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To determine the prevalence of uveal effusion in acute and chronic primary angle-closure glaucoma (PACG) or primary angle closure (PAC) and to compare it with the prevalence in eyes with open-angle glaucoma (OAG) or ocular hypertension.Prospective consecutive case series.Five hundred one eyes of 351 consecutive patients with PAC and 156 eyes of 116 randomly selected primary OAG or ocular hypertension patients. The PAC group included 40 eyes of 35 patients with acute PACG and 30 unaffected fellow eyes, 39 eyes and 35 fellow eyes with a history of acute PACG, and 357 eyes with chronic PAC.Ultrasound biomicroscopic examination was performed to diagnose uveal effusion and to measure anterior chamber depth (ACD).Presence of uveal effusion and ACD.Uveal effusion was demonstrated in 23 eyes (58%) with acute PACG and 7 fellow eys (23%) (chi2 = 8.17, P = 0.0043). Among eyes with chronic PAC, uveal effusion was present in 69 [corrected](14%[corrected]), a higher prevalence than was found in open-angle patients (2 eyes [1.3%]) (chi2 = 19.3, P0.001). In the chronic PAC group, the ACD of phakic eyes with uveal effusion (1.92+/-0.42 mm) was significantly shallower than that of phakic eyes without effusion (2.06+/-0.32 mm) (P = 0.019).Uveal effusion diagnosed by ultrasound biomicroscopy is a special feature in PAC, and is prevalent in acute PACG. Uveal effusion in phakic eyes with PAC is associated with shallowing of ACD.

Rap2 belongs to the Ras family of small GTP-binding proteins, but its specific roles in cell signaling remain unknown. In the present study, we have affinity-purified from rat brain a Rap2-interacting protein of approximately 155 kDa, p155. By liquid chromatography tandem mass spectrometry, we have identified p155 as Traf2- and Nck-interacting kinase (TNIK). TNIK possesses an N-terminal kinase domain homologous to STE20, the Saccharomyces cerevisiae mitogen-activated protein kinase kinase kinase kinase, and a C-terminal regulatory domain termed the citron homology (CNH) domain. TNIK induces disruption of F-actin structure, thereby inhibiting cell spreading. In addition, TNIK specifically activates the c-Jun N-terminal kinase (JNK) pathway. Among our observations, TNIK interacted with Rap2 through its CNH domain but did not interact with Rap1 or Ras. TNIK interaction with Rap2 was dependent on the intact effector region and GTP-bound configuration of Rap2. When co-expressed in cultured cells, TNIK colocalized with Rap2, while a mutant TNIK lacking the CNH domain did not. Rap2 potently enhanced the inhibitory function of TNIK against cell spreading, but this was not observed for the mutant TNIK lacking the CNH domain. Rap2 did not significantly enhance TNIK-induced JNK activation, but promoted autophosphorylation and translocation of TNIK to the detergent-insoluble cytoskeletal fraction. These results suggest that TNIK is a specific effector of Rap2 to regulate actin cytoskeleton.