Abstract
We isolated a new chemotactic protein from bovine lung, and its partial protein sequence analysis indicated that this protein was identical with S100L, one member of the Ca2+-binding S100 protein family. The chemotactic activity of S100L on guinea pig eosinophils is observed at 0.1nM protein concentration, and the effects appear mediated by a novel specific surface receptor. We characterized the receptor for S100L on guinea pig eosinophils. Scatchard analyses of the data that [125I]S100L bound to S100L receptor indicate the presence of two receptor populations on eosinophils with a Kd value of 3.3 x 10(-11)M and 1.1 x 10(-9)M. Thus, S100L protein has the most potent chemotactic activity on guinea pig eosinophils of all the chemotactic proteins.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Brain / metabolism
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Cattle
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Chemotactic Factors / isolation & purification
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Chemotactic Factors / metabolism*
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Chemotactic Factors / pharmacology*
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Chemotaxis, Leukocyte* / drug effects
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Eosinophils / drug effects
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Eosinophils / physiology*
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Guinea Pigs
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Kinetics
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Lung / metabolism
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Myocardium / metabolism
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Receptors, Formyl Peptide
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Receptors, Immunologic / drug effects
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Receptors, Immunologic / metabolism
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Receptors, Immunologic / physiology*
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Receptors, Peptide / drug effects
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Receptors, Peptide / metabolism
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Receptors, Peptide / physiology*
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S100 Proteins / isolation & purification
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S100 Proteins / metabolism*
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S100 Proteins / pharmacology*
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Substrate Specificity
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Swine
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Virulence Factors, Bordetella / pharmacology
Substances
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Chemotactic Factors
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Receptors, Formyl Peptide
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Receptors, Immunologic
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Receptors, Peptide
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S100 Proteins
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S100A2 protein, human
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Virulence Factors, Bordetella