• Korean Journal of Plant Resources
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• v.25 no.2
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• pp.240-245
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• 2012

In this study, we investigated the boosting effects on collagen biosynthesis of $Anthriscus$ $sylvestris$ ethanol extract (ASE) in human dermal fibroblasts. To obtain more effective fraction and subfraction for collagen biosynthesis, standard solvent partition and open column chromatography were performed. The EtOH extract, solvent fractions, and 8 EtOAc subfractions were tested for their collagen synthesis capacity by [$^3H$]Proline-incorporation and ELISA assay. ASE increased 25% of total collagen synthesis and 27% of procollagen biosynthesis. The total collagen biosynthesis was increased by EtOAc fraction and E6 subfraction to 28% and 50% respectively. Type I procollagens were also upregulated by EtOAc fraction and E6 subfraction to 30% and 47%, each. Taken together, our data suggest that potential anti-aging effect of ASE on skin is via increasing collagen biosynthesis and effective subtraction is E6 subfraction of EtOAc fraction.

• The Journal of the Korean dental association
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• v.15 no.9
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• pp.650-655
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• 1977

• The Journal of the Korean dental association
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• v.19 no.7 s.146
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• pp.609-614
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• 1981

Effects of steroid hormones on the collagen biosynthesis in aorta and uterus were studied with ovariectomized Sprague-Dawley rats. Effects of administration of hormones, such as estrogen, testosterone and prednisolone, to the ovariectomized animals were studied, comparing with the control. Each group was injected with ³H-proline and sacrificed, followed by removals of aorta and uterus. Separations and quantitative analyses of proline and hydroxyproline were performed by means of thin layer chromatography; and radioactivities of the separated amino acids were assayed by liquid scintillation counter. Normally the incorporation of ³H-proline into hydroxyproline was greater in uterus than in aorta, and collagen turnover rate of uterus was observed rapid as well than that of aorta. In the two tissues from ovariectomized rats, the incorporation rate of ³H-proline into hydroxypoline was markedly decreased than that of the former. Changes in the turnover rate of collagen in these tissues were not observed. Decrease in ³H-proline incorporation into collagen in ovariectomized rats was markedly antagonized by estrogen, but not influenced by prednisolone in the tissues tested.

• BMB Reports
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• v.42 no.11
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• pp.743-746
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• 2009

L-ascorbic acid (Vitamin C) and peptide are both useful compounds for collagen biosynthesis in cosmeceuticals (cosmetic and pharmaceutical fields). The instability of these compounds, however, limit their application in these industries. In this report, we describe the development of a novel compound, Stabilized Ascorbyl Pentapeptide (SAP), which physically is much more stable than L-ascorbic acid in water. The inhibitory effects of this SAP compound on tyrosinase and melanin synthesis is comparable to that of L-ascorbic acid. Importantly, the SAP compound displays no cytotoxicity at a high concentration (5 mM). The ability of SAP to promote collagen biosynthesis is greater than that of L-ascorbic acid or the KTTKS peptide alone. Considering the in vitro stability and functional effects, our data strongly suggest that the SAP compound is a good candidate not only as a cosmetic ingredient, but also as a wound healing agent.

• The Journal of the Korean dental association
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• v.19 no.6 s.145
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• pp.529-533
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• 1981

The effect of insulin on the collagen metabolism in dental pulp and gingiva was studied using Sprague-Dawley rat and ³H-proline was injected intraperitoneally and then sacrificed according to predetermined schedule. Lower incisor pulp and gingiva were removed immediatedly and hydrolysed with acid. After digestion, proline and hydroxyproline were separated and analysed quantitatively employing thin-layer chromatography and radioactivity of each amino acid was counted by liquid scintillation counter. The label incorporated into lower incisor pulp and gingiva and radioactivity of ³H-hydroxyproline were increased in insulin administered group. And disappearance rate of ³H-hydroxyproline was decreased. Those results indicated that amino acid, I.e. proline transport and collagen biosynthesis were increased in dental pulp and gingiva by insulin administration.

• The Journal of the Korean dental association
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• v.19 no.7 s.146
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• pp.635-639
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• 1981

• Korean Journal of Pharmacognosy
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• v.38 no.4
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• pp.349-353
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• 2007

Skin wrinkle formations are associated with collagen synthesis and matrix metalloproteinase-I(MMP-1) activity. This study was carried out to find out skin wrinkle reducing components in Torilis Fructus. Torilis Fructus were extracted with 70% ethanol and the ethanol extracts were systematically fractionated with n-hexane, ethylacetate, n-butanol and distilled water. Among them, antiwrinkle component from n-hexane fraction was purified by several column chromatographies and HPLC, which identified as torilin by $^1H-NMR,\;^{13}C-NMR$ and ESI-MS. To determine cell viability, collagen biosynthesis and MMP-1 activity, human dermal fibroblast was treated with 1-5 ppm concentrations of Torilis Fructus extract fraction and torilin. Cell viability was showed 84-102% at all group treated with 1-5 ppm. Collagen synthesis was increased in all group, especially torilin-treated group was highest amount. Active forms of MMP-1 were decreased in all group. From these results, we consider that Torilis Fructus have several antiwrinkle components and torilin may be one of the effective components.

• Journal of the Korean Society of Food Science and Nutrition
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• v.27 no.2
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• pp.305-312
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• 1998

Normal tensile strength in collagen fibrils is due to intermolecular and intramolecular crosslinks which are known to be altered in aging. Pyridinoline, a mature crosslink which is stable and nonreducible, is derived from two hydroxyallysine and one hydroxylysine residues of collagen fibrils. The excess formation of pyridinoline in collagen is associated with making the tissue stiffer, less soluble and less digestible by enzymes. Lysyl oxidase is the enzyme that initiates the biosynthesis or crosslinks in collagen by catalyzing the oxidative deamination of the lysyl and hydroxylysyl residues in these molecules, and its activity is inhibited by $\beta$-aminopropionitrile(BAPN). Our previous work demonstrated that the pyridinoline content of bone collagen significantly was increased during incubation for 5 weeks at 37$^{\circ}C$ invitro, but it was diecrased by the addition of ascorbic acdi(AsA). In this study, we clarified the specific action of AsA in aging process in vitro enzymatic reaction.

• Journal of Life Science
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• v.31 no.12
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• pp.1142-1148
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• 2021

As the average human lifespan has been extended, there has been a lot of interest in the quality of life of women after menopause. It is known that the average age of menopause among Korean women is 49.7 years, and the post-menopausal life of a woman takes up more than one third of her life. L-ascorbic acid (AsA) is known to be involved in the synthesis and maturation of collagen, a bone constituent protein. The aim of this review is to discuss the potential of AsA in bone health in postmenopausal women. AsA plays an important role in collagen biosynthesis, and collagen is a protein constituting bone and is a necessary material for calcification of the bone matrix. Collagen crosslinking is necessary for the stabilization and elasticity of collagen fibers during growth and matruation of animals, but an excessive increase is likely to lead to further aging because the movement of intercellular nutrients or waste is suppressed. AsA acts as a reducing agent to stabilize the immature collagen crosslinking and suppress pyridinoline production, a mature crosslinking. Therefore, AsA participates in collagen biosynthesis and helps bone tissue health, while regulating the excessive maturation of collagen crosslinking, it is expected to play an important role in bone-related problems that may occur in postmenopausal women.

• BMB Reports
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• v.54 no.6
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• pp.329-334
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• 2021

Collagen type I is the most abundant form of collagen in human tissues, and is composed of two identical α-1 type I chains and an α-2 type I chain organized in a triple helical structure. A previous study has shown that human collagen α-2 type I (hCOL1A2) promotes collagen synthesis, wound healing, and elastin production in normal human dermal fibroblasts (HDFs). However, the biological effects of human collagen α-1 type I (hCOL1A1) on various skin properties have not been investigated. Here, we isolate and identify the hCOL1A1-collagen effective domain (CED) which promotes collagen type I synthesis. Recombinant hCOL1A1-CED effectively induces cell proliferation and collagen biosynthesis in HDFs, as well as increased cell migration and elastin production. Based on these results, hCOL1A1-CED may be explored further for its potential use as a preventative agent against skin aging.