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Importance: Cross-Facial Nerve Grafting (CFNG) for facial palsy offers potential to restore spontaneous facial expression, but specific indications and associated outcomes are limited. Updates to this technique have aided in its successful employment in select cases. This review aims to explore the context in which CFNG has been successfully utilized as a primary modality. Observations: Literature review was performed auditing all studies investigating CFNG as a primary modality, which reported outcomes. A total of 326 cases reporting outcomes for primary CFNG were included. Eye closure outcomes were 83.3% successful at ages 0-18, 77.3% successful at ages 19-40, and 57.1% successful at ages 41+. Smile outcomes were 73.7% successful at ages 0-18, 81.5% successful at ages 19-40, and 52.8% successful at ages 41+. For synkinesis, 89% of cases were considered successful; 100% successful at ages 0-18, and 78.4% successful in adults. Conclusions and Relevance: CFNG may offer return of spontaneous facial function in select cases. Higher percentages of successful outcomes are observed in younger patients, when performed in two stages, and when performed earlier from the onset of FP in cases of eye closure restoration. In the modern era, CFNG has been more commonly employed as an adjunctive procedure to other reanimation techniques.
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Introduction: JayDoc Free Clinic (JayDoc) serves medical needs of uninsured patients in the Kansas City metropolitan area. It is known that patients who have access to primary care are less likely to visit their local Emergency Department (ED) for non-emergent needs. However, it is not well described if JayDoc lowers usage of The University of Kansas Health System (TUKHS) ED. This is the first study to assess the patient referral process between TUKHS ED and JayDoc. Methods: The authors administered a voluntary survey to every patient triaged at JayDoc, even if they were ultimately not accepted for a visit. Items on the questionnaire included health insurance status, primary language, and access to a primary care physician. The authors included questions on the usage of TUKHS ED in the last 12 months. Results: Seventy-three patients completed the questionnaire. Approximately 10% of respondents reported they visited the ED in the last 12 months and received a referral to JayDoc from staff. However, authors observed no statistically significant difference in the proportion of new patients who used the ED in the last 12 months compared to that of returning patients. Conclusions: Results of this study demonstrated an existing referral system between JayDoc and TUKHS ED. However, the authors could not conclude that JayDoc reduces non-emergent ED visits among its patient population. Future initiatives will include further education to ED providers to increase the number of patients being referred to JayDoc.
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The protein gC1qR/C1qBP/HABP-1 plays an essential role in mitochondrial biogenesis, but becomes localized at the cellular surface in numerous pathophysiological states. When this occurs on endothelial cells, surface-exposed gC1qR activates the classical pathway of complement. It also promotes assembly of a multi-protein complex comprised of coagulation factor XII (FXII), pre-kallikrein (PK), and high-molecular weight kininogen (HMWK) that activates the contact system and the kinin-generating system. Since surface-exposed gC1qR triggers intravascular inflammatory pathways, there is interest in identifying molecules that block gC1qR function. Here we further that objective by reporting the outcome of a structure/function investigation of gC1qR, its interactions with FXII, and the impact of a panel of monoclonal anti-gC1qR antibodies on FXII binding to gC1qR. Although deletion mutants have been used extensively to assess gC1qR function, none of these proteins have been characterized structurally. To that end, we determined a 2.2 Å resolution crystal structure of a gC1qR mutant lacking both of its acidic loops, but which retained nanomolar-affinity binding to FXII and FXIIa. This structure revealed that the trimeric gC1qR assembly was maintained despite loss of roughly thirty residues. Characterization of a novel panel of anti-gC1qR monoclonal antibodies identified several with biochemical properties distinct from previously described antibodies, as well as one which bound to the first acidic loop of gC1qR. Intriguingly, we found that each of these antibodies could partly inhibit binding of FXII and FXIIa to gC1qR. Based on these results and previously published studies, we offer new perspectives for developing gC1qR inhibitors.