Abstract
To date, the structure of the autocrine motility factor (AMF), a tumorsecreted cytokine which stimulates cell migration in vitro and metastasis in vivo, is unknown. Here, AMF secreted by Gc-4 PF murine fibrosarcoma into a protein-free conditioned media was isolated, purified, and microsequenced. The results demonstrate that AMF is the previously cloned cytokine and enzyme designated as neuroleukin, and phosphohexose isomerase (PHI), which has been independently implicated in cell motility, and to be a cancer progression marker. PHI catalyzes isomerization of glucose 6-phosphate to fructose 6-phosphate and is specific for both sugars. Murine AMF exhibits the enzymatic properties of PHI and rabbit heart PHI-stimulated mouse fibrosarcoma cells' motility similar to those of the endogenous AMF. Specific PHI inhibitors (carbohydrate phosphates) inhibited enzymatic activity and AMF-induced cell motility.
Footnotes
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↵1 This work was supported in part by Grant 0065 from the Japan Orthopaedics and Traumatology Foundation, Inc., by Grant-in-Aid 0567118 from the Ministry of Education, Science and Culture (to H. W.), by NIH Grant CA 51714, and by UroCor (to A. R.).
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↵2 To whom requests for reprints should be addressed, at Barbara Ann Karmanos Cancer Institute, Wayne State University, School of Medicine, 110 East Warren Avenue, Detroit, MI 48201.
- Received April 30, 1996.
- Accepted May 14, 1996.
- ©1996 American Association for Cancer Research.
Volume 56, Issue 13
