Prospective randomized evaluation of short-term complications when using buffered or unbuffered lidocaine 1% with epinephrine for blepharoplasty surgery.

PURPOSE: To determine whether there is a difference in the incidence of short-term complications using plain lidocaine with epinephrine versus the buffered equivalent in eyelid surgery. METHODS: The authors performed a prospective, double-masked, randomized study in patients scheduled for combined upper eyelid blepharoplasty and levator advancement ptosis repair surgery with local anesthesia. Exclusion criteria included: documented allergies to lidocaine and/or epinephrine; known pregnancy; profound cognitive impairment; inability to understand the visual analog scale or the informed consent; and previous eyelid surgery. Each subject was his/her own control by using the unbuffered local anesthetic in one eye, while the buffered solution was used in the other eye. The surgeon completed a specific standardized data collection form for quantifying both intraoperative and postoperative complications, such as bleeding, bruising, and edema. Data regarding pain on injection and postoperative pain were collected from patients using a visual analog pain scale. RESULTS: Thirty-nine patients were included in this study, of which 18 experienced less pain during the injection on the side where buffered lidocaine was used, 11 reported no difference, and 10 reported less pain in the eye injected with unbuffered lidocaine. Injection pain revealed a mean operative pain rating of 4.01 +/- 2.45 in the eye with buffered lidocaine versus 4.49 +/- 2.58 in the control (p = 0.06). There were no significant differences between the buffered and unbuffered lidocaine eyes as regards postoperative bleeding, swelling, or pain, and there was a trend toward less pain on injection with the buffered solution. CONCLUSIONS: There were no significant differences in postoperative pain, swelling, or bleeding with the use of plain versus buffered lidocaine in eyelid surgery. There was a trend for the buffered anesthetic to cause less pain on injection.

Regional dissection and determination of loosely bound and non-heme iron in the developing mouse brain.

Iron is a trace metal essential for normal brain development but toxic in excess as it is capable of generating highly reactive radicals that damage cells and tissue. Iron is stringently regulated by the iron regulatory proteins, IRP1 and IRP2, which regulate proteins involved in iron homeostasis at the posttranscriptional level. In this study, 12 distinct regions were microdissected from the mouse brain and regional changes in the levels of loosely bound and non-heme iron that occur with development were measured. We examined 6, 12, and 24 week old wildtype C57BL/6 mice and mice with a targeted deletion of iron regulatory protein 2 (IRP2-/-) that have been reported to develop neurodegenerative symptoms in adulthood. In wildtype mice, levels of loosely bound iron decreased while non-heme iron increased with development. In contrast, an increase in loosely bound and a more pronounced increase in non-heme iron was seen in IRP2-/- mice between 6 and 12 weeks of age, stemming from lower levels at 6 weeks (the youngest age examined) compared to wildtype. These results have implications for understanding the increase in regional brain iron that is associated with normal aging and is postulated to be exacerbated in neurodegenerative disorders.

The PIM-2 kinase phosphorylates BAD on serine 112 and reverses BAD-induced cell death.

Hematopoietic growth factors mediate the survival and proliferation of blood-forming cells, but the mechanisms through which these proteins produce their effects are incompletely known. Recent studies have identified the pim family of kinases as mediators of cytokine-dependent survival signals. Several studies have identified substrates for the pim-1 kinase, but little is known about the other family members, pim-2 and pim-3. We have investigated potential functions for the pim-2 kinase in factor-dependent murine hematopoietic cells. We find that pim-2 mRNA and protein expression are regulated by cytokines similarly to pim-1. Three PIM-2 protein isoforms are produced in cytokine-treated cells. All three forms are active kinases, and the short (PIM-2(34 kDa)) form is the most active at enhancing survival of FDCP1 cells after cytokine withdrawal. This pro-survival function involves inhibition of apoptosis and caspase activation. Enforced expression of PIM-2(34 kDa) kinase does not appear to regulate expression of BCL-2, BCL-xL, BIM, or BAX proteins. However, the kinase can phosphorylate the pro-apoptotic protein BAD on serine 112, which accounts in part for its ability to reverse Bad-induced cell death. Our results indicate that pim-2 functions similarly to pim-1 as a pro-survival kinase and suggest that BAD is a legitimate PIM-2 substrate.