Evidence map›Paper›PMID 39219046›Full record

ArticleBMB reports2024

Development of a highly effective recombinant protein from human collagen type III Alpha 1 (COL3A1) to enhance human skin cell functionality.

Young Un Kim, HyunJoon Gi, Eun Kyung Jeong, Seokwon Han, Woo-Young Seo, Young Jun Kim, Sang Bae Lee, KyeongJin Kim

Abstract read
In one paragraph

Article in BMB reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
–field-weighted citation impact
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

7 citing papers in PubMed.

  1. Trial
  2. Article
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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

8 authors.

Young Un KimDepartment of Biomedical Sciences, College of Medicine, Inha University, Incheon 22212, 2Program in Biomedical Science & Engineering, Inha University, Incheon 22212; Research Center for Controlling Intercellular Communication (RCIC), College of Medicine, Inha University, Incheon 22212, Korea.
HyunJoon GiDepartment of Biomedical Sciences, College of Medicine, Inha University, Incheon 22212, 2Program in Biomedical Science & Engineering, Inha University, Incheon 22212; Research Center for Controlling Intercellular Communication (RCIC), College of Medicine, Inha University, Incheon 22212, Korea.
Eun Kyung JeongDepartment of Food Regulatory Science, Korea University, Sejong 30019, Korea.
Seokwon HanABIOTECH Co., Ltd., Suwon 16675, Korea.
Woo-Young SeoABIOTECH Co., Ltd., Suwon 16675, Korea.
Young Jun KimDepartment of Food Regulatory Science, Korea University, Sejong 30019, Korea.
Sang Bae LeeDepartment of Life Sciences, Jeonbuk National University, Jeonju 54896, Korea.
KyeongJin KimDepartment of Biomedical Sciences, College of Medicine, Inha University, Incheon 22212, 2Program in Biomedical Science & Engineering, Inha University, Incheon 22212; Research Center for Controlling Intercellular Communication (RCIC), College of Medicine, Inha University, Incheon 22212, Korea.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Collagen type III, a member of the fibrillar collagen group, is a major component of the extracellular matrix in various internal organs, the vascular systems, and skin. It is essential to maintain the structural integrity and functionality of these tissues, and plays a significant role in wound healing, often found alongside collagen type I. Despite being the second most abundant collagen in human tissues after type I, its biological functions on various skin properties have not been thoroughly studied. In this study, we have isolated and developed an effective recombinant protein derived from human collagen type III alpha 1 chain (hCOL3A1). Our findings demonstrate that the recombinant proteins hCOL3A1-THR-M1 and M4 stimulate cell proliferation and collagen biosynthesis in human dermal fibroblasts (HDFs), and enhance wound healing. Notably, hCOL3A1-THR- M1 (referred to as HUCOLLATIN3) specifically penetrates both the epidermal and dermal layers in a full-thickness skin model. These results collectively indicate that hCOL3A1-THR-M1 holds promise as a potential biomaterial to prevent skin aging. [BMB Reports 2024; 57(9): 424-429].

Indexed as

Cell ProliferationCollagen Type IIIFibroblastsRecombinant ProteinsSkinWound HealingAnimalsHumansMiceCOL3A1 protein, humanCollagen Type IIIRecombinant Proteins

Identifiers

PMID39219046
PMCPMC11444990

What OpenQuestion holds

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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.