Source:http://linkedlifedata.com/resource/pubmed/id/14525775
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7
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pubmed:dateCreated |
2004-3-22
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pubmed:abstractText |
The chemokine stromal-derived factor-1 (SDF-1), which is constitutively expressed in most tissues as SDF-1alpha and SDF-1beta resulting from alternative gene splicing, regulates hematopoiesis, lymphocyte homing, B-lineage cell growth, and angiogenesis. Because SDF-1alpha and SDF-1beta are constitutively and ubiquitously expressed, their degradation must serve an important regulatory role. Here we show that SDF-1alpha and SDF-1beta are secreted as full-length molecules. When exposed to human serum, full-length SDF-1alpha (1-68) undergoes processing first at the COOH terminus to produce SDF-1alpha 1-67 and then at the NH2 terminus to produce SDF-1alpha 3-67. By contrast, full-length SDF-1beta (1-72) is processed only at the NH2 terminus to produce SDF-1beta 3-72. CD26/dipeptidyl peptidase is responsible for serum cleavage of SDF-1alpha and SDF-1beta at the NH2 terminus. Serum processing of SDF-1alpha at the COOH terminus, which has not been previously reported, reduces the ability of the polypeptide to bind to heparin and to cells and to stimulate B-cell proliferation and chemotaxis. The additional processing at the NH2 terminus renders both forms of SDF-1 unable to bind to heparin and to activate cells. The differential processing of SDF-1alpha and SDF-1beta provides biologic significance to the existence of 2 splice forms of the chemokine and adds a tool to precisely regulate SDF-1's biologic activity by changes in specific activity.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/CXCL12 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Chemokine CXCL12,
http://linkedlifedata.com/resource/pubmed/chemical/Chemokines, CXC,
http://linkedlifedata.com/resource/pubmed/chemical/Cytokines,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0006-4971
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
103
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2452-9
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:14525775-Alternative Splicing,
pubmed-meshheading:14525775-Cell Line,
pubmed-meshheading:14525775-Chemokine CXCL12,
pubmed-meshheading:14525775-Chemokines, CXC,
pubmed-meshheading:14525775-Cytokines,
pubmed-meshheading:14525775-Endothelium, Vascular,
pubmed-meshheading:14525775-Flow Cytometry,
pubmed-meshheading:14525775-Gene Expression Regulation,
pubmed-meshheading:14525775-Genetic Variation,
pubmed-meshheading:14525775-Humans,
pubmed-meshheading:14525775-Kinetics,
pubmed-meshheading:14525775-Recombinant Proteins,
pubmed-meshheading:14525775-Sequence Deletion,
pubmed-meshheading:14525775-Spectrometry, Mass, Electrospray Ionization,
pubmed-meshheading:14525775-Umbilical Veins
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pubmed:year |
2004
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pubmed:articleTitle |
Differential processing of stromal-derived factor-1alpha and stromal-derived factor-1beta explains functional diversity.
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pubmed:affiliation |
Experimental Transplantation and Immunology Branch, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.
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pubmed:publicationType |
Journal Article
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