/resource/pubmed/id/7642568

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
32
pubmed:dateCreated
1995-9-18
pubmed:abstractText
Surfactant protein D (SP-D) is a member of the C-type lectin superfamily with four distinct structural domains: an amino terminus involved in forming intermolecular disulfides, a collagen-like domain, a neck region, and a carbohydrate recognition domain. A collagen domain deletion mutant (CDM) of SP-D was created by site-directed mutagenesis. A second variant lacking both the amino-terminal region and the collagen-like domain was generated by collagenase treatment and purification of the collagenase-resistant fragment (CRF). The CDM expressed in CHO-K1 cells formed the covalent trimers, but not the noncovalent dodecamers, typical of native SP-D. The CRF derived from recombinant SP-D formed only monomers. The CDM bound mannose-Sepharose and phosphatidylinositol (PI) as well as SP-D, but the binding to mannosyl bovine serum albumin and glucosylceramide was diminished by approximately 60%. The CRF displayed weak binding to mannose-Sepharose and PI and essentially no binding to mannosyl bovine serum albumin and glucosylceramide. Both SP-D and CDM altered the self-aggregation of PI-containing liposomes. SP-D reduced the density and the light scattering properties of PI aggregates. These results demonstrate that the collagen-like domain is required for dodecamer but not covalent trimer formation of SP-D and plays an important, but not essential, role in the interaction of SP-D with PI and GlcCer. Removal of the amino-terminal domain of SP-D along with the collagen-like domain diminishes PI binding and effectively eliminates GlcCer binding.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
11
pubmed:volume
270
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
19052-8
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
The role of the amino-terminal domain and the collagenous region in the structure and the function of rat surfactant protein D.
pubmed:affiliation
Lord and Taylor Laboratory for Lung Biochemistry, National Jewish Center for Immunology and Respiratory Medicine, Denver, Colorado 80206, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.