[Purification and characterization of a growth factor from human bone matrix].
A growth factor was purified from human bone matrix by extraction with EDTA, acetone treatment, gel filtration column chromatography, ion exchange column chromatography, and reversed-phase HPLC. Purified protein migrated as a single band to an area with a molecular weight of about 6,000 on SDS-polyacrylamide gel. The purified protein stimulated dose dependent osteoblast proliferation. The sequence of the first 30 N-terminal amino acids of the protein was identical to that of the human insulin-like growth factor-II (IGF-II). MC3T3-E1 cells reacted immunocytochemically to the monoclonal antibody against IGF-II. The culture medium of MC3T3-E1 cells contained immunoreactive IGF-II, which was measured by an enzyme immunoassay. These results indicate that IGF-II is contained in bone matrix, is effective in osteoblast proliferation, produced by the osteoblasts, and secreted from the osteoblasts. Taken together, these results show that IGF-II is present as a local growth factor in the bone system, playing an important role in bone formation following bone resorption.
Suzuki
K
K
Department of Orthopaedic Surgery, Hokkaido University School of Medicine, Japan.
D000818:Animals; D001846:Bone Development; D001857:Bone Matrix / Q000737:chemistry*; D002453:Cell Cycle; D002642:Chick Embryo; D006133:Growth Substances / Q000302:isolation & purification*; D006801:Humans; D007335:Insulin-Like Growth Factor II / Q000302:isolation & purification* / Q000378:metabolism / Q000502:physiology; D010006:Osteoblasts / Q000166:cytology / Q000378:metabolism
D006133:Growth Substances; D007335:Insulin-Like Growth Factor II