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PMID: 9531587 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

New insights into the negative regulation of hematopoiesis by chemokine platelet factor 4 and related peptides.

Blood ·Vol. 91 ·No. 8 ·1998-04-15 ·Pages 2772-80

Lecomte-Raclet L, Alemany M, Sequira-Le Grand A, Amiral J, Quentin G, Vissac AM, Caen JP, Han ZC

Abstract

Platelet factor 4 (PF4) has been recognized as an inhibitor of myeloid progenitors. However, the mechanism of action of this chemokine remains poorly understood. The present study was designed to determine its structure/function relationship. A series of peptides overlapping the C-terminal and central regions of PF4 were analyzed in vitro for their action on murine hematopoietic progenitor growth to assess the minimal sequence length required for activity. The peptides p17-58 and p34-58 possessed an increased hematopoietic inhibitory activity when compared with PF4, whereas the shorter peptides p47-58 and p47-70 were equivalent to the native molecule and the peptide p58-70 was inactive. The PF4 functional motif DLQ located in 54-56 was required for the activity of these peptides. The peptide p34-58 impaired to a similar extent the growth of colony-forming unit-megakaryocyte (CFU-MK) as well as burst-forming unit-erythroid (BFU-E) and colony-forming unit-granulocyte-macrophage (CFU-GM), whereas PF4 was more active on CFU-MK. In the experiments using purified murine CD34(+) marrow cells, statistically significant inhibition induced by p34-58 was shown at concentrations of 2.2 nmol/L or greater for progenitors of the three lineages, whereas that induced by PF4 was seen at 130 nmol/L for CFU-MK and 650 nmol/L for CFU-GM and BFU-E, indicating that the p34-58 acts directly on hematopoietic progenitors and its activity is approximately 60- to 300-fold higher than PF4. The p34-58, unlike PF4, lacked affinity for heparin and its inhibitory activity could not be abrogated by the addition of heparin. In addition, an antibody recognizing p34-58 neutralized the activity of p34-58 but not whole PF4 molecule. These results demonstrate that PF4 contains a functional domain in its central region, which is independent of the heparin binding properties, and provide evidence for a model of heparin-dependent and independent pathways of PF4 in inhibiting hematopoiesis.

MeSH Terms
Amino Acid Sequence Animals Cells, Cultured Coagulants/chemistry,pharmacology Hematopoiesis/drug effects Mice Mice, Inbred BALB C Molecular Sequence Data Peptides/chemistry,pharmacology Platelet Factor 4/chemistry,pharmacology Structure-Activity Relationship
Chemicals
Coagulants Peptides Platelet Factor 4
Authors & Affiliations
8 authors, click to expand affiliations / ORCID
Lecomte-Raclet L
Institut des Vaisseaux et du Sang, Hôpital Lariboisière, Paris, France.
Alemany M
Sequira-Le Grand A
Amiral J
Quentin G
Vissac A M
Caen J P
Han Z C
Article Info
Journal
Blood
Abbr.
Blood
ISSN
0006-4971
Published
1998-04-15
Pages
2772-80
Language
English
Region
United States
NLM ID
7603509
Subset
IM
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