Fasciclin I, a neuronal
cell adhesion molecule, was first identified in the grasshopper. To date, various
fasciclin I-like
proteins have been identified but their
biological functions have not been well characterized. Here, we have purified a
fasciclin I-like
protein with a molecular weight of 33kDa from sea urchin (Strongylocentrotus intermedius) ovaries using hydrophobic chromatography and gel filtration. The
protein was not N-glycosylated. Partial amino acid sequences of
cyanogen bromide (CNBr)-cleaved fragments were highly conserved to other sea urchin
fasciclin I-like
proteins identified previously. The circular dichroism (CD) spectrum analysis demonstrated that the 33kDa
protein contained high content of alpha-helical structure. These results suggest that the 33kDa
protein is a
fasciclin I-like family. Additionally, the
fasciclin I-like
protein promoted HT1080 human
fibrosarcoma cell attachment. Further, a synthetic
peptide (P1: GLREAANIAEQVDLRQVLRDVDL) of the
protein corresponding to a highly conserved region of the
fasciclin I-like family promoted
heparin-dependent HT1080 cell attachment. Moreover, the
peptide inhibited HT1080 cell attachment to the
fasciclin I-like
protein. These results suggest that the 33kDa
protein from sea urchin ovaries isolated here is a member of the
fasciclin I family and that the N-terminal region of the
protein is important for cell attachment activity. The
protein has a potential to be involved in
biological functions in sea urchin as a cell adhesive molecule.