Phospholipase C zeta 1 Proteins (PLCz1)

Pig (Porcine) Phospholipase C zeta 1 (PLCz1) interaction partners

1. Results suggest a mechanism by which phospholipase C zeta originates from an oocyte-penetrating assembly--the sperm perinuclear matrix--to induce mammalian oocyte activation at fertilization.

Mouse (Murine) Phospholipase C zeta 1 (PLCz1) interaction partners

1. Human PLCzeta exhibits superior fertilization potency over mouse PLCzeta in triggering the Ca(2 (show CA2 Proteins)+) oscillations required for mammalian oocyte activation.

2. these results suggest that both PLCzeta- and sperm-mediated Ca2 (show CA2 Proteins)+ release preferentially use an intracellular membranous source of PI(4,5)P2, in contrast to PLCdelta1, which targets PI(4,5)P2 in the plasma membrane.

3. Data suggest that positively charged residues within the XY linker play an important role in the PLCzeta interaction with PtdIns(4,5)P(2), a crucial step in generating the Ca(2 (show CA2 Proteins)+) activation signal that is essential for fertilization in mammals.

4. Murine PLCZ1 and bovine PLCZ1 possess species-specific differences in activity and suggest potential differences in the mode of action of the protein between the two species.

5. purified PLCzeta protein induces Ca(2 (show CA2 Proteins)+) oscillations, indicating that PLCzeta is a proper candidate of the mammalian egg-activating sperm factor

6. Cell cycle-dependent Ca2 (show CA2 Proteins)+ oscillations are regulated by nuclear targeting of PlCzeta.

7. Results suggest a mechanism by which phospholipase C zeta originates from an oocyte-penetrating assembly--the sperm perinuclear matrix--to induce mammalian oocyte activation at fertilization.

8. PLCzeta is the physiological trigger of Ca(2 (show CA2 Proteins)+) oscillations required for activation of development

9. interaction of PI(3 (show PI3 Proteins))P and PI(5)P could play a role for negative regulation of PLCzeta

10. PLCzeta exhibited alternative cytoplasm/nucleus localization during development

Human Phospholipase C zeta 1 (PLCz1) interaction partners

1. we evaluate sperm motility and the proportion of sperm expressing PLC (show HSPG2 Proteins) zeta in 71 males (22-54 years; 44 fertile controls and 27 infertile patients), along with total levels and localisation patterns of PLC (show HSPG2 Proteins) zeta within the sperm head.

2. findings suggest that human PLCZ1 RNA is a better therapeutic agent to rescue human oocytes from failed activation, leading to normal and efficient development.

3. The value of PAWP (show WBP2NL Proteins) and PLCzeta as indicators of sperm quality was studied.

4. The role of the PLCZ1 protein in male infertility, and its expression regulation and therapeutic potential have been discussed. (Review)

5. latest developments that have begun to unravel the vital role of PLCzeta at mammalian fertilisation and decipher its unique mechanism of action within the fertilising egg.

6. The findings highlight the importance of PLCzeta at fertilization and the vital role of the C2 domain in PLCzeta function, possibly due to its novel binding characteristics.

7. The findings of the present study illustrate that one of the etiologies of reduced fertility associated with varicocele is the low expression of PLCzeta

8. In male infertility, the absence of PLCZ1 alone is sufficient to prevent oocyte activation irrespective of the presence of PAWP (show WBP2NL Proteins).

9. Human PLCzeta elicited the characteristic Ca(2 (show CA2 Proteins)+) oscillations present at mammalian fertilization, which produced oocyte activation and embryo development.

10. Study further supports the fundamental role of PLCzeta in the oocyte activation process.

Cow (Bovine) Phospholipase C zeta 1 (PLCz1) interaction partners

1. Data show that the level of actin/PLC (show PLC Proteins)-zeta interaction was twice as high in G-actin (show ACTB Proteins) that reflected an increase in affinity.

2. A novel splice variant of Phospholipase C zeta 1 in the testis tissues of adult and fetal Chinese Holstein bulls was characterized.

3. Murine PLCZ1 and bovine PLCZ1 possess species-specific differences in activity and suggest potential differences in the mode of action of the protein between the two species