Peptides Abstracts 2

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The role of biologically active peptides in tissue repair using umbilical cord mesenchymal stem cells.
            (Cabrera et al., 2012) Download
The role of bioactive compounds in wound repair is critical. The preliminary work described herein includes the study of the effects of second degree burns in a Rex rabbit model and the action of human umbilical cord cells on the regulation and secretion of bioactive compounds. When applied on blood scaffolds as heterograft matrices, fibroblasts proliferate from these primary cultures and release biologically active peptides under tight control. Our work in progress indicates that mesenchymal stem cell (MSC)-mediated therapy provides better quality and more efficient burn reepithelialization of injured tissues by controlling the release of these peptides. Improvement of wound aesthetics is achieved in less time than without MSC-mediated therapy. Well-organized epidermal regeneration and overall better quality of reepithelialization, with no rejection, can be demonstrated consistently with periodic biopsies. Our studies indicate that MSCs have the capacity to produce, regulate, and deliver biologically active peptides that result in superior regeneration, compared with conventional treatments.

Antioxidant activity of proteins and peptides.
            (Elias et al., 2008) Download
Proteins can inhibit lipid oxidation by biologically designed mechanisms (e.g. antioxidant enzymes and iron-binding proteins) or by nonspecific mechanisms. Both of these types of antioxidative proteins contribute to the endogenous antioxidant capacity of foods. Proteins also have excellent potential as antioxidant additives in foods because they can inhibit lipid oxidation through multiple pathways including inactivation of reactive oxygen species, scavenging free radicals, chelation of prooxidative transition metals, reduction of hydroperoxides, and alteration of the physical properties of food systems. A protein's overall antioxidant activity can be increased by disruption of its tertiary structure to increase the solvent accessibility of amino acid residues that can scavenge free radicals and chelate prooxidative metals. The production of peptides through hydrolytic reactions seems to be the most promising technique to form proteinaceous antioxidants since peptides have substantially higher antioxidant activity than intact proteins. While proteins and peptides have excellent potential as food antioxidants, issues such as allergenicity and bitter off-flavors as well as their ability to alter food texture and color need to be addressed.

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A novel anti-ageing mechanism for retinol: induction of dermal elastin synthesis and elastin fibre formation.
            (Rossetti et al., 2011) Download
Dermal elastic fibres are extracellular matrix protein complexes produced by fibroblasts and involved in skin elasticity. Elastin fibres decrease with age as a result of reduced synthesis and increased degradation, resulting in skin sagging and reduced skin elasticity. In this study, we show that retinol (ROL), known to enhance dermal collagen production, is also enhancing elastin fibre formation. ROL induced elastin gene expression and elastin fibre formation in cultured human dermal fibroblasts. Topical treatment of cultured human skin explants with a low dose (0.04%) of ROL increased mRNA and protein levels of tropoelastin and of fibrillin-1, an elastin accessory protein, as documented by QPCR and immunohistochemistry staining. Luna staining confirmed the increased elastin fibre network in the ROL-treated skin explants, as compared with untreated controls. These data demonstrate that ROL exerts its anti-ageing benefits not only via enhanced epidermal proliferation and increased collagen production, but also through an increase in elastin production and assembly.

Immediate and Long-term Clinical Benefits of a Topical Treatment for Facial Lines and Wrinkles.
            (Trookman et al., 2009) Download
OBJECTIVE:  To evaluate the efficacy and tolerance of a novel line treatment for periocular and perioral wrinkles. The line treatment was formulated with multiple growth factors, antioxidants, and a collagen-building peptide-ingredients that have been shown to increase collagen levels and provide long-term aesthetic benefits. To help provide immediate smoothing effects, hyaluronic acid filling spheres and a muscle contraction-inhibiting peptide were also included in the formulation. DESIGN:  Three-month, single-center, open-label, clinical study with clinical assessments at Baseline, Minutes (within 15 minutes of initial application), Month 1, and Month 3. TREATMENT:  Subjects treated periocular and perioral wrinkles twice daily for three months with the line treatment. PARTICIPANTS:  Thirty-seven females, 33 to 45 years of age, with mild-to-moderate, fine and coarse periocular and perioral wrinkles, were enrolled in the study. MEASUREMENTS:  Investigator assessments of fine and coarse periocular and perioral wrinkles, digital photography, and tolerance assessments were conducted at all visits. Subject self-assessment questionnaires were conducted within 15 minutes of initial application and at Month 3. RESULTS:  Investigator assessments of both periocular and perioral wrinkles showed statistically significant improvements over Baseline within minutes of initial application; these positive findings continued to improve through Months 1 and 3 (all P</=0.0003). No treatment-related adverse events were reported. CONCLUSIONS:  The results from this study demonstrate that this uniquely formulated line treatment was well tolerated and provided both immediate and long-term improvements in the appearance of fine and coarse wrinkles.

Laminin peptide YIGSR induces collagen synthesis in Hs27 human dermal fibroblasts.
            (Yoon et al., 2012) Download
The dermal ECM is synthesized from fibroblasts and is primarily compromised of fibrillar collagen and elastic fibers, which support the mechanical strength and resiliency of skin, respectively. Laminin, a major glycoprotein located in the basement membrane, promotes cell adhesion, cell growth, differentiation, and migration. The laminin tyrosine-isoleucine-glycine-serine-arginine (YIGSR) peptide, corresponding to the 929-933 sequence of the β1 chain, is known to be a functional motif with effects on the inhibition of tumor metastasis, the regulation of sensory axonal response and the inhibition of angiogenesis through high affinity to the 67kDa laminin receptor. In this study, we identified a novel function of the YIGSR peptide to enhance collagen synthesis in human dermal fibroblasts. To elucidate this novel function regarding collagen synthesis, we treated human dermal fibroblasts with YIGSR peptide in both a time- and dose-dependent manner. According to subsequent experiments, we found that the YIGSR peptide strongly enhanced collagen type 1 synthesis without changing cell proliferation or cellular MMP-1 level. This YIGSR peptide-mediated collagen type 1 synthesis was modulated by FAK inhibitor and MEK inhibitor. This study clearly reveals that YIGSR peptide plays a novel function on the collagen type 1 synthesis of dermal fibroblasts and also suggests that YIGSR is a strong candidate peptide for the treatment of skin aging and wrinkles.

 


References

Cabrera, C, et al. (2012), ‘The role of biologically active peptides in tissue repair using umbilical cord mesenchymal stem cells.’, Ann N Y Acad Sci, 1270 93-97. PubMed: 23050823
Elias, RJ, SS Kellerby, and EA Decker (2008), ‘Antioxidant activity of proteins and peptides.’, Crit Rev Food Sci Nutr, 48 (5), 430-41. PubMed: 18464032
Rossetti, D, et al. (2011), ‘A novel anti-ageing mechanism for retinol: induction of dermal elastin synthesis and elastin fibre formation.’, Int J Cosmet Sci, 33 (1), 62-69. PubMed: 20704601
Trookman, NS, et al. (2009), ‘Immediate and Long-term Clinical Benefits of a Topical Treatment for Facial Lines and Wrinkles.’, J Clin Aesthet Dermatol, 2 (3), 38-43. PubMed: 20729942
Yoon, JH, et al. (2012), ‘Laminin peptide YIGSR induces collagen synthesis in Hs27 human dermal fibroblasts.’, Biochem Biophys Res Commun, 428 (3), 416-21. PubMed: 23111328