ArticleBMB reports2021
Effects of human collagen α-1 type I-derived proteins on collagen synthesis and elastin production in human dermal fibroblasts.
Article in BMB reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
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Who cites it
16 citing papers in PubMed, 34 citations in OpenAlex.
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- Elastogenesis in Focus: Navigating Elastic Fibers Synthesis for Advanced Dermal Biomaterial Formulation.Advanced healthcare materials · 2024Review
- Development of a highly effective recombinant protein from human collagen type III Alpha 1 (COL3A1) to enhance human skin cell functionality.BMB reports · 2024Article
- Human Dermal Decellularized ECM Hydrogels as Scaffolds for 3D In Vitro Skin Aging Models.International journal of molecular sciences · 2024Article
- Dialdehyde Starch as a Cross-Linking Agent Modifying Fish Collagen Film Properties.Materials (Basel, Switzerland) · 2024Article
- Anti-skin aging effect of sea buckthorn proanthocyanidins in D-galactose-induced aging mice.Food science & nutrition · 2024Article
- Aquaporin-8 promotes human dermal fibroblasts to counteract hydrogen peroxide-induced oxidative damage: A novel target for management of skin aging.Open life sciences · 2024Article
- Fibroblasts are not just fibroblasts: clear differences between dermal and pulmonary fibroblasts' response to fibrotic growth factors.Scientific reports · 2023Article
- A Novel Hyaluronic Acid Matrix Ingredient with Regenerative, Anti-Aging and Antioxidant Capacity.International journal of molecular sciences · 2023Article
- The Fabrication of Gelatin-Elastin-Nanocellulose Composite Bioscaffold as a Potential Acellular Skin Substitute.Polymers · 2023Article
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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. [BMB Reports 2021; 54(6): 329-334].
Indexed as
Identifiers
34078526PMC8249875W3165285113What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.