Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1999-10-28
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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0300-8177
pubmed:author
pubmed:issnType
Print
pubmed:volume
195
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
245-56
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1999
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.
pubmed:affiliation
Neurobiotechnology Center, The Ohio State University, Columbus 53210, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.