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Characterization of a fasciclin I-like protein with cell attachment activity from sea urchin (Strongylocentrotus intermedius) ovaries.

Abstract
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.
AuthorsKoji Sato, Norio Nishi, Motoyoshi Nomizu
JournalArchives of biochemistry and biophysics (Arch Biochem Biophys) Vol. 424 Issue 1 Pg. 1-10 (Apr 01 2004) ISSN: 0003-9861 [Print] United States
PMID15019831 (Publication Type: Journal Article)
Chemical References
  • Amino Acids
  • Cell Adhesion Molecules
  • Cell Adhesion Molecules, Neuronal
  • Peptide Fragments
  • fasciclin I
Topics
  • Amino Acid Sequence
  • Amino Acids (analysis)
  • Animals
  • Cell Adhesion (drug effects)
  • Cell Adhesion Molecules (chemistry, genetics, pharmacology, physiology)
  • Cell Adhesion Molecules, Neuronal (chemistry, genetics, pharmacology, physiology)
  • Cell Line, Tumor
  • Circular Dichroism
  • Dose-Response Relationship, Drug
  • Female
  • Glycosylation
  • Humans
  • Molecular Sequence Data
  • Molecular Weight
  • Ovary (chemistry)
  • Peptide Fragments (genetics, metabolism, pharmacology)
  • Sea Urchins (chemistry)
  • Sequence Homology, Amino Acid

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