Publications by authors named "Kamila Dilimulati"
Article Synopsis
- Phosphatidylcholine (PC)-specific phospholipase C (PC-PLC) and phosphatidylethanolamine (PE)-specific PLC (PE-PLC) have been found in mammalian tissue but their specific genes and proteins have been largely unidentified for decades.
- Recent studies indicate that human sphingomyelin synthase 2 (SMS2) exhibits both PC-PLC and PE-PLC activities along with other enzymatic functions, marking it as a significant enzyme with multiple roles.
- In experiments, SMS2 showed substrate selectivity for certain types of phospholipids and was inhibited by specific compounds like D609 and zinc, suggesting its unique enzymatic properties as a potential long-sought mammalian PC
Mammalian fertilization is a species-selective event that involves a series of interactions between sperm proteins and the oocyte's zona pellucida (ZP) glycoproteins. Bovine ZP consists of three glycoproteins: bZP2, bZP3, and bZP4. In our previous study, we demonstrated that bovine sperm binds to plastic wells coated with recombinant bZP4 and identified that the -terminal domain and the middle region of bZP4 are critical for sperm-binding activity.
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- * SMS1 can produce DG by breaking down phosphatidylcholine (PC) and phosphatidylethanolamine (PE) without needing ceramide, showing that it has multiple enzymatic activities.
- * The study found that SMS1 generates around 65% of DG from SMS activity and 35% from PC-phospholipase C, highlighting SMS1's unique function in lipid metabolism, with distinct inhibitors affecting its different activities. *
The species-selective interaction between sperm and egg at the beginning of mammalian fertilisation is partly mediated by a transparent envelope called the zona pellucida (ZP). The ZP is composed of three or four glycoproteins (ZP1-ZP4). The functions of the three proteins present in mice (ZP1-ZP3) have been extensively studied.
View Article and Find Full Text PDFThe zona pellucida (ZP) is a transparent envelope that surrounds the mammalian oocyte and mediates species-selective sperm-oocyte interactions. The bovine ZP consists of the glycoproteins ZP2, ZP3, and ZP4. Sperm-binding mechanisms of the bovine ZP are not yet fully elucidated.
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