rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1-2
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pubmed:dateCreated |
1999-10-28
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pubmed:abstractText |
Human macrophage inflammatory protein-1alpha (hMIP-1alpha) and human macrophage inflammatory protein-1beta (hMIP-1beta) are chemokines involved in a diverse range of immunological effects. Both hMIP-1alpha and hMIP-1beta are involved in the activation of monocytes and THP-1 cells probably through a common receptor(s). However, only hMIP-1alpha can bind to neutrophils with high affinity, presumably through CC-CKR1 (CKR1). Since the structure of these two proteins is highly conserved, non-conserved amino acids must define the disparate binding patterns that these two proteins exhibit. Measurements of binding, chemotaxis and calcium influx conducted with hMIP-1alpha and hMIP-1beta chimeric proteins and mutants show that two amino acids (37K and 43L) are important in the binding and signaling of hMIP-1alpha through CKR1. Furthermore, we also show that mutations of the three charged amino acids at the C-terminus of hMIP-1alpha and hMIP-1beta (amino acids 61, 65 and 67), do not adversely affect the binding to THP-1 cells.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Chemokine CCL4,
http://linkedlifedata.com/resource/pubmed/chemical/Leucine,
http://linkedlifedata.com/resource/pubmed/chemical/Lysine,
http://linkedlifedata.com/resource/pubmed/chemical/Macrophage Inflammatory Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Chemokine,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/macrophage inflammatory protein...
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0300-8177
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
195
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
245-56
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:10395089-Amino Acid Sequence,
pubmed-meshheading:10395089-Amino Acids,
pubmed-meshheading:10395089-Calcium,
pubmed-meshheading:10395089-Cells, Cultured,
pubmed-meshheading:10395089-Chemokine CCL4,
pubmed-meshheading:10395089-Humans,
pubmed-meshheading:10395089-K562 Cells,
pubmed-meshheading:10395089-Leucine,
pubmed-meshheading:10395089-Lysine,
pubmed-meshheading:10395089-Macrophage Inflammatory Proteins,
pubmed-meshheading:10395089-Molecular Sequence Data,
pubmed-meshheading:10395089-Neutrophils,
pubmed-meshheading:10395089-Protein Binding,
pubmed-meshheading:10395089-Receptors, Chemokine,
pubmed-meshheading:10395089-Recombinant Fusion Proteins,
pubmed-meshheading:10395089-Recombinant Proteins,
pubmed-meshheading:10395089-U937 Cells
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pubmed:year |
1999
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pubmed:articleTitle |
Identification of amino acids involved in the binding of hMIP-1 alpha to CC-CKR1, a MIP-1 alpha receptor found on neutrophils.
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pubmed:affiliation |
Neurobiotechnology Center, The Ohio State University, Columbus 53210, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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