Tumor cell autocrine motility factor is the neuroleukin/phosphohexose isomerase polypeptide.

Abstract

To date, the structure of the autocrine motility factor (AMF), a tumor-secreted 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.

• Authors: H Watanabe, K Takehana, M Date, T Shinozaki, A Raz
• Journal: Cancer research (Cancer Res) Vol. 56 Issue 13 Pg. 2960-3 (Jul 01 1996) ISSN: 0008-5472 [Print] United States
• PMID: 8674049 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Neoplasm Proteins
• Glucose-6-Phosphate Isomerase

Topics

• Amino Acid Sequence
• Animals
• Cell Movement (drug effects)
• Fibrosarcoma (enzymology)
• Glucose-6-Phosphate Isomerase (analysis, antagonists & inhibitors, isolation & purification)
• Mice
• Molecular Sequence Data
• Neoplasm Proteins (analysis, antagonists & inhibitors, isolation & purification)
• Rabbits
• Tumor Cells, Cultured