Disease relevance of Ptpn18

• We examined the cellular functions of PTP20 in granulosa cells by expressing the wild type, a catalytically inactive CS mutant in which Cys229 of PTP20 was changed to Ser, or a substrate-trapping DA mutant in which Asp197 was mutated to Ala, using an adenovirus vector [1].

High impact information on Ptpn18

• Consistent with this observation, stable overexpression of PTP20 in PC12 cells resulted in accelerated neurite formation following NGF treatment [2].
• A novel cytoplasmic protein-tyrosine phosphatase (PTPase) designated PTP20 was isolated from a PC12 cDNA library and shown to positively regulate the differentiation process in PC12 cells [2].
• The PTP20 open reading frame of 453 amino acids contains a single tyrosine phosphatase catalytic domain and displays closest homology to members of the PTP-PEST protein-tyrosine phosphatase family [2].
• These results demonstrate that PTP20 regulates the functions of granulosa cells in an FSH-dependent manner by dephosphorylating p190 RhoGAP and subsequently inducing reorganization of the actin cytoskeleton [1].
• Protein tyrosine phosphatase PTP20 induces actin cytoskeleton reorganization by dephosphorylating p190 RhoGAP in rat ovarian granulosa cells stimulated with follicle-stimulating hormone [1].

Biological context of Ptpn18

• Of these PTPs, the expression levels of at least PTP20, PTP-MEG1, PTPepsilonM, and PTPepsilonC significantly changed during the estrous cycle [1].

Anatomical context of Ptpn18

• The novel protein-tyrosine phosphatase PTP20 is a positive regulator of PC12 cell neuronal differentiation [2].

Associations of Ptpn18 with chemical compounds

• The FSH-enhanced phosphotyrosine (p-Tyr) level of p190 RhoGAP was selectively reduced by the overexpressed wild type, but not by mutated PTP20 [1].

Analytical, diagnostic and therapeutic context of Ptpn18

• Confocal microscopy analysis revealed that PTP20 intracellularly colocalizes with p190 RhoGAP [1].

References