A Combined Treatment Proposal for the Empty Deep Pyriform Space.

Background: Deepening of the nasolabial fold (NLF), drooping of the nasal tip, and facial expressions perceived as angry face, are common esthetic concerns. However, no studies have correlated this set of signs and symptoms with common anatomical causes. We review anatomical considerations of the region and propose a combined treatment modality.

An Innovative Treatment Using Calcium Hydroxyapatite for Non-Surgical Facial Rejuvenation: The Vectorial-Lift Technique.

Background: The facial aging process entails alterations in the volume, shape, and texture of all skin layers over time. Calcium hydroxyapatite (CaHA) is a well-established safe skin filler with unique properties to resolve some skin alterations by stimulating neocollagenesis. The vectoral-lift (V-lift) technique targets the global repositioning of facial structures by addressing distinct anatomical injection planes.

Advanced Injection of Botulinum Toxin in the Nasal Muscles: A Novel Dynamic Change in Facial Expression.

Background: Among the nasal muscles, the levator labii superior alaeque nasi (LLSAN) acts as a transitional muscle that conjugates with other nasal and perinasal muscles. Thus, when treating the nasal region with Botulinum toxin (BTX), it is important to understand local nasal muscular dynamics and how they can influence the muscular dynamics of the entire face.

Methods: This is a retrospective analysis of cases treated by an injection pattern encompassing the face, including nasal muscles.

Defensin 1 Eradicates Mouse Metastatic Lung Nodules from B16F10 Melanoma Cells.

d1 is a pea plant defensin which can be actively expressed in and shows broad antifungal activity. This activity is dependent on fungal membrane glucosylceramide (GlcCer), which is also important for its internalization, nuclear localization, and endoreduplication. Certain cancer cells present a lipid metabolism imbalance resulting in the overexpression of GlcCer in their membrane.

Nuclear magnetic resonance solution structure of Pisum sativum defensin 2 provides evidence for the presence of hydrophobic surface-clusters.

Pisum sativum defensin 2 (Psd2) is a small (4.7 kDa) antifungal peptide whose structure is held together by four conserved disulfide bridges. Psd2 shares the cysteine-stabilized alpha-beta (CSαβ) fold, which lacks a regular hydrophobic core.

Psd2 pea defensin shows a preference for mimetic membrane rafts enriched with glucosylceramide and ergosterol.

Psd2 is a pea defensin with 47 amino acid residues that inhibits the growth of fungal species by an uncharacterized mechanism. In this work, Psd2 interactions with model membranes mimicking the lipid compositions of different organisms were evaluated. Protein-lipid overlay assays indicated that Psd2 recognizes Fusarium solani glucosylceramide (GlcCer) and ergosterol (Erg) in addition to phosphatidylcholine (POPC) and some phosphatidylinositol species, such as PtdIns (3)P, (5)P and (3,5)P, suggesting that these lipids may play important roles as Psd2 targets.