Bruton's Tyrosine Kinase (Btk) is a Binding Partner for Hypoxia Induced Mitogenic Factor (Himf/Fizz1) and Mediates Myeloid Cell Chemotaxis.
From: Department of Anesthesiology and Critical Care Medicine, Johns Hopkins University School of Medicine, 720 Rutland Ave., Baltimore, MD 21205, USA.
The FASEB journal : official publication of the Federation of American Societies for Experimental Biology
- Publish Date: May 2007
- ISSN: 1530-6860
- Volume: 21
- Issue: 7
- Pages: 1376-82
- Medium: Internet
- Language: English
- Citation (JAMA): Su Qingning, Zhou Yifu, Johns Roger A, et al. Bruton's Tyrosine Kinase (Btk) is a Binding Partner for Hypoxia Induced Mitogenic Factor (Himf/Fizz1) and Mediates Myeloid Cell Chemotaxis.. FASEB J. May 2007;21:1376-82
Abstract
Hypoxia induced mitogenic factor (HIMF) is a member of the FIZZ/resistin/RELM family of proteins that we have shown to have potent mitogenic, angiogenic, and vasoconstrictive effects in the lung vasculature. In the current report, we identified Bruton’s tyrosine kinase (BTK) as a functional HIMF binding partner through glutathione S-transferase (GST)-HIMF pull-down studies and mass spectrometry. Using primary cultured HIMF-stimulated murine bone marrow cells, we demonstrated that HIMF causes redistribution of BTK to the leading edge of the cells. HIMF stimulation induced BTK autophosphorylation, which peaked at 2.5 min. A transwell migration assay showed that treatment with recombinant murine HIMF induced migration of primary cultured bone marrow cells that was completely blocked by the BTK inhibitor, LFM-A13. Our results demonstrate BTK as the first known functional binding partner of the HIMF/FIZZ family of proteins and that HIMF acts as a chemotatic molecule in stimulating the migration of myeloid cells through activation of the BTK pathway.
Mesh Headings (Keywords): Animals, Base Sequence, Bone Marrow Cells, Cell Line, Chemotaxis, DNA Primers, Glutathione Transferase, Mass Spectrometry, Mice, Mice, Inbred C57BL, Nerve Growth Factor, Phosphorylation, Protein Binding, Protein-Tyrosine Kinases, Proteins, Recombinant Fusion Proteins, Reverse Transcriptase Polymerase Chain Reaction
Check for Full Text / PubMed Unique Identifier (PMID): 17264170
This abstract is part of PubMed, a service of the U.S. National Library of Medicine. PubMed includes more than 17 million citations from MEDLINE and other life science journals for biomedical articles. See Copyright and Disclaimers.
Linked medical terms appearing on this page are added by Healia to help readers find more information and are not part of the original PubMed document.
The data herein was last updated on July 8th, 2008 and may not reflect the most current and accurate data available from NLM.