Our results indicate that GCP-WD broadly mediates targeting of the gammaTuRC to sites of microtubule nucleation and to the mitotic spindle, which is essential for spindle formation.
Knockdown of this essential protein resulted in reduction of γ-TuRC recruitment to cortical microtubules and total nucleation frequency, showing that GCP-WD controls γ-TuRC positioning and function in these interphase arrays.
These results suggest that GCP-WD contains a phosphorylation-dependent Plk1 docking site.
Treatment of mitotic cells with a Cdk inhibitor reverses this mobility shift, as does mutation of serine 418, a consensus Cdk1 phosphorylation site, to alanine, suggesting that GCP-WD phosphorylation is mainly driven by the mitotic kinase Cdk1 [13].
Interestingly, a mouse equivalent of CXCL8 does not exist as none of the mouse ELR-chemokines show robust activity for either human or mouse CXCR1, and it has been proposed that GCP-2/CXCL6 fulfils this role in mice [26].
Figure 3(F) shows that GCPs express the P2Y1 purinergic receptor.
Immunocytochemistry and pharmacological assays indicated that GCPs expressed P2Y1Rs (P2Y1 receptors) and that deletion or blockade of these receptors decreased the migration rate of GCPs and the frequency of Ca2+ oscillations.
A prospective 10-year study that examined GCP subjects with rough surface implants revealed a slightly higher peri-implantitis rate (28.6%) [31].
Peri-implant bone loss in GAP subjects was 2.89 mm (SD 1.90) and that in GCP subjects 1.38 mm (SD 1.05).
