The scientific basis and empiric evidence supporting the use of various agents is presented. Combination therapy, using surgical excision followed by intradermal steroid or other adjuvant therapy, currently appears to be the most efficacious and safe current regimen for keloid management.

Needlestick injuries are common among surgeons in training and are often not reported. Improved prevention and reporting strategies are needed to increase occupational safety for surgical providers.

This is a clinical review of current techniques in wound bed preparation found to be effective in assisting the wound-healing process. The process begins with the identification of a correct diagnosis of the wound's etiology and continues with optimizing the patient's medical condition, including blood flow to the wound site. Débridement as the basis of most wound-healing strategies is then emphasized. Various débridement techniques, including surgery, topical agents, and biosurgery, are thoroughly discussed and illustrated. Wound dressings, including the use of negative pressure wound therapy, are then reviewed. To properly determine the timing of advance therapeutic intervention, the wound-healing progress needs to be monitored carefully with weekly measurements. A reduction in wound area of 10 to 15 percent per week represents normal healing and does not mandate a change in the current wound-healing strategy. However, if this level of wound area reduction is not met consistently on a weekly basis, then alternative healing interventions should be considered. There is a growing body of evidence that can provide guidance on the appropriate use of such adjuvants in the problem wound. Several adjuvants are discussed, including growth factor, bioengineered tissues, and hyperbaric medicine.

No abstract

Fibroblast growth factor-binding protein (FGF-BP) 1 is a secreted protein that can bind fibroblast growth factors (FGFs) 1 and 2. These FGFs are typically stored on heparan sulfate proteoglycans in the extracellular matrix in an inactive form, and it has been proposed that FGF-BP1 functions as a chaperone molecule that can mobilize locally stored FGF and present the growth factor to its tyrosine kinase receptor. FGF-BP1 is upregulated in squamous cell, colon, and breast cancers and can act as an angiogenic switch during malignant progression of epithelial cells. For the present studies, we focused on FGF-1 and -2 and investigated interactions with recombinant human FGF-BP1 protein as well as effects on signal transduction, cell proliferation, and angiogenesis. We show that recombinant FGF-BP1 specifically binds FGF-2 and that this binding is inhibited by FGF-1, heparan sulfate, and heparinoids. Furthermore, FGF-BP1 enhances FGF-1-and FGF-2-dependent proliferation of NIH-3T3 fibroblasts and FGF-2-induced extracellular signal-regulated kinase 2 phosphorylation. Finally, in the chicken chorioallantoic membrane angiogenesis assay, FGF-BP1 synergizes with exogenously added FGF-2. We conclude that FGF-BP1 binds directly to FGF-1 and FGF-2 and positively modulates the biological activities of these growth factors. Fibroblast growth factors (FGFs)1 represent a family of over 20 distinct proteins that are widely expressed in various tissues. FGFs have been reported to be involved in both development and adult tissue homeostasis, as well as in angiogenesis and cancer progression. FGF-2 (basic FGF), a 16 -18-kDa protein, is one of the best-studied members of this family and has been shown to have a variety of biological effects in different cells and organ systems, including embryonic development, tumorigenesis, and angiogenesis (for a review, see Refs. 1 and 2).FGF-2 interacts with low affinity cell surface and extracellular matrix heparan sulfate proteoglycans, which enable the growth factor to bind and activate its high affinity tyrosine kinase receptors (FGFRs), thereby forming a trimolecular active complex (3-6). It has been reported that cell surface heparan sulfate proteoglycans can modulate the action of FGF-2 by increasing its affinity for FGFRs (7). Moreover, heparan sulfate proteoglycans seem to protect FGF-2 from degradation by proteases in the extracellular environment (8, 9) and modulate the bioavailability of FGF-2, generating a local reservoir for the growth factor (10). The binding of FGF-2 to the cell surface receptor induces receptor tyrosine kinase dimerization and autophosphorylation (11). The phosphorylated FGFRs associate and subsequently activate SH2 domain-containing downstream signaling molecules, such as phospholipase C␥ (12, 13) and Src (14,15). Moreover, upon ligand-dependent receptor autophosphorylation, adaptor proteins, such as Grb2 and Shc, link the FGFRs to the Ras/MAPK signaling cascade (16 -18). Grb2 and Shc form a complex with the GDP/GTP exchange factor Son of Sevenless (Sos), which ...

Therapeutic, IV.

The course of these two nerves differs in several critical aspects from that described in classic anatomical reports. These findings have direct implications for application of nerve blocks and surgical decompression of these nerves.

In certain patients undergoing microvascular free flap reconstruction, undiagnosed hypercoagulability risk factors can be a source of free flap failure that is independent of patient selection or technical factors. Diagnosis, management, patient counseling, and initiation of deep venous thromboembolism prophylaxis measures are critical clinical components of care of these patients.