Evidence map›Paper›PMID 32843132›Full record

ArticleBMB reports2020

Human collagen alpha-2 type I stimulates collagen synthesis, wound healing, and elastin production in normal human dermal fibroblasts (HDFs).

Su Jin Hwang, Geun-Hyoung Ha, Woo-Young Seo, Chung Kwon Kim, KyeongJin Kim, Sang Bae Lee

Open access · goldAbstract readNews
In one paragraph

Article in BMB reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
1.7field-weighted citation impact, top 17% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

30 citing papers in PubMed, 53 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 1 country.

Su Jin HwangABIOTECH Co., Ltd., Suwon 16675, Korea.
Geun-Hyoung HaABIOTECH Co., Ltd., Suwon 16675, Korea.
Woo-Young SeoABIOTECH Co., Ltd., Suwon 16675, Korea.
Chung Kwon KimDepartment of Anatomy and Cell Biology, Biomedical Institute for Convergence at SKKU (BICS), Sungkyunkwan University School of Medicine, Suwon 16419, Korea.
KyeongJin KimDepartment of Biomedical Sciences, College of Medicine, Inha University, Incheon 22212; Program in Biomedical Science & Engineering, Inha University, Incheon 22212, Korea.
Sang Bae LeeDivision of Life Sciences, Jeonbuk National University, Jeonju 54896, Korea.
Inha University · KRJeonbuk National University · KRSungkyunkwan University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Skin aging appears to be the result of overlapping intrinsic (including genetic and hormonal factors) and extrinsic (external environment including chronic light exposure, chemicals, and toxins) processes. These factors cause decreases in the synthesis of collagen type I and elastin in fibroblasts and increases in the melanin in melanocytes. Collagen Type I is the most abundant type of collagen and is a major structural protein in human body tissues. In previous studies, many products containing collagen derived from land and marine animals as well as other sources have been used for a wide range of purposes in cosmetics and food. However, to our knowledge, the effects of human collagenderived peptides on improvements in skin condition have not been investigated. Here we isolate and identify the domain of a human COL1A2-derived protein which promotes fibroblast cell proliferation and collagen type I synthesis. This human COL 1A2-derived peptide enhances wound healing and elastin production. Finally, the human collagen alpha-2 type I-derived peptide (SMM) ameliorates collagen type I synthesis, cell proliferation, cell migration, and elastin synthesis, supporting a significant anti-wrinkle effect. Collectively, these results demonstrate that human collagen alpha-2 type I-derived peptides is practically accessible in both cosmetics and food, with the goal of improving skin condition. [BMB Reports 2020; 53(10): 539-544].

Indexed as

Cell MovementCell ProliferationCells, CulturedCollagenCollagen Type IElastinFibroblastsHumansSkinSkin AgingWound HealingCOL1A2 protein, humanCollagenCollagen Type IElastin

Identifiers

PMID32843132
PMCPMC7607150
OpenAlexW3081500767

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

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.