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A carboxyl terminal truncation mutant of CD36 is secreted and binds
thrombospondin: evidence for a single transmembrane domain
SF Pearce, J Wu and RL Silverstein
Department of Medicine, Cornell University Medical College, New York, NY
10021.
CD36 has been implicated in several intracellular signalling events,
including platelet and monocyte activation, and receptor-mediated
internalization of bound ligands such as oxidized low-density lipoprotein
and apoptotic neutrophils. These processes are presumably mediated by the
intracytoplasmic domain(s) of the molecule. By analysis of hydrophobicity
plots and by analogy to rat LIMPII, which has a 60% homology to CD36, a
two-transmembrane domain model has been proposed. To characterize the
structure-function relationships of CD36 involved in transducing the
signal, we have defined the number of transmembrane and intracellular
domains experimentally using a mutagenesis approach. A truncated CD36 cDNA
was constructed that encodes a protein that terminates just proximal to the
putative C-terminal transmembrane domain. This mutant was cloned into
eukaryotic expression plasmid vectors to generate short-term and stable
transfected cells. Our results indicate that the truncated mutant is
secreted by the transfectants into the postculture medium, indicating that
there is only one transmembrane domain in CD36, which is present at the C-
terminal end. The soluble secreted protein from all of these cells is
functional as indicated by its binding to thrombospondin.
Volume 84,
Issue 2,
pp. 384-389,
07/15/1994
Copyright © 1994 by The American Society of Hematology
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