PMID- 3986773
OWN - NLM
STAT- MEDLINE
DCOM- 19850606
LR  - 20151119
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 45
IP  - 5
DP  - 1985 May
TI  - Binding of formyl peptides to Walker 256 carcinosarcoma cells and the chemotactic 
      response of these cells.
PG  - 2288-93
AB  - N-Formylmethionylleucylphenylalanine (fMLP) induces chemotaxis in leukocytes, the 
      response being mediated by peptide binding to a receptor on the plasma membrane. 
      In tumor cells, this peptide has been reported to induce cellular swelling and 
      chemotaxis in vitro and to enhance the localization of circulating tumor cells in 
      vivo. In the Boyden chamber, we evaluated the migratory responses of Walker 
      carcinosarcoma 256 cells to varying concentrations of fMLP. Sigmoidal 
      dose-response curves were obtained with the dose of chemotactic factor that 
      elicits a half-maximal chemotactic response of 5.0 +/- 2.5 X 10(-8) M. 
      Checkerboard analysis indicated that these responses were dependent upon a 
      concentration gradient of fMLP with increases in migration of circa 2 to 2.5 
      times that of random movement. To examine the binding of fMLP, the tumor cells 
      were incubated with 5 X 10(-9) M fML-[3H]P in Hanks' balanced salt solution. 
      Specific binding (0.5 to 1% of total radioligand, to whole cells inhibited by 5 X 
      10(-6) M fMLP) approached equilibrium after 4 to 6 h at 4 degrees C and after 6 
      to 10 h at 22 degrees C. Autoradiographic studies demonstrated heterogeneous 
      binding of the peptide by tumor cells and also showed its intracellular 
      localization. In homogenates of Walker cells prepared in 0.1 M Tris HCl, pH 7.4, 
      with 10 mM MgCl2 and bovine serum albumin (1 mg/ml), specific binding of 
      approximately 0.5% of total fML-[3H]P reached equilibrium after 60 min at 4 
      degrees C. In whole cells and homogenates, binding was reversible by addition of 
      unlabeled fMLP. In whole cells, displacement curves demonstrated a Kd of 1.9 +/- 
      0.1 X 10(-7) M, whereas in homogenates there was a background of low affinity (Kd 
      greater than 10(-5) M) nonsaturable binding, but also a high-affinity component 
      with Kd of 4.9 +/- 1.8 X 10(-8) M. Both chemotaxis and binding were inhibited by 
      the oligopeptide, N-carbobenzoxy-L-phenylalanyl-L-methionine, which is a 
      competitive inhibitor of formyl peptide-induced neutrophil chemotaxis. These data 
      suggest that fMLP stimulates chemotaxis in tumor cells by a receptor-mediated 
      pathway.
FAU - Rayner, D C
AU  - Rayner DC
FAU - Orr, F W
AU  - Orr FW
FAU - Shiu, R P
AU  - Shiu RP
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Dipeptides)
RN  - 10028-17-8 (Tritium)
RN  - 13126-07-3 (carbobenzoxyphenylalanylmethionine)
RN  - 59880-97-6 (N-Formylmethionine Leucyl-Phenylalanine)
SB  - IM
MH  - Animals
MH  - Carcinoma 256, Walker/*metabolism
MH  - Cells, Cultured
MH  - *Chemotaxis
MH  - Dipeptides/pharmacology
MH  - Female
MH  - N-Formylmethionine Leucyl-Phenylalanine/*metabolism
MH  - Rats
MH  - Tritium
EDAT- 1985/05/01 00:00
MHDA- 1985/05/01 00:01
CRDT- 1985/05/01 00:00
PHST- 1985/05/01 00:00 [pubmed]
PHST- 1985/05/01 00:01 [medline]
PHST- 1985/05/01 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1985 May;45(5):2288-93.