IGF-1 Upregulates Biglycan and Decorin by Increasing Translation and Reducing ADAMTS5 Expression

Lee, Hanon; Lim, Jiyeong; Oh, Joo Youn; Cho, Soyun; Chung, Jin Ho

doi:10.3390/ijms22031403

Cited by 7 publications

(4 citation statements)

References 64 publications

(82 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Total RNA was isolated from cultured HaCaT cells using RNAiso Plus (Takara Bio Inc., Shiga, Japan) at 18 h after TNF-α/IFN-γ-stimulation. Subsequent cDNA synthesis and product confirmation by real-time PCR was performed as detailed in our previous report [ 66 ]. The following primer sequences were used for amplification: TARC forward: 5′-TTGTAACTGTGCAGGGCAGG-3′, reverse: 5′-TGAACACCAACGGTGGAGGT-3′, MDC forward: 5′-GAAGCCTGTGCCAACTCTCT-3′, reverse: 5′-GGGAATCGCTGATGGGAACA-3′, CTSS forward: 5′-TGGGCTTTCAGTGCTGTGGG-3′, reverse: 5′-TCAATGATGTACTGGAAAGC-3′, 18S rRNA forward: 5′-GTAACCCGTTGAACCCCATT-3′, reverse: 5′-CCATCCAATCGGTAGTAGCG-3′, GAPDH forward: 5′-ATTGTTGCCATCAATGACCC-3′, reverse: 5′-AGTAGAGGCAGGGATGATGT-3′, U6 snRNA forward: 5′-CTCGCTTCGGCAGCACA-3′, and reverse: 5′-AACGCTTCACGAATTTGCGT-3′.…”

Section: Methodsmentioning

confidence: 99%

“…To extract the proteins for western blotting, cells were harvested by scraping on ice with 1× SDS-lysis buffer containing high concentrations of SDS (1.75%) and 2-mercaptoethanol (715 mM), along with the Complete Mini protease inhibitor cocktail (Roche Applied Science, Indianapolis, IN, USA) and phosphatase inhibitor cocktails (Sigma-Aldrich, St. Louis, MO, USA). Subsequent processes were performed as detailed in ourprevious report [ 66 ]. Membranes were blocked using 5% BSA in tris-buffered saline with 0.1% Tween ® 20 (TBS-T), instead of 5% skim milk in TBS-T for the phospho-forms of target proteins.…”

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

Skullcapflavone II Suppresses TNF-α/IFN-γ-Induced TARC, MDC, and CTSS Production in HaCaT Cells

Lee

et al. 2021

IJMS

Self Cite

View full text Add to dashboard Cite

Skullcapflavone II (SFII), a flavonoid derived from Scutellaria baicalensis, has been reported to have anti-inflammatory properties. However, its therapeutic potential for skin inflammatory diseases and its mechanism are unknown. Therefore, this study aimed to investigate the effect of SFII on TNF-α/IFN-γ-induced atopic dermatitis (AD)-associated cytokines, such as thymus- and activation-regulated chemokine (TARC) and macrophage-derived chemokine (MDC). Co-stimulation with TNF-α/IFN-γ in HaCaT cells is a well-established model for induction of pro-inflammatory cytokines. We treated cells with SFII prior to TNF-α/IFN-γ-stimulation and confirmed that it significantly inhibited TARC and MDC expression at the mRNA and protein levels. Additionally, SFII also inhibited the expression of cathepsin S (CTSS), which is associated with itching in patients with AD. Using specific inhibitors, we demonstrated that STAT1, NF-κB, and p38 MAPK mediate TNF-α/IFN-γ-induced TARC and MDC, as well as CTSS expression. Finally, we confirmed that SFII significantly suppressed TNF-α/IFN-γ-induced phosphorylation of STAT1, NF-κB, and p38 MAPK. Taken together, our study indicates that SFII inhibits TNF-α/IFN-γ-induced TARC, MDC, and CTSS expression by regulating STAT1, NF-κB, and p38 MAPK signaling pathways.

show abstract

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Skullcapflavone II Suppresses TNF-α/IFN-γ-Induced TARC, MDC, and CTSS Production in HaCaT Cells

Lee

et al. 2021

IJMS

Self Cite

View full text Add to dashboard Cite

show abstract

“…Furthermore, recent studies have revealed that IGF-1 increases biglycan protein translation by preventing ADAMTS5-mediated degradation indicating a new role of IGF-1 regulating biglycan expression [214]. Since biglycan activates fibroblasts, inducing tumor stiffness [215] and facilitating tumor cell invasion, its interactions with IGF-signaling could present a plausible cancer therapy target.…”

Section: Igf Signaling In Tumor Angiogenesismentioning

confidence: 99%

The Role of IGF/IGF-IR-Signaling and Extracellular Matrix Effectors in Bone Sarcoma Pathogenesis

Tzanakakis

Giatagana

Berdiaki

et al. 2021

Cancers

View full text Add to dashboard Cite

Bone sarcomas, mesenchymal origin tumors, represent a substantial group of varying neoplasms of a distinct entity. Bone sarcoma patients show a limited response or do not respond to chemotherapy. Notably, developing efficient chemotherapy approaches, dealing with chemoresistance, and preventing metastasis pose unmet challenges in sarcoma therapy. Insulin-like growth factors 1 and 2 (IGF-1 and -2) and their respective receptors are a multifactorial system that significantly contributes to bone sarcoma pathogenesis. Whereas failures have been registered in creating novel targeted therapeutics aiming at the IGF pathway, new agent development should continue, evaluating combinatorial strategies for enhancing antitumor responses and better classifying the patients that could best benefit from these therapies. A plausible approach for developing a combinatorial strategy is to focus on the tumor microenvironment (TME) and processes executed therein. Herewith, we will discuss how the interplay between IGF-signaling and the TME constituents affects sarcomas’ basal functions and their response to therapy. This review highlights key studies focusing on IGF signaling in bone sarcomas, specifically studies underscoring novel properties that make this system an attractive therapeutic target and identifies new relationships that may be exploited. Potential direct and adjunct therapeutical implications of the extracellular matrix (ECM) effectors will also be summarized.

show abstract

“…Under normal circumstances the expression and activity of proteases in skin and other organs is tightly regulated to prevent excessive tissue destruction which could lead to chronic disease and loss of tissue function [6]. In healthy skin, the mechanisms that mediate protease activity occur at multiple levels, from the control of protease gene transcription [7] through to secretion of proteases as inactive zymogens [8], and the selective activation [9] and suppression of activity by specific inhibitors [10]. However, failure of these mechanisms, through genetic or acquired causes, may contribute to excessive protease activity and the development of skin conditions such as Netherton syndrome [11], rosacea [12], chronic wounds [13] and photoageing [14].…”

Section: Introductionmentioning

confidence: 99%

Defining the Protease and Protease Inhibitor (P/PI) Proteomes of Healthy and Diseased Human Skin by Modified Systematic Review

et al. 2022

View full text Add to dashboard Cite

Proteases and protease inhibitors (P/PIs) are involved in many biological processes in human skin, yet often only specific families or related groups of P/PIs are investigated. Proteomics approaches, such as mass spectrometry, can define proteome signatures (including P/PIs) in tissues; however, they struggle to detect low-abundance proteins. To overcome these issues, we aimed to produce a comprehensive proteome of all P/PIs present in normal and diseased human skin, in vivo, by carrying out a modified systematic review using a list of P/PIs from MEROPS and combining this with key search terms in Web of Science. Resulting articles were manually reviewed against inclusion/exclusion criteria and a dataset constructed. This study identified 111 proteases and 77 protease inhibitors in human skin, comprising the serine, metallo-, cysteine and aspartic acid catalytic families of proteases. P/PIs showing no evidence of catalytic activity or protease inhibition, were designated non-peptidase homologs (NPH), and no reported protease inhibitory activity (NRPIA), respectively. MMP9 and TIMP1 were the most frequently published P/PIs and were reported in normal skin and most skin disease groups. Normal skin and diseased skin showed significant overlap with respect to P/PI profile; however, MMP23 was identified in several skin disease groups, but was absent in normal skin. The catalytic profile of P/PIs in wounds, scars and solar elastosis was distinct from normal skin, suggesting that a different group of P/PIs is responsible for disease progression. In conclusion, this study uses a novel approach to provide a comprehensive inventory of P/PIs in normal and diseased human skin reported in our database. The database may be used to determine either which P/PIs are present in specific diseases or which diseases individual P/PIs may influence.

show abstract

IGF-1 Upregulates Biglycan and Decorin by Increasing Translation and Reducing ADAMTS5 Expression

Cited by 7 publications

References 64 publications

Skullcapflavone II Suppresses TNF-α/IFN-γ-Induced TARC, MDC, and CTSS Production in HaCaT Cells

Skullcapflavone II Suppresses TNF-α/IFN-γ-Induced TARC, MDC, and CTSS Production in HaCaT Cells

The Role of IGF/IGF-IR-Signaling and Extracellular Matrix Effectors in Bone Sarcoma Pathogenesis

Defining the Protease and Protease Inhibitor (P/PI) Proteomes of Healthy and Diseased Human Skin by Modified Systematic Review

Contact Info

Product

Resources

About