No abstract

Plastic surgeons are keenly aware of the principle "replace like with like." This principle underlies much of the rationale behind the clinical use of autologous fat transplantation, despite the procedure's drawbacks. Autologous fat transplantation is frequently used for a variety of cosmetic and reconstructive indications not limited to posttraumatic defects of the face and body, involutional disorders such as hemifacial atrophy, sequelae of radiation therapy, and many aesthetic uses such as lip and facial augmentation and wrinkle therapy. However, the limitations of fat transplantation are well known, particularly the long-term unpredictability of volume maintenance. Regenerative cell-based strategies such as those encompassing the use of stem cells hold tremendous promise for augmentation of the soft-tissue space. Preclinical studies and early clinical series show that adipose-derived stem cells offer the possibility of finally fulfilling the key principle of replacing like with like as an aesthetic filler, without the drawbacks of current technology.

Autologous adipose tissue derived stem and regenerative cells, as used in this disc injury model, were effective in promoting disc regeneration, as evidenced by disc matrix production and overall disc morphology.

Members of the interleukin-17 cytokine family are present in a variety of tissues (1-3), although the founding member, interleukin-17, is expressed exclusively in T cells and B cells (4 -8). The cloning and characterization of a novel single-pass transmembrane protein with limited homology to the interleukin-17 receptor is reported. High mRNA levels were detected in prostate, cartilage, kidney, liver, heart, and muscle, whereas transcripts were barely detected in thymus and leukocytes. At least 11 RNA splice variants were found, transcribed from 19 exons on human chromosome 3p25.3-3p24.1. Differential exon usage was found in different tissues by quantitative reverse transcriptase-PCR. Predicted proteins range from 186 to 720 amino acids. Soluble secreted proteins lacking transmembrane and intracellular domains are predicted from several splice isoforms and may function as extracellular antagonists to cytokine signaling by functioning as soluble decoy receptors. Using antibodies directed at the cytoplasmic and extracellular domains of this protein, we investigated its localization and found that it was expressed in a variety of normal human tissues including prostate and in prostate cancer.Interleukins were historically defined as soluble secreted factors expressed in immune cells that mediate interactions between leukocytes. However, this definition has evolved to include cytokines with a spectrum of pleiotropic actions (reviewed in Refs. 9 and 10). Interleukin-17 is a recently discovered cytokine that exerts its effect on many different tissues due to the nearly ubiquitous distribution of its receptor (5,(11)(12)(13)(14)(15). 1 is a proinflammatory cytokine that has been implicated in a number of diseases including rheumatoid arthritis (16 -18), allergic skin immune response (19), organ transplant rejection (20 -23), and multiple sclerosis (24). Recent work has identified three related proteins, establishing an IL-17 family of cytokines. These new family members, IL-17B, IL-17C, and IL-17E, share 20 -30% homology with IL-17 and have four conserved cysteines, and all contain a putative Nterminal signal peptide typically required for secretion (1-3).The IL-17 signaling pathway is currently being studied. Although it is not a kinase itself, the IL-17 receptor (IL-17R) has been shown to transduce its signal through the activation of ERK, JNK/SAPK, and p38 MAP kinase pathways (25-27). In the presence of IL-17 ligand, these pathways lead to the upregulation of genes typically associated with inflammation, such as stromelysin, IL-6, and IL-1␤, and the activation of NFkB (28 -30). One additional receptor was first identified as a receptor for IL-17B and named IL-17BR (3). This receptor was subsequently shown to have greater affinity for IL-17E than for IL-17B and was also named IL-17Rh1. This receptor was shown to activate NFkB in an in vitro luciferase assay (2). However, the signal transduction pathway and the in vivo functions of this receptor are not known.The existence of several IL-17-related proteins led us to ...