Taste and/or Odour Disturbances in Pediatric Patients Undergoing IV Flush with Normal Saline Administered by Prefilled Syringe.

BACKGROUND: At the Children's Hospital of Eastern Ontario, more than 6000 inpatients per year undergo IV saline flushes by prefilled syringe to assess and maintain patency of IV tubing. In studies involving adults, it has been reported that volatile substances may leach from syringe materials into the saline, leading to taste and/or odour disturbances. OBJECTIVE: To determine the incidence of taste and/or odour disturbances in pediatric patients after flushing of IV tubing with 0.9% sodium chloride (normal saline [NS]) from prefilled syringes. METHODS: Inpatients aged 5-18 years who had undergone routine flushing of central or peripheral IV tubing with commercially available prefilled NS syringes were interviewed. Children aged 5-10 years used a visual hedonic scale to rate taste and odour sensations, and those aged 11-18 years used a numeric rating scale. RESULTS: During the study period (April to July 2011), a total of 104 pediatric inpatients (21 aged 5-10 years and 83 aged 11-18 years) underwent NS flushing of central (10 patients [10%]) or peripheral (94 patients [90%]) tubing. For 100 of these patients, BD Posiflush NaCl 0.9% 10-mL sterile prefilled syringes were used, and for 4 patients BD Saline XS NaCl 0.9% 10-mL sterile prefilled syringes were used. Taste and/or odour disturbances were reported by 76 (73%) of the patients. Twelve patients described more than one taste or odour sensation. Taste and odour disturbances were detected by children in both age groups. CONCLUSIONS: Flushing of IV tubing with prefilled NS syringes resulted in taste and/or odour disturbances in a pediatric population.

Implications of pannexin 1 and pannexin 3 for keratinocyte differentiation.

Pannexin (Panx) 1 and Panx3 are integral membrane proteins that share some sequence homology with the innexin family of invertebrate gap junctions. They are expressed in mammalian skin. Pannexins have been reported to form functional mechanosensitive single-membrane channels, but their importance in regulating cellular function is poorly understood. In this study, Panx1 and Panx3 were detected in the epidermis of 13.5 day embryonic mice. Compared with newborn mice, there was less Panx1 expression in both thin and thick murine skin, whereas Panx3 expression was unchanged. To investigate the role of pannexins in keratinocyte differentiation, we employed rat epidermal keratinocytes (REKs) that have the capacity to differentiate into organotypic epidermis, and engineered them to overexpress Panx1, Panx1-GFP or Panx3. The expression of Panx1 or Panx3 resulted in the increased ability of REKs to take up dye, suggesting that cell-surface channels were formed. Compared with monolayer REKs, endogenous Panx1 levels remained unchanged, whereas the 70 kDa immunoreactive species of Panx3 was greatly increased in the organotypic epidermis. In monolayer cultures, ectopic Panx1 and Panx1-GFP localized to the plasma membrane, whereas Panx3 displayed both intracellular and plasma-membrane profiles. Although both pannexins reduced cell proliferation, only Panx1 disrupted the architecture of the organotypic epidermis and markedly dysregulated cytokeratin 14 expression and localization. Furthermore, ectopic expression of only Panx1 reduced the vital layer thickness of the organotypic epidermis. In summary, Panx1 and Panx3 are coexpressed in the mammalian epidermis, and the regulation of Panx1 plays a key role in keratinocyte differentiation.

Diverse subcellular distribution profiles of pannexin 1 and pannexin 3.

Pannexins have been proposed to play a role in gap junctional intercellular communication and as single-membrane channels, although many of their molecular characteristics differ from connexins. Localization of untagged Panx1 and Panx3 exogenously expressed in five cultured cell lines revealed a cell surface distribution profile with limited evidence of cell surface clustering and variable levels of intracellular pools. However, N-glycosylation-defective mutants of pannexins exhibited a more prominent intracellular distribution with decreased cell surface labeling, suggesting an important role for pannexin glycosylation in trafficking. Similar to wild-type pannexins, the glycosylation-defective mutants failed to noticeably transfer microinjected fluorescent dyes to neighboring cells, suggesting that few, or no functional intercellular channels were formed. Finally, varied distribution patterns of endogenous Panx1 and Panx3 were observed in cells of osteoblast origin and Madin-Darby canine kidney cells. Collectively, diverse expression and distribution profiles of Panx1 and Panx3 suggest that they may have multiple cellular functions.

Pannexin 1 and pannexin 3 are glycoproteins that exhibit many distinct characteristics from the connexin family of gap junction proteins.

Pannexins are mammalian orthologs of the invertebrate gap junction proteins innexins and thus have been proposed to play a role in gap junctional intercellular communication. Localization of exogenously expressed pannexin 1 (Panx1) and pannexin 3 (Panx3), together with pharmacological studies, revealed a cell surface distribution profile and life cycle dynamics that were distinct from connexin 43 (Cx43, encoded by Gja1). Furthermore, N-glycosidase treatment showed that both Panx1 (approximately 41-48 kD species) and Panx3 (approximately 43 kD) were glycosylated, whereas N-linked glycosylation-defective mutants exhibited a decreased ability to be transported to the cell surface. Tissue surveys revealed the expression of Panx1 in several murine tissues--including in cartilage, skin, spleen and brain--whereas Panx3 expression was prevalent in skin and cartilage with a second higher-molecular-weight species present in a broad range of tissues. Tissue-specific localization patterns of Panx1 and Panx3 ranging from distinct cell surface clusters to intracellular profiles were revealed by immunostaining of skin and spleen sections. Finally, functional assays in cultured cells transiently expressing Panx1 and Panx3 were incapable of forming intercellular channels, but assembled into functional cell surface channels. Collectively, these studies show that Panx1 and Panx3 have many characteristics that are distinct from Cx43 and that these proteins probably play an important biological role as single membrane channels.