Tumor cell autocrine motility factor.
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Journal: 1986/June - Proceedings of the National Academy of Sciences of the United States of America
ISSN: 0027-8424
PUBMED: 3085086
Abstract:
A cell motility-stimulating factor has been isolated, purified, and partially characterized from the serum-free conditioned medium of human A2058 melanoma cells. We term this activity "autocrine motility factor" (AMF). AMF has the properties of a protein with an estimated size of 55 kDa. At concentrations of 10 nM or less, AMF stimulated the random or directed motility of the producer cells. However, AMF is not an attractant for neutrophils. Amino acid analysis of the purified AMF protein revealed a high content of serine, glycine, glutamic acid, and aspartic acid residues. The activity of AMF was not replaced or blocked by known growth factors such as epidermal growth factor or type beta transforming growth factor. Mechanistic studies showed that AMF stimulated the incorporation of [3H]methyl into cell membrane phospholipids after incubation with [methyl-3H]methionine with a sustained increase in the methylation of phosphatidyldimethylethanolamine to phosphatidylcholine. In contrast, AMF did not affect the incorporation of [1,2-14C]choline into phosphatidylcholine. AMF was produced in large amounts by three different clones of ras oncogene-transfected metastatic NIH 3T3 cells but not by the nontransformed parental cells. AMF may play a major role in the local invasive behavior of tumor cells and may also facilitate the concerted invasion by groups of tumor cells.
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Proc Natl Acad Sci U S A 83(10): 3302-3306
PMID: 3085086

Tumor cell autocrine motility factor.

Abstract

A cell motility-stimulating factor has been isolated, purified, and partially characterized from the serum-free conditioned medium of human A2058 melanoma cells. We term this activity "autocrine motility factor" (AMF). AMF has the properties of a protein with an estimated size of 55 kDa. At concentrations of 10 nM or less, AMF stimulated the random or directed motility of the producer cells. However, AMF is not an attractant for neutrophils. Amino acid analysis of the purified AMF protein revealed a high content of serine, glycine, glutamic acid, and aspartic acid residues. The activity of AMF was not replaced or blocked by known growth factors such as epidermal growth factor or type beta transforming growth factor. Mechanistic studies showed that AMF stimulated the incorporation of [3H]methyl into cell membrane phospholipids after incubation with [methyl-3H]methionine with a sustained increase in the methylation of phosphatidyldimethylethanolamine to phosphatidylcholine. In contrast, AMF did not affect the incorporation of [1,2-14C]choline into phosphatidylcholine. AMF was produced in large amounts by three different clones of ras oncogene-transfected metastatic NIH 3T3 cells but not by the nontransformed parental cells. AMF may play a major role in the local invasive behavior of tumor cells and may also facilitate the concerted invasion by groups of tumor cells.

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Selected References

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  • Lam WC, Delikatny EJ, Orr FW, Wass J, Varani J, Ward PA. The chemotactic response of tumor cells. A model for cancer metastasis. Am J Pathol. 1981 Jul;104(1):69–76.[PMC free article] [PubMed] [Google Scholar]
  • McCarthy JB, Basara ML, Palm SL, Sas DF, Furcht LT. The role of cell adhesion proteins--laminin and fibronectin--in the movement of malignant and metastatic cells. Cancer Metastasis Rev. 1985;4(2):125–152. [PubMed] [Google Scholar]
  • Todaro GJ, Fryling C, De Larco JE. Transforming growth factors produced by certain human tumor cells: polypeptides that interact with epidermal growth factor receptors. Proc Natl Acad Sci U S A. 1980 Sep;77(9):5258–5262.[PMC free article] [PubMed] [Google Scholar]
  • Anzano MA, Roberts AB, Smith JM, Sporn MB, De Larco JE. Sarcoma growth factor from conditioned medium of virally transformed cells is composed of both type alpha and type beta transforming growth factors. Proc Natl Acad Sci U S A. 1983 Oct;80(20):6264–6268.[PMC free article] [PubMed] [Google Scholar]
  • Russo RG, Foltz CM, Liotta LA. New invasion assay using endothelial cells grown on native human basement membrane. Clin Exp Metastasis. 1983 Apr-Jun;1(2):115–127. [PubMed] [Google Scholar]
  • Thorgeirsson UP, Turpeenniemi-Hujanen T, Williams JE, Westin EH, Heilman CA, Talmadge JE, Liotta LA. NIH/3T3 cells transfected with human tumor DNA containing activated ras oncogenes express the metastatic phenotype in nude mice. Mol Cell Biol. 1985 Jan;5(1):259–262.[PMC free article] [PubMed] [Google Scholar]
  • Postlethwaite AE, Snyderman R, Kang AH. The chemotactic attraction of human fibroblasts to a lymphocyte-derived factor. J Exp Med. 1976 Nov 2;144(5):1188–1203.[PMC free article] [PubMed] [Google Scholar]
  • Zigmond SH, Hirsch JG. Leukocyte locomotion and chemotaxis. New methods for evaluation, and demonstration of a cell-derived chemotactic factor. J Exp Med. 1973 Feb 1;137(2):387–410.[PMC free article] [PubMed] [Google Scholar]
  • Tomono T, Ikeda H, Tokunaga E. High-performance ion-exchange chromatography of plasma proteins. J Chromatogr. 1983 Aug 26;266:39–47. [PubMed] [Google Scholar]
  • Koop DR, Morgan ET, Tarr GE, Coon MJ. Purification and characterization of a unique isozyme of cytochrome P-450 from liver microsomes of ethanol-treated rabbits. J Biol Chem. 1982 Jul 25;257(14):8472–8480. [PubMed] [Google Scholar]
  • Schiffmann E, Gallin JI. Biochemistry of phagocyte chemotaxis. Curr Top Cell Regul. 1979;15:203–261. [PubMed] [Google Scholar]
  • Bareis DL, Hirata F, Schiffmann E, Axelrod J. Phospholipid metabolism, calcium flux, and the receptor-mediated induction of chemotaxis in rabbit neutrophils. J Cell Biol. 1982 Jun;93(3):690–697.[PMC free article] [PubMed] [Google Scholar]
  • Wiesmann WP, Johnson JP, Miura GA, Chaing PK. Aldosterone-stimulated transmethylations are linked to sodium transport. Am J Physiol. 1985 Jan;248(1 Pt 2):F43–F47. [PubMed] [Google Scholar]
  • Hirata F, Schiffmann E, Venkatasubramanian K, Salomon D, Axelrod J. A phospholipase A2 inhibitory protein in rabbit neutrophils induced by glucocorticoids. Proc Natl Acad Sci U S A. 1980 May;77(5):2533–2536.[PMC free article] [PubMed] [Google Scholar]
  • Pike MC, Kredich NM, Snyderman R. Phospholipid methylation in macrophages is inhibited by chemotactic factors. Proc Natl Acad Sci U S A. 1979 Jun;76(6):2922–2926.[PMC free article] [PubMed] [Google Scholar]
  • Garcia-Castro I, Mato JM, Vasanthakumar G, Wiesmann WP, Schiffmann E, Chiang PK. Paradoxical effects of adenosine on neutrophil chemotaxis. J Biol Chem. 1983 Apr 10;258(7):4345–4349. [PubMed] [Google Scholar]
  • Guranowski A, Montgomery JA, Cantoni GL, Chiang PK. Adenosine analogues as substrates and inhibitors of S-adenosylhomocysteine hydrolase. Biochemistry. 1981 Jan 6;20(1):110–115. [PubMed] [Google Scholar]
  • Aksamit RR, Backlund PS, Jr, Cantoni GL. Chemotaxis and the synthesis of specific proteins are inhibited by 3-deazaadenosine and other adenosine analogs in a mouse macrophage cell line. J Biol Chem. 1983 Jan 10;258(1):20–23. [PubMed] [Google Scholar]
  • Stopford CR, Wolberg G, Prus KL, Reynolds-Vaughn R, Zimmerman TP. 3-Deazaadenosine-induced disorganization of macrophage microfilaments. Proc Natl Acad Sci U S A. 1985 Jun;82(12):4060–4064.[PMC free article] [PubMed] [Google Scholar]
  • Mato JM, Pencev D, Vasanthakumar G, Schiffmann E, Pastan I. Inhibitors of endocytosis perturb phospholipid metabolism in rabbit neutrophils and other cells. Proc Natl Acad Sci U S A. 1983 Apr;80(7):1929–1932.[PMC free article] [PubMed] [Google Scholar]
  • Grotendorst GR. Alteration of the chemotactic response of NIH/3T3 cells to PDGF by growth factors, transformation, and tumor promoters. Cell. 1984 Feb;36(2):279–285. [PubMed] [Google Scholar]
  • Yoshida K, Ozaki T, Ushijima K, Hayashi H. Studies on the mechanisms of invasion in cancer. I. Isolation and purification of a factor chemotactic for cancer cells. Int J Cancer. 1970 Jul 15;6(1):123–132. [PubMed] [Google Scholar]
  • Mato JM, Marín-Cao D. Protein and phospholipid methylation during chemotaxis in Dictyostelium discoideum and its relationship to calcium movements. Proc Natl Acad Sci U S A. 1979 Dec;76(12):6106–6109.[PMC free article] [PubMed] [Google Scholar]
  • Kort EN, Goy MF, Larsen SH, Adler J. Methylation of a membrane protein involved in bacterial chemotaxis. Proc Natl Acad Sci U S A. 1975 Oct;72(10):3939–3943.[PMC free article] [PubMed] [Google Scholar]
  • Springer WR, Koshland DE., Jr Identification of a protein methyltransferase as the cheR gene product in the bacterial sensing system. Proc Natl Acad Sci U S A. 1977 Feb;74(2):533–537.[PMC free article] [PubMed] [Google Scholar]
  • Stock J, Borczuk A, Chiou F, Burchenal JE. Compensatory mutations in receptor function: a reevaluation of the role of methylation in bacterial chemotaxis. Proc Natl Acad Sci U S A. 1985 Dec;82(24):8364–8368.[PMC free article] [PubMed] [Google Scholar]
  • Castaño JG, Alemany S, Nieto A, Mato JM. Activation of phospholipid methyltransferase by glucagon in rat hepatocytes. J Biol Chem. 1980 Oct 10;255(19):9041–9043. [PubMed] [Google Scholar]
  • Kelly KL, Kiechle FL, Jarett L. Insulin stimulation of phospholipid methylation in isolated rat adipocyte plasma membranes. Proc Natl Acad Sci U S A. 1984 Feb;81(4):1089–1092.[PMC free article] [PubMed] [Google Scholar]
  • Bokoch GM, Gilman AG. Inhibition of receptor-mediated release of arachidonic acid by pertussis toxin. Cell. 1984 Dec;39(2 Pt 1):301–308. [PubMed] [Google Scholar]
  • Molski TF, Naccache PH, Marsh ML, Kermode J, Becker EL, Sha'afi RI. Pertussis toxin inhibits the rise in the intracellular concentration of free calcium that is induced by chemotactic factors in rabbit neutrophils: possible role of the "G proteins" in calcium mobilization. Biochem Biophys Res Commun. 1984 Oct 30;124(2):644–650. [PubMed] [Google Scholar]
  • Okajima F, Ui M. ADP-ribosylation of the specific membrane protein by islet-activating protein, pertussis toxin, associated with inhibition of a chemotactic peptide-induced arachidonate release in neutrophils. A possible role of the toxin substrate in Ca2+-mobilizing biosignaling. J Biol Chem. 1984 Nov 25;259(22):13863–13871. [PubMed] [Google Scholar]
  • Backlund PS, Jr, Meade BD, Manclark CR, Cantoni GL, Aksamit RR. Pertussis toxin inhibition of chemotaxis and the ADP-ribosylation of a membrane protein in a human-mouse hybrid cell line. Proc Natl Acad Sci U S A. 1985 May;82(9):2637–2641.[PMC free article] [PubMed] [Google Scholar]
  • Gilman AG. G proteins and dual control of adenylate cyclase. Cell. 1984 Mar;36(3):577–579. [PubMed] [Google Scholar]
  • Albini A, Allavena G, Parodi S, Santi L. Comparison of the chemotactic response to conditioned medium of BALB/c3T3 fibroblasts and their SV 40 transformants. Tumori. 1985 Apr 30;71(2):97–100. [PubMed] [Google Scholar]
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Abstract
A cell motility-stimulating factor has been isolated, purified, and partially characterized from the serum-free conditioned medium of human A2058 melanoma cells. We term this activity "autocrine motility factor" (AMF). AMF has the properties of a protein with an estimated size of 55 kDa. At concentrations of 10 nM or less, AMF stimulated the random or directed motility of the producer cells. However, AMF is not an attractant for neutrophils. Amino acid analysis of the purified AMF protein revealed a high content of serine, glycine, glutamic acid, and aspartic acid residues. The activity of AMF was not replaced or blocked by known growth factors such as epidermal growth factor or type beta transforming growth factor. Mechanistic studies showed that AMF stimulated the incorporation of [3H]methyl into cell membrane phospholipids after incubation with [methyl-3H]methionine with a sustained increase in the methylation of phosphatidyldimethylethanolamine to phosphatidylcholine. In contrast, AMF did not affect the incorporation of [1,2-14C]choline into phosphatidylcholine. AMF was produced in large amounts by three different clones of ras oncogene-transfected metastatic NIH 3T3 cells but not by the nontransformed parental cells. AMF may play a major role in the local invasive behavior of tumor cells and may also facilitate the concerted invasion by groups of tumor cells.
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