Linked Life Data

8253811

Source:http://linkedlifedata.com/resource/pubmed/id/8253811

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
35
pubmed:dateCreated
1994-1-13
pubmed:abstractText
Pulmonary surfactant protein C (SP-C) is a small hydrophobic peptide that is palmitoylated on 2 adjacent cysteine residues. SP-C enhances the adsorption of phospholipids into a monolayer. The function of the acylation is not clear yet. The experiments described in this article were carried out in order to investigate the function of SP-C acylation in (protein-catalyzed) lipid monolayer formation, and in bilayer interactions. Palmitoylated and nonpalmitoylated human recombinant SP-C were used. In addition, a nonacylated SP-C with a Cys-->Ser mutations was included in these studies. In Wilhelmy plate experiments using negatively charged, protein-containing phospholipid monolayers and negatively charged vesicles, CaCl2 was required to obtain a maximal insertion rate of lipids into the monolayer. If the negatively charged phospholipids in the monolayer were replaced by neutral phospholipids, CaCl2 was only required to show a maximal SP-C-catalyzed insertion rate (if the molecule is palmitoylated, but not if nonpalmitoylated proteins were added). In pressure area measurements, the palmitoylated protein showed a different change in pressure as a function of the surface area, as compared with the nonpalmitoylated proteins. Circular dichroism experiments showed that all three proteins had a high content of alpha-helix. All three proteins showed a preferential orientation at the air-water interface, but the palmitoylated protein has an orientation which is more parallel to the monolayer than that of the nonpalmitoylated proteins. It is concluded that acylation of SP-C alters structural and physical properties of this protein.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
268
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
26752-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Effect of acylation on structure and function of surfactant protein C at the air-liquid interface.
pubmed:affiliation
Laboratory of Veterinary Biochemistry, University of Utrecht, The Netherlands.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't