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Article

Atelocollagen Increases Collagen Synthesis by Promoting Glycine Transporter 1 in Aged Mouse Skin

1
Department of Anatomy and Cell Biology, College of Medicine, Gachon University, Incheon 21936, Republic of Korea
2
LIBON Inc., Incheon 22006, Republic of Korea
3
GangnamON Clinic, Seoul 06129, Republic of Korea
4
Functional Cellular Networks Laboratory, Lee Gil Ya Cancer and Diabetes Institute, Gachon University, Incheon 21999, Republic of Korea
5
Maylin Clinic, Goyang 10391, Republic of Korea
6
Misogain Dermatology Clinic, Gimpo 10108, Republic of Korea
7
Inee Clinic, Seoul 06030, Republic of Korea
8
Department of Thoracic and Cardiovascular Surgery, Gil Medical Center, Gachon University, Incheon 21565, Republic of Korea
9
Department of Health Sciences and Technology, Gachon Advanced Institute for Health Sciences and Technology, Gachon University, Incheon 21999, Republic of Korea
*
Authors to whom correspondence should be addressed.
These authors contributed equally to this work.
Int. J. Mol. Sci. 2025, 26(24), 11825; https://doi.org/10.3390/ijms262411825 (registering DOI)
Submission received: 21 October 2025 / Revised: 3 December 2025 / Accepted: 3 December 2025 / Published: 7 December 2025
(This article belongs to the Section Biochemistry)

Abstract

Aging results in decreased collagen synthesis and the disruption of extracellular matrix integrity, primarily due to increased oxidative stress. This study evaluated whether atelocollagen can restore collagen synthesis in aged skin by modulating glycine transporter 1 (GlyT1)-mediated glycine uptake, regulating oxidative stress, and influencing extracellular matrix remodeling factors in senescent human cells and the skin of older mice. Human dermal fibroblasts (HDFs) and aged mouse skin were treated with atelocollagen, with analyses of GlyT1 expression, glutathione and intracellular glycine concentrations, oxidative stress markers, nuclear factor-kappa-B (NF-κB) activity, matrix metalloproteinases (MMPs), SMAD proteins (SMADs) signaling, and collagen I/III. Treatment with GlyT1 inhibitors and glycine was tested. Atelocollagen significantly increased GlyT1 expression and intracellular glycine concentration, promoted glutathione synthesis, and reduced oxidative stress. These effects led to decreased NF-κB activity and MMP1/3/9 expression, increased SMAD2/3 phosphorylation, and upregulated type I/III collagen synthesis in senescent HDFs and aged mouse skin. All beneficial effects were blocked by GlyT1 inhibition and were generally superior to glycine alone. Histology showed increased collagen density and improved skin elasticity in atelocollagen-treated mice. In summary, atelocollagen enhances collagen synthesis and reduces oxidative stress in aged skin through GlyT1-dependent glycine transport, providing a potential strategy for skin rejuvenation.
Keywords: atelocollagen; collagen; glycine transporter 1 atelocollagen; collagen; glycine transporter 1

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MDPI and ACS Style

Byun, K.-A.; Oh, S.M.; Oh, S.; Kim, H.M.; Oh, M.; Kim, G.; Kim, M.S.; Son, K.H.; Byun, K. Atelocollagen Increases Collagen Synthesis by Promoting Glycine Transporter 1 in Aged Mouse Skin. Int. J. Mol. Sci. 2025, 26, 11825. https://doi.org/10.3390/ijms262411825

AMA Style

Byun K-A, Oh SM, Oh S, Kim HM, Oh M, Kim G, Kim MS, Son KH, Byun K. Atelocollagen Increases Collagen Synthesis by Promoting Glycine Transporter 1 in Aged Mouse Skin. International Journal of Molecular Sciences. 2025; 26(24):11825. https://doi.org/10.3390/ijms262411825

Chicago/Turabian Style

Byun, Kyung-A, Seung Min Oh, Seyeon Oh, Hyoung Moon Kim, Myungjune Oh, Geebum Kim, Min Seung Kim, Kuk Hui Son, and Kyunghee Byun. 2025. "Atelocollagen Increases Collagen Synthesis by Promoting Glycine Transporter 1 in Aged Mouse Skin" International Journal of Molecular Sciences 26, no. 24: 11825. https://doi.org/10.3390/ijms262411825

APA Style

Byun, K.-A., Oh, S. M., Oh, S., Kim, H. M., Oh, M., Kim, G., Kim, M. S., Son, K. H., & Byun, K. (2025). Atelocollagen Increases Collagen Synthesis by Promoting Glycine Transporter 1 in Aged Mouse Skin. International Journal of Molecular Sciences, 26(24), 11825. https://doi.org/10.3390/ijms262411825

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