Expression and tyrosine phosphorylation of Cbl regulates macrophage chemokinetic and chemotactic movement

Elena Caveggion, Silvia Continolo, Fiona J. Pixley, E. Richard Stanley, David D L Bowtell, Clifford A. Lowell, Giorgio Berton

Research output: Contribution to journalArticle

38 Citations (Scopus)

Abstract

Primary macrophages isolated from hck-/-fgr-/- mice display altered morphology and F-actin cytoskeletal structures and reduced migration. The ability of phorbol myristyl acetate (PMA), a protein kinase C activator that has been reported to increase macrophage spreading and carcinoma cell motility, to rescue these hck-/- fgr-/- defects was tested. Although PMA-treated wild-type and hck-/-fgr-/- macrophages exhibited a similar flattened, spread phenotype, PMA did not rescue the hck-/-fgr-/- macrophage migration defect. Instead, both PMA-treated wild type and hck-/-fgr-/- macrophages were defective in spontaneous and chemotactic migration and tyrosine phosphorylation of the Cbl protooncoprotein was decreased in both. Moreover, c-cbl-/- macrophages displayed the same impairment of motility as hck-/-fgr-/- macrophages and a similar morphology with less polarization and more dorsal ruffling than wild-type macrophages. As Hck and Fgr expression and activity were not decreased in c-cbl-/- macrophages, these results suggest that Cbl is likely to be an important downstream mediator of the Src family kinase-regulated macrophage motility pathway.

Original languageEnglish (US)
Pages (from-to)276-289
Number of pages14
JournalJournal of Cellular Physiology
Volume195
Issue number2
DOIs
StatePublished - May 1 2003

Fingerprint

Phosphorylation
Macrophages
Tyrosine
Acetates
Defects
src-Family Kinases
Protein Kinase C
Cell Movement
Actins
Cells
Polarization
Carcinoma
Phenotype

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Cell Biology
  • Physiology

Cite this

Caveggion, E., Continolo, S., Pixley, F. J., Stanley, E. R., Bowtell, D. D. L., Lowell, C. A., & Berton, G. (2003). Expression and tyrosine phosphorylation of Cbl regulates macrophage chemokinetic and chemotactic movement. Journal of Cellular Physiology, 195(2), 276-289. https://doi.org/10.1002/jcp.10236

Expression and tyrosine phosphorylation of Cbl regulates macrophage chemokinetic and chemotactic movement. / Caveggion, Elena; Continolo, Silvia; Pixley, Fiona J.; Stanley, E. Richard; Bowtell, David D L; Lowell, Clifford A.; Berton, Giorgio.

In: Journal of Cellular Physiology, Vol. 195, No. 2, 01.05.2003, p. 276-289.

Research output: Contribution to journalArticle

Caveggion, E, Continolo, S, Pixley, FJ, Stanley, ER, Bowtell, DDL, Lowell, CA & Berton, G 2003, 'Expression and tyrosine phosphorylation of Cbl regulates macrophage chemokinetic and chemotactic movement', Journal of Cellular Physiology, vol. 195, no. 2, pp. 276-289. https://doi.org/10.1002/jcp.10236
Caveggion, Elena ; Continolo, Silvia ; Pixley, Fiona J. ; Stanley, E. Richard ; Bowtell, David D L ; Lowell, Clifford A. ; Berton, Giorgio. / Expression and tyrosine phosphorylation of Cbl regulates macrophage chemokinetic and chemotactic movement. In: Journal of Cellular Physiology. 2003 ; Vol. 195, No. 2. pp. 276-289.
@article{624fe87687ba47fca43694b9cb51df91,
title = "Expression and tyrosine phosphorylation of Cbl regulates macrophage chemokinetic and chemotactic movement",
abstract = "Primary macrophages isolated from hck-/-fgr-/- mice display altered morphology and F-actin cytoskeletal structures and reduced migration. The ability of phorbol myristyl acetate (PMA), a protein kinase C activator that has been reported to increase macrophage spreading and carcinoma cell motility, to rescue these hck-/- fgr-/- defects was tested. Although PMA-treated wild-type and hck-/-fgr-/- macrophages exhibited a similar flattened, spread phenotype, PMA did not rescue the hck-/-fgr-/- macrophage migration defect. Instead, both PMA-treated wild type and hck-/-fgr-/- macrophages were defective in spontaneous and chemotactic migration and tyrosine phosphorylation of the Cbl protooncoprotein was decreased in both. Moreover, c-cbl-/- macrophages displayed the same impairment of motility as hck-/-fgr-/- macrophages and a similar morphology with less polarization and more dorsal ruffling than wild-type macrophages. As Hck and Fgr expression and activity were not decreased in c-cbl-/- macrophages, these results suggest that Cbl is likely to be an important downstream mediator of the Src family kinase-regulated macrophage motility pathway.",
author = "Elena Caveggion and Silvia Continolo and Pixley, {Fiona J.} and Stanley, {E. Richard} and Bowtell, {David D L} and Lowell, {Clifford A.} and Giorgio Berton",
year = "2003",
month = "5",
day = "1",
doi = "10.1002/jcp.10236",
language = "English (US)",
volume = "195",
pages = "276--289",
journal = "Journal of Cellular Physiology",
issn = "0021-9541",
publisher = "Wiley-Liss Inc.",
number = "2",

}

TY - JOUR

T1 - Expression and tyrosine phosphorylation of Cbl regulates macrophage chemokinetic and chemotactic movement

AU - Caveggion, Elena

AU - Continolo, Silvia

AU - Pixley, Fiona J.

AU - Stanley, E. Richard

AU - Bowtell, David D L

AU - Lowell, Clifford A.

AU - Berton, Giorgio

PY - 2003/5/1

Y1 - 2003/5/1

N2 - Primary macrophages isolated from hck-/-fgr-/- mice display altered morphology and F-actin cytoskeletal structures and reduced migration. The ability of phorbol myristyl acetate (PMA), a protein kinase C activator that has been reported to increase macrophage spreading and carcinoma cell motility, to rescue these hck-/- fgr-/- defects was tested. Although PMA-treated wild-type and hck-/-fgr-/- macrophages exhibited a similar flattened, spread phenotype, PMA did not rescue the hck-/-fgr-/- macrophage migration defect. Instead, both PMA-treated wild type and hck-/-fgr-/- macrophages were defective in spontaneous and chemotactic migration and tyrosine phosphorylation of the Cbl protooncoprotein was decreased in both. Moreover, c-cbl-/- macrophages displayed the same impairment of motility as hck-/-fgr-/- macrophages and a similar morphology with less polarization and more dorsal ruffling than wild-type macrophages. As Hck and Fgr expression and activity were not decreased in c-cbl-/- macrophages, these results suggest that Cbl is likely to be an important downstream mediator of the Src family kinase-regulated macrophage motility pathway.

AB - Primary macrophages isolated from hck-/-fgr-/- mice display altered morphology and F-actin cytoskeletal structures and reduced migration. The ability of phorbol myristyl acetate (PMA), a protein kinase C activator that has been reported to increase macrophage spreading and carcinoma cell motility, to rescue these hck-/- fgr-/- defects was tested. Although PMA-treated wild-type and hck-/-fgr-/- macrophages exhibited a similar flattened, spread phenotype, PMA did not rescue the hck-/-fgr-/- macrophage migration defect. Instead, both PMA-treated wild type and hck-/-fgr-/- macrophages were defective in spontaneous and chemotactic migration and tyrosine phosphorylation of the Cbl protooncoprotein was decreased in both. Moreover, c-cbl-/- macrophages displayed the same impairment of motility as hck-/-fgr-/- macrophages and a similar morphology with less polarization and more dorsal ruffling than wild-type macrophages. As Hck and Fgr expression and activity were not decreased in c-cbl-/- macrophages, these results suggest that Cbl is likely to be an important downstream mediator of the Src family kinase-regulated macrophage motility pathway.

UR - http://www.scopus.com/inward/record.url?scp=0037401969&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0037401969&partnerID=8YFLogxK

U2 - 10.1002/jcp.10236

DO - 10.1002/jcp.10236

M3 - Article

C2 - 12652654

AN - SCOPUS:0037401969

VL - 195

SP - 276

EP - 289

JO - Journal of Cellular Physiology

JF - Journal of Cellular Physiology

SN - 0021-9541

IS - 2

ER -