Linked Life Data

10395089

Source:http://linkedlifedata.com/resource/pubmed/id/10395089

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pubmed-article:10395089pubmed:abstractTextHuman 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.lld:pubmed
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pubmed-article:10395089pubmed:dateRevised2007-11-15lld:pubmed
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pubmed-article:10395089pubmed:articleTitleIdentification of amino acids involved in the binding of hMIP-1 alpha to CC-CKR1, a MIP-1 alpha receptor found on neutrophils.lld:pubmed
pubmed-article:10395089pubmed:affiliationNeurobiotechnology Center, The Ohio State University, Columbus 53210, USA.lld:pubmed
pubmed-article:10395089pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:10395089pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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