Title : Characterization of the post-translational modification of recombinant human
BMP-15 mature
protein
Abstract :
- Bone morphogenetic protein-15 ( BMP-15 ) is an oocyte-secreted factor critical for the regulation of ovarian physiology
- When recombinant human BMP-15 ( rhBMP-15 ) produced in human embryonic kidney 293 cells was subjected to SDS-PAGE analysis, two mature protein forms corresponding to 16 kDa ( P16 ) and 17 kDa ( P17 ) were observed
- Despite the physiological relevance and critical function of BMP-15 in female reproduction, little is known about the structure of rhBMP-15
- Here, we have analyzed the structure of the rhBMP-15 mature proteins ( P16 and P17 ) using state-of-the-art proteomics technology
- Our findings are as follows: (1) the N-terminal amino acid of P16 and P17 is pyroglutamic acid; (2 ) the Ser residue at the sixth position of P16 is phosphorylated; ( 3) P17 is O-glycosylated at Thr10 ; and (4) the C-terminal amino acid of P16 and P17 is truncated
- These findings are the first knowledge of the structure of rhBMP-15 mature protein toward understanding the molecular basis of BMP-15 function and could provide an important contribution to the rapidly progressing research area involving oocyte-specific growth factors in modulation of female fertility
Output (sent_index, trigger,
protein,
sugar,
site):
- 5. O-glycosylated, , 3) P17, -, Thr10
Output(Part-Of) (sent_index,
protein,
site):
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):