8
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: not found
      • Article: not found

      Evaluation of cutaneous rejuvenation associated with the use of ortho-silicic acid stabilized by hydrolyzed marine collagen

      Read this article at

      ScienceOpenPublisher
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Related collections

          Most cited references21

          • Record: found
          • Abstract: not found
          • Article: not found

          Orthosilicic acid stimulates collagen type 1 synthesis and osteoblastic differentiation in human osteoblast-like cells in vitro

            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            Characteristics of the Aging Skin

            Although most researches into the changes in skin with age focus on the unwelcome aesthetic aspects of the aging skin, skin deterioration with age is more than a merely cosmetic problem. Although mortality from skin disease is primarily restricted to melanoma, dermatological disorders are ubiquitous in older people with a significant impact on quality of life. The structural and functional deterioration of the skin that occurs with age has numerous clinical presentations, ranging from benign but potentially excruciating disorders like pruritus to the more threatening carcinomas and melanomas.
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              A bound form of silicon in glycosaminoglycans and polyuronides.

              Silicon was found to be a constituent of certain glycosaminoglycans and polyuronides, where it occurs firmly bound to the polysaccharide matrix. 330-554 ppm of bound Si were detected in purified hyaluronic acid from umbilical cord, chondroitin 4-sulfate, dermatan sulfate, and heparan sulfate. These amounts correspond to 1 atom of Si per 50,000-85,000 molecular weight or 130-280 repeating units. 57-191 ppm occur in chondroitin 6-sulfate, heparin, and keratan sulfate-2 from cartilage, while hyaluronic acids from vitreous humor and keratan sulfate-1 from cornea were Si-free. Large amounts of bound Si are also present in pectin (2580 ppm) and alginic acid (451 ppm). The bound Si is not dialyzable, does not react with ammonium molybdate, is not liberated by autoclaving or 8 M urea, and is stable against weak alkali and acid. Strong alkali and acid hydrolyze the Si-polysaccharide bond. Free, direct-reacting, dialyzable silicate is obtained. Enzymatic hydrolysis of hyaluronic acid or pectin does not liberate silicic acid, but leads to products of low molecular weight still containing Si in bound form. It is concluded that Si is present as a silanolate, i.e., an ether (or esterlike) derivative of silicic acid, and that R(1)-O-Si-O-R(2) or R(1)-O-Si-O-Si-O-R(2) bridges play a role in the structural organization of glycosaminoglycans and polyuronides. Thus, Si may function as a biological crosslinking agent and contribute to architecture and resilience of connective tissue.
                Bookmark

                Author and article information

                Journal
                Journal of Cosmetic Dermatology
                J Cosmet Dermatol
                Wiley
                14732130
                October 2018
                October 2018
                September 20 2017
                : 17
                : 5
                : 814-820
                Affiliations
                [1 ]Célia Kalil Dermatologic Clinic; Porto Alegre-Rio Grande de Sul Brazil
                [2 ]Valéria Campos Dermatologic Clinic; Jundiaí-São Paulo Brazil
                [3 ]Pharmaceutical; Farmatec Pharmacy; Porto Alegre Brazil
                Article
                10.1111/jocd.12430
                0c607e34-9803-4298-bec5-d2371b765f9e
                © 2017

                http://doi.wiley.com/10.1002/tdm_license_1.1

                http://onlinelibrary.wiley.com/termsAndConditions#vor

                History

                Comments

                Comment on this article