Abstract:
:Erythropoietin (EPO) stimulates the production of small erythroid cell stimulating factors (molecular weight <5 kDa) in cultures of bone marrow endothelial cells. We identified a fragment of thrombospondin-4 (TSP-4) as an EPO-stimulated protein in endothelial cell lysates. Pre-incubation of the low molecular weight fractions from supernatants of EPO-treated umbilical cord endothelial cells (HUVEC) with antibodies against the C-terminal residues of TSP-1,2 and TSP-4 decreased the erythroid cell stimulating activity. The C-terminal TSP-1 section corresponding to a molecular weight lower than 6 kDa has the integrin-associated protein binding motif VVM. The corresponding TSP-4 fragment, lacking the three residue sequence VVM, has a distinctive acidic peptide comprising the last 21 amino acids (C21) with the characteristics of an amphipathic helix. C21 stimulated thymidine incorporation into bovine erythroid cells, increased cell numbers in cultures of cord blood CD36+ erythroid precursors and skin fibroblasts, and decreased HUVEC proliferation. SC21, a homologous peptide of identical amino acid composition but with interchanged residues, was non-amphipathic and had no erythroid cell stimulating activity.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Congote LF,Difalco MR,Gibbs BFdoi
10.1016/j.bbrc.2004.09.107subject
Has Abstractpub_date
2004-11-12 00:00:00pages
673-8issue
2eissn
0006-291Xissn
1090-2104pii
S0006-291X(04)02160-6journal_volume
324pub_type
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