A protein possessing vascular smooth muscle cell (SMC) growth-promoting
activity (VSGP) was purified from bovine ovarian follicular fluid. The
purified protein showed a broad band on SDS-PAGE with an apparent molecular
mass of 90-100 kDa, The purified protein was characterized by amino acid
sequence analysis of its N-terminal and internal peptides. Based on the
information of the peptide sequences, bovine ovarian cDNA library was screened
and cDNA clones encoding the protein were isolated. Human homolog of the
protein was also cloned from human ovarian cDNA library. Nucleotide sequence
analysis revealed that bovine VSGP transcript has a 2421-bp open reading
frame, which encodes a protein of 807 amino acid residues. A homology search
indicated that bovine and human VSGP are counterparts of rat F-spondin, which
has been previously identified as a promoter molecule of neurite extension in
rat fetal floor plate.
NCBI Summary:
Very strongly similar to rat F-spondin (Rn.7546); may have a role in the growth and guidance of axons
General function
Ligand, Growth factor
Comment
Cellular localization
Secreted
Comment
Ovarian function
Comment
Miyamoto K, et al 2001 reported the isolation and characterization of vascular smooth muscle cell
growth promoting factor from bovine ovarian follicular fluid
and its cDNA cloning from bovine and human ovary.
RNA blot analysis showed wide distribution of
VSGP/F-spondin transcripts in fetal and adult human tissues. Especially the
expression was highest in the adult human ovary. The purified bovine
VSGP/F-spondin showed vascular SMC growth promoting activity with an ED,,
value of 10(-8) M. Together with these findings, we demonstrated here that
VSGP/F-spondin is a major factor for vascular SMC proliferation in the ovary.