Yasufumi Niinaka

TL;DR: The results suggest that extracellular AMF activity may be a result of the product of intracellular cleavage of a precursor polypeptide, which is overexpressed and selectively secreted through a nonclassical secretory mechanism by neoplastic cells.

TL;DR: Cloned full‐length cDNAs for both human and mouse AMFR genes revealed no significant homology with all known seven transmembrane proteins, but a significant structural similarity to a hypothetical protein of Caenorhabditis elegans, F26E4.11.

TL;DR: It is established that AMF signaling induced anti‐apoptotic activity and that human fibrosarcoma HT‐1080 line that secreted high levels of AMF were resistant to drug‐induced apoptosis and might indicate a novel route by which tumor cells protect themselves with products, such as AMF, and proliferate despite various stresses and chemical insults.

TL;DR: In this paper, a recombinant human AMF (rhAMF) was generated, expressed and isolated, which retained the biological activities of the native AMF and catalyzes phosphohexose isomerization and stimulated cell motility.

TL;DR: Morphological and motility analyses revealed LMF4 cells to have the highest motile activity among those cells and shared the similar features with HSC-3: high level secretion of AMF, enhancement of gp78 expression, co-expression of vimentin and cytokeratin, although LMF 4 cells showed twice as high motile reactivity as HSC -3.