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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
11
|
| pubmed:dateCreated |
1997-5-29
|
| pubmed:abstractText |
Psoriasin is a novel chemotactic inflammatory protein that possesses weak similarity to the S100 family members of Ca(2+)-binding proteins, and that is highly up-regulated in hyperproliferative psoriatic keratinocytes. Here we have used the psoriasin cDNA to express recombinant human (rh) psoriasin in Escherichia coli as a fusion protein containing a hexa His tag and a factor Xa cleavage site in the NH2-terminus. The protein was purified by affinity chromatography on Ni(2+)-nitrilotriacetic acid agarose, digested with factor Xa, further purified by ion-exchange chromatography and characterized by two-dimensional (2-D) gel electrophoresis and NH2-terminal sequencing. The ability of rh psoriasin to bind Ca2+, Zn2+, and Mg2+ was determined by dialysis experiments. We found that rh psoriasin may bind at least seven molecules of Ca2+ in KCl and several molecules in NaCl, with an affinity for the first bound molecule of 1.3-1.6 x 10(4) M-1. This indicates that psoriasin may cooperatively bind several molecules of Ca2+ when present in the extracellular space, or putatively, if localized in subcellular compartments where the concentration of Ca2+ is relatively high. At least eight molecules of Zn2+ were bound in KCl and four in NaCl, with an affinity just below 1 x 10(4) M-1 for the first molecule. Thus psoriasin does not bind significant amounts of Zn2+ at physiological concentrations. Mg2+ and Ca2+ are bound anti-cooperatively and binding of each of the ions (Ca2+, Zn2+, or Mg2+), is accompanied by conformational changes that move tyrosine residues to more hydrophobic areas.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cations, Divalent,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/S100 Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/S100A7 protein, human
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Nov
|
| pubmed:issn |
0173-0835
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
17
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1787-96
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:8982613-Amino Acid Sequence,
pubmed-meshheading:8982613-Base Sequence,
pubmed-meshheading:8982613-Calcium-Binding Proteins,
pubmed-meshheading:8982613-Cations, Divalent,
pubmed-meshheading:8982613-DNA, Complementary,
pubmed-meshheading:8982613-Electrophoresis, Gel, Two-Dimensional,
pubmed-meshheading:8982613-Escherichia coli,
pubmed-meshheading:8982613-Extracellular Space,
pubmed-meshheading:8982613-Humans,
pubmed-meshheading:8982613-Molecular Sequence Data,
pubmed-meshheading:8982613-Multigene Family,
pubmed-meshheading:8982613-Protein Binding,
pubmed-meshheading:8982613-Protein Denaturation,
pubmed-meshheading:8982613-Recombinant Fusion Proteins,
pubmed-meshheading:8982613-S100 Proteins,
pubmed-meshheading:8982613-Sequence Alignment,
pubmed-meshheading:8982613-Sequence Homology, Amino Acid,
pubmed-meshheading:8982613-Spectrophotometry, Ultraviolet,
pubmed-meshheading:8982613-Subcellular Fractions
|
| pubmed:year |
1996
|
| pubmed:articleTitle |
Expression and divalent cation binding properties of the novel chemotactic inflammatory protein psoriasin.
|
| pubmed:affiliation |
Department of Medical Biochemistry, University of Aarhus, Denmark.
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|