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      • Record: found
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      Hydrolyzed Collagen—Sources and Applications

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          Abstract

          Hydrolyzed collagen (HC) is a group of peptides with low molecular weight (3–6 KDa) that can be obtained by enzymatic action in acid or alkaline media at a specific incubation temperature. HC can be extracted from different sources such as bovine or porcine. These sources have presented health limitations in the last years. Recently research has shown good properties of the HC found in skin, scale, and bones from marine sources. Type and source of extraction are the main factors that affect HC properties, such as molecular weight of the peptide chain, solubility, and functional activity. HC is widely used in several industries including food, pharmaceutical, cosmetic, biomedical, and leather industries. The present review presents the different types of HC, sources of extraction, and their applications as a biomaterial.

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          Tricine-SDS-PAGE.

          Hermann Schägger (2006)
          Tricine-SDS-PAGE is commonly used to separate proteins in the mass range 1-100 kDa. It is the preferred electrophoretic system for the resolution of proteins smaller than 30 kDa. The concentrations of acrylamide used in the gels are lower than in other electrophoretic systems. These lower concentrations facilitate electroblotting, which is particularly crucial for hydrophobic proteins. Tricine-SDS-PAGE is also used preferentially for doubled SDS-PAGE (dSDS-PAGE), a proteomic tool used to isolate extremely hydrophobic proteins for mass spectrometric identification, and it offers advantages for resolution of the second dimension after blue-native PAGE (BN-PAGE) and clear-native PAGE (CN-PAGE). Here I describe a protocol for Tricine-SDS-PAGE, which includes efficient methods for Coomassie blue or silver staining and electroblotting, thereby increasing the versatility of the approach. This protocol can be completed in 1-2 d.
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            Decreased collagen production in chronologically aged skin: roles of age-dependent alteration in fibroblast function and defective mechanical stimulation.

            James Varani, Michael Dame, Laure Rittié … (2006)
            Reduced synthesis of collagen types I and III is characteristic of chronologically aged skin. The present report provides evidence that both cellular fibroblast aging and defective mechanical stimulation in the aged tissue contribute to reduced collagen synthesis. The reduction in collagen synthesis due to fibroblast aging was demonstrated by a lower in vitro production of type I procollagen by dermal fibroblasts isolated from skin of young (18 to 29 years) versus old (80+ years) individuals (82 +/- 16 versus 56 +/- 8 ng/ml; P < 0.05). A reduction in mechanical stimulation in chronologically aged skin was inferred from morphological, ultrastructural, and fluorescence microscopic studies. These studies, comparing dermal sections from young and old individuals, demonstrated a greater percentage of the cell surface attached to collagen fibers (78 +/- 6 versus 58 +/- 8%; P < 0.01) and more extensive cell spreading (1.0 +/- 0.3 vs. 0.5 +/- 0.3; P < 0.05) in young skin compared with old skin. These features are consistent with a lower level of mechanical stimulation on the cells in old versus young skin. Based on the findings presented here, we conclude that reduced collagen synthesis in chronologically aged skin reflects at least two different underlying mechanisms: cellular fibroblast aging and a lower level of mechanical stimulation.
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              Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons.

              F Hillenkamp, Michael Karas, M Karas (1988)
              Article 0 comments Cited 162 times – based on 0 reviews     Review now
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                Author and article information

                Contributors
                Manuela Pintado: Role: Academic Editor
                Ezequiel Coscueta: Role: Academic Editor
                María Emilia Brassesco: Role: Academic Editor
                Journal
                Journal ID (nlm-ta): Molecules
                Journal ID (iso-abbrev): Molecules
                Journal ID (publisher-id): molecules
                Title: Molecules
                Publisher: MDPI
                ISSN (Electronic): 1420-3049
                Publication date (Electronic): 07 November 2019
                Publication date Collection: November 2019
                Volume: 24
                Issue: 22
                Electronic Location Identifier: 4031
                Affiliations
                [1 ]Instituto de Ciencias Agropecuarias, Universidad Autónoma del Estado de Hidalgo, Av. Universidad km 1. Ex Hacienda de Aquetzalpa. Tulancingo, Hidalgo 43600, Mexico; arlely@ 123456hotmail.com (A.L.-L.); victormj@ 123456uaeh.edu.mx (V.M.M.-J.); apolovt@ 123456hotmail.com (A.V.-T.)
                [2 ]Universidad Autónoma del Estado de Hidalgo, Escuela Superior de Apan, Carretera Apan-Calpulalpan s/n, Colonia, Chimalpa Tlalayote, Apan, Hidalgo 43920 Mexico; lacirem71@ 123456yahoo.com.mx
                [3 ]Regenerative, Modular & Developmental Engineering Laboratory (REMODEL), National University of Ireland Galway (NUI Galway), H91 TK33 Galway, Ireland; dimitrios.zeugolis@ 123456nuigalway.ie
                [4 ]Science Foundation Ireland (SFI) Centre for Research in Medical Devices (CÚRAM) National University of Ireland Galway (NUI Galway), H91 TK33 Galway, Ireland
                Author notes
                [* ]Correspondence: aguirre@ 123456uaeh.edu.mx ; Tel.: +52-775-145-9265
                Author information
                https://orcid.org/0000-0002-7599-5191
                https://orcid.org/0000-0001-7652-2647
                Article
                Publisher ID: molecules-24-04031
                DOI: 10.3390/molecules24224031
                PMC ID: 6891674
                PubMed ID: 31703345
                SO-VID: ce23b083-e23d-470e-ad67-d85553ab13e4
                Copyright © © 2019 by the authors.
                License:

                Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                Date received : 07 October 2019
                Date accepted : 05 November 2019
                Categories
                Subject: Review

                Keywords: hydrolyzed collagen,peptide,antioxidant activity,denaturation,hydrolysates
                Data availability:
                Keywords: hydrolyzed collagen, peptide, antioxidant activity, denaturation, hydrolysates

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