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PURPOSE OF REVIEW: Telehealth in neonatology is a rapidly expanding modality for providing care to neonatal patient populations. In this review, we describe the most recent published innovations in neonatal telehealth, spanning the neonatal ICU (NICU), community/rural hospitals and the patient's home. RECENT FINDINGS: Telemedicine for neonatal subspecialty care has continued to expand, from well established uses in retinopathy of prematurity screening and tele-echocardiography, to applications in genetics and neurology. Within the NICU itself, neonatologist-led remote rounding has been shown to be a feasible method of increasing access to expert care for neonates in rural hospitals. Telehealth has improved parental and caregiver education, eased the NICU-to-home transition experience and expanded access to lactation services for rural mothers. Telemedicine-assisted neonatal resuscitation has improved the quality of resuscitation and reduced unnecessary neonatal transports to higher levels of care. Finally, the global COVID-19 pandemic has accelerated the expansion of neonatal telehealth. SUMMARY: Telehealth provides increased access to expert neonatal care and improves patient outcomes, while reducing the cost of care for neonates in diverse settings. Continued high-quality investigation of the impacts of telehealth on patient outcomes and healthcare systems is critical to the continued development of neonatal telemedicine best practices.

Carnitine-acylcarnitine translocase (CACT) deficiency is a rare disorder of long chain fatty acid oxidation with a very high mortality rate due to cardiomyopathy or multiorgan failure. We present the course of a very premature infant with early onset CACT deficiency complicated by multiple episodes of necrotizing enterocolitis, sepsis, and liver insufficiency, followed by eventual demise. The complications of prematurity, potentiated by the overlay of CACT deficiency, contributed to the difficulty of reaching the ultimate diagnosis of CACT deficiency.

We have investigated the mechanism by which high concentrations of glucose inhibit insulin stimulation of glycogen synthase. In NIH-3T3-L1 adipocytes cultured in low glucose (LG; 2.5 mm), the half-maximal activation concentration (A(0.5)) of glucose 6-phosphate was 162 +/- 15 microm. Exposure to either high glucose (HG; 20 mm) or glucosamine (GlcN; 10 mm) increased the A(0.5) to 558 +/- 61 or 612 +/- 34 microm. Insulin treatment with LG reduced the A(0.5) to 96 +/- 10 microm, but cells cultured with HG or GlcN were insulin-resistant (A(0.5) = 287 +/- 27 or 561 +/- 77 microm). Insulin resistance was not explained by increased phosphorylation of synthase. In fact, culture with GlcN decreased phosphorylation to 61% of the levels seen in cells cultured in LG. Hexosamine flux and subsequent enzymatic protein O-glycosylation have been postulated to mediate nutrient sensing and insulin resistance. Glycogen synthase is modified by O-linked N-acetylglucosamine, and the level of glycosylation increased in cells treated with HG or GlcN. Treatment of synthase in vitro with protein phosphatase 1 increased basal synthase activity from cells cultured in LG to 54% of total activity but was less effective with synthase from cells cultured in HG or GlcN, increasing basal activity to only 13 or 16%. After enzymatic removal of O-GlcNAc, however, subsequent digestion with phosphatase increased basal activity to over 73% for LG, HG, and GlcN. We conclude that O-GlcNAc modification of glycogen synthase results in the retention of the enzyme in a glucose 6-phosphate-dependent state and contributes to the reduced activation of the enzyme in insulin resistance.