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      Anti-Aging Effects of the Hanwoo Leg Bone, Foot and Tail Infusions (HLI, HFI and HTI) on Skin Fibroblast

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          Abstract

          Many researchers revealed that collagen contribute to maintaining the skin’s elasticity and inhibit wrinkling of skin. Korean native cattle ( Hanwoo) bone (leg bone, foot and tail) infusion contains the various inorganic materials, collagen and chondroitin sulfate. All of this, a large quantity of collagen is included in Hanwoo infusion. Therefore, this study emphasized on the effects of collagen in the Hanwoo bone infusion. For the first time, Hanwoo bone infusions were directly added to the media of Human Dermal Fibroblast (NHDF-c) to test anti-aging effects. First, it was identified that growth rate of skin fibroblast was increased. Furthermore, the Hanwoo bone infusion increased a 50% of fibroblast collagen synthesis. Also, suppression of skin fibroblast aging was confirmed by treatment Hanwoo bone infusion. In conclusion, this study demonstrates the effects of infusion made from Hanwoo leg bone, foot and tail on anti-aging, wrinkle inhibiting and skin fibroblast elasticity maintaining. Therefore, this study identified that traditional infusion has effects that are good for skin elasticity.

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          Collagen cross-links as a determinant of bone quality: a possible explanation for bone fragility in aging, osteoporosis, and diabetes mellitus.

          M. Saito, K Marumo (2010)
          Collagen cross-linking, a major post-translational modification of collagen, plays important roles in the biological and biomechanical features of bone. Collagen cross-links can be divided into lysyl hydroxylase and lysyloxidase-mediated enzymatic immature divalent cross-links,mature trivalent pyridinoline and pyrrole cross-links, and glycation- or oxidation-induced non-enzymatic cross-links(advanced glycation end products) such as glucosepane and pentosidine. These types of cross-links differ in the mechanism of formation and in function. Material properties of newly synthesized collagen matrix may differ in tissue maturity and senescence from older matrix in terms of crosslink formation. Additionally, newly synthesized matrix in osteoporotic patients or diabetic patients may not necessarily be as well-made as age-matched healthy subjects. Data have accumulated that collagen cross-link formation affects not only the mineralization process but also microdamage formation. Consequently, collagen cross-linking is thought to affect the mechanical properties of bone. Furthermore,recent basic and clinical investigations of collagen cross-links seem to face a new era. For instance, serum or urine pentosidine levels are now being used to estimate future fracture risk in osteoporosis and diabetes. In this review, we describe age-related changes in collagen cross-links in bone and abnormalities of cross-links in osteoporosis and diabetes that have been reported in the literature.
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            Identification of food-derived collagen peptides in human blood after oral ingestion of gelatin hydrolysates.

            Takanori Hasegawa, Leo K. Iwai, Akane Higashi … (2005)
            In the present study, we identified several food-derived collagen peptides in human blood after oral ingestion of some gelatin hydrolysates. Healthy human volunteers ingested the gelatin hydrolysates (9.4-23 g) from porcine skin, chicken feet, and cartilage after 12 h of fasting. Negligible amounts of the peptide form of hydroxyproline (Hyp) were observed in human blood before the ingestion. After the oral ingestion, the peptide form of Hyp significantly increased and reached a maximum level (20-60 nmol/mL of plasma) after 1-2 h and then decreased to half of the maximum level at 4 h after the ingestion. Major constituents of food-derived collagen peptides in human serum and plasma were identified as Pro-Hyp. In addition, small but significant amounts of Ala-Hyp, Ala-Hyp-Gly, Pro-Hyp-Gly, Leu-Hyp, Ile-Hyp, and Phe-Hyp were contained.
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              Adhesion to Vitronectin and Collagen I Promotes Osteogenic Differentiation of Human Mesenchymal Stem Cells

              Roman Salasznyk, William A. Williams, Adele L. Boskey … (2004)
              The mechanisms controlling human mesenchymal stem cells (hMSC) differentiation are not entirely understood. We hypothesized that the contact with extracellular matrix (ECM) proteins normally found in bone marrow would promote osteogenic differentiation of hMSC in vitro. To test this hypothesis, we cultured hMSC on purified ECM proteins in the presence or absence of soluble osteogenic supplements, and assayed for the presence of well-established differentiation markers (production of mineralized matrix, osteopontin, osteocalcin, collagen I, and alkaline phosphatase expression) over a 16-day time course. We found that hMSC adhere to ECM proteins with varying affinity ( fibronectin > collagen I ≥ collagen IV ≥ vitronectin > laminin-1 ) and through distinct integrin receptors. Importantly, the greatest osteogenic differentiation occurred in cells plated on vitronectin and collagen I and almost no differentiation took place on fibronectin or uncoated plates. We conclude that the contact with vitronectin and collagen I promotes the osteogenic differentiation of hMSC, and that ECM contact alone may be sufficient to induce differentiation in these cells.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Korean J Food Sci Anim Resour
                Journal ID (iso-abbrev): Korean J Food Sci Anim Resour
                Journal ID (publisher-id): ksfsar
                Title: Korean Journal for Food Science of Animal Resources
                Publisher: Korean Society for Food Science of Animal Resources
                ISSN (Print): 1225-8563
                ISSN (Electronic): 2234-246X
                Publication date (Print): 2016
                Publication date (Electronic): 30 April 2016
                Volume: 36
                Issue: 2
                Pages: 237-243
                Affiliations
                [1] Division of Biological Science, Sookmyung Women’s University, Seoul 04310, Korea
                [1 ] Department of Le Cordon Blue Hospitality Management, Sookmyung Women's University, Seoul 04310, Korea
                [2 ] Traditional Dietary Life Food, Graduate School of Traditional Culture and Arts, Sookmyung Women's University, Seoul 04310, Korea
                [3 ] Department of Food & Nutrition, Sookmyung Women's University, Seoul 04310, Korea
                Author notes
                [* ]Corresponding author: Soon Young Choi, Division of Biological Science, Sookmyung Women's University, Seoul 04310, Korea. Tel:+82-2-710-9510, Fax:+82-2-2077-7322, E-mail: sychoi@ 123456sookmyung.ac.kr
                Article
                Publisher ID: kosfa-36-237
                DOI: 10.5851/kosfa.2016.36.2.237
                PMC ID: 4869551
                PubMed ID: 27194933
                SO-VID: 3ec90e7c-f986-4d79-a344-30d3aa96d2bf
                Copyright © Copyright © 2016, Korean Society for Food Science of Animal Resources
                License:

                This is an open access article distributed under the terms of the Creative Commons Attribution Non-Commercial License ( http://creativecommons.org/licences/by-nc/3.0) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                Date received : 06 September 2015
                Date revision received : 22 February 2016
                Date accepted : 22 February 2016
                Categories
                Subject: Article

                Keywords: korean native cattle (hanwoo),leg bone infusion,foot infusion,tail infusion,skin fibroblast (nhdf-c),anti-aging
                Data availability:
                Keywords: korean native cattle (hanwoo), leg bone infusion, foot infusion, tail infusion, skin fibroblast (nhdf-c), anti-aging

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