Introduction: Current research within other surgical specialties suggests that a co-surgeon

Given the short recovery and immediate results, facial fillers have become a popular alternative to surgical rejuvenation of the face. Reported complications arising from facial filler injections include erythema, tissue loss, blindness, stroke, and even death. In this article, the authors describe their anatomically based techniques to minimize risk and maximize safety when injecting in the facial danger zones, including the glabella/brow, temporal region, perioral region, nasolabial fold, nose, and infraorbital region. Complications generally arise secondary to vasculature injury and/or cannulation with filler. The authors have outlined their preferred injection techniques in the facial danger zones with respect to the pertinent anatomy in an attempt to minimize risk and maximize results. Most importantly, the practitioner should be able to recognize complications and address them immediately.

"Extra" domains in members of the families of secondary transport carrier and channel proteins provide secondary functions that expand, amplify or restrict the functional nature of these proteins. Domains in secondary carriers include TrkA and SPX domains in DASS family members, DedA domains in TRAP-T family members (both of the IT superfamily), Kazal-2 and PDZ domains in OAT family members (of the MF superfamily), USP, IIA(Fru) and TrkA domains in ABT family members (of the APC superfamily), ricin domains in OST family members, and TrkA domains in AAE family members. Some transporters contain highly hydrophilic domains consisting of multiple repeat units that can also be found in proteins of dissimilar function. Similarly, transmembrane alpha-helical channel-forming proteins contain unique, conserved, hydrophilic domains, most of which are not found in carriers. In some cases the functions of these domains are known. They may be ligand binding domains, phosphorylation domains, signal transduction domains, protein/protein interaction domains or complex carbohydrate-binding domains. These domains mediate regulation, subunit interactions, or subcellular targeting. Phylogenetic analyses show that while some of these domains are restricted to closely related proteins derived from specific organismal types, others are nearly ubiquitous within a particular family of transporters and occur in a tremendous diversity of organisms. The former probably became associated with the transporters late in the evolutionary process; the latter probably became associated with the carriers much earlier. These domains can be located at either end of the transporter or in a central region, depending on the domain and transporter family. These studies provide useful information about the evolution of extra domains in channels and secondary carriers and provide novel clues concerning function.

Therapeutic, IV.

Diagnostic, IV.