Linked Life Data

9733783

Source:http://linkedlifedata.com/resource/pubmed/id/9733783

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
38
pubmed:dateCreated
1998-10-15
pubmed:databankReference
pubmed:abstractText
A previously undescribed human member of the cystatin superfamily called cystatin F has been identified by expressed sequence tag sequencing in human cDNA libraries. A full-length cDNA clone was obtained from a library made from mRNA of CD34-depleted cord blood cells. The sequence of the cDNA contained an open reading frame encoding a putative 19-residue signal peptide and a mature protein of 126 amino acids with two disulfide bridges and enzyme-binding motifs homologous to those of Family 2 cystatins. Unlike other human cystatins, cystatin F has 2 additional Cys residues, indicating the presence of an extra disulfide bridge stabilizing the N-terminal region of the molecule. Recombinant cystatin F was produced in a baculovirus expression system and characterized. The mature recombinant protein processed by insect cells had an N-terminal segment 7 residues longer than that of cystatin C and displayed reversible inhibition of papain and cathepsin L (Ki = 1.1 and 0.31 nM, respectively), but not cathepsin B. Like cystatin E/M, cystatin F is a glycoprotein, carrying two N-linked carbohydrate chains at positions 36 and 88. An immunoassay for quantification of cystatin F showed that blood contains low levels of the inhibitor (0.9 ng/ml). Six B cell lines in culture secreted barely detectable amounts of cystatin F, but several T cell lines and especially one myeloid cell line secreted significant amounts of the inhibitor. Northern blot analysis revealed that the cystatin F gene is primarily expressed in peripheral blood cells and spleen. Tissue expression clearly different from that of the ubiquitous inhibitor, cystatin C, was also indicated by a high incidence of cystatin F clones in cDNA libraries from dendritic and T cells, but no clones identified by expressed sequence tag sequencing in several B cell libraries and in >600 libraries from other human tissues and cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
273
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
24797-804
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:9733783-Amino Acid Sequence, pubmed-meshheading:9733783-Base Sequence, pubmed-meshheading:9733783-Cloning, Molecular, pubmed-meshheading:9733783-Cystatin C, pubmed-meshheading:9733783-Cystatins, pubmed-meshheading:9733783-DNA, Complementary, pubmed-meshheading:9733783-Databases, Factual, pubmed-meshheading:9733783-Gene Library, pubmed-meshheading:9733783-Glycoproteins, pubmed-meshheading:9733783-Glycosylation, pubmed-meshheading:9733783-Humans, pubmed-meshheading:9733783-Molecular Sequence Data, pubmed-meshheading:9733783-Molecular Weight, pubmed-meshheading:9733783-Phylogeny, pubmed-meshheading:9733783-Recombinant Proteins, pubmed-meshheading:9733783-Sequence Alignment, pubmed-meshheading:9733783-Sequence Homology, Amino Acid, pubmed-meshheading:9733783-Tumor Markers, Biological
pubmed:year
1998
pubmed:articleTitle
Cystatin F is a glycosylated human low molecular weight cysteine proteinase inhibitor.
pubmed:affiliation
Human Genome Sciences, Inc., Rockville, Maryland 20850-3338, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't