Collagen prolyl 4-hydroxylases modify tumor progression

Shi, Run; Gao, Shanshan; Zhang, Jie; Xu, Jianmin; Graham, Linda M.; Yang, Xiaowen; Li, Chaoyang

doi:10.1093/abbs/gmab065

Cited by 32 publications

(27 citation statements)

References 117 publications

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“…In vitro , enhanced expression of COL1A1 promotes the invasion and migration of GC cells, while knocking out COL1A1 inhibits the increase in cell metastasis ability ( Li et al, 2021 ). It plays an important role in promoting tumor cell proliferation, migration, invasion, epithelial–mesenchymal transformation (EMT), and chemotherapy resistance ( Armstrong et al, 2004 ; Koenig et al, 2006 ; Shintani et al, 2008 ; Yang et al, 2014 ; Zheng X. et al, 2017 ; Yamazaki et al, 2018 ; Shi et al, 2021 ). ROC analysis showed high diagnostic value of COL1A1 (AUC = 0.916) based on 414 GC samples and 210 normal gastric tissues.…”

Section: Discussionmentioning

confidence: 99%

Identification of Potential Diagnostic and Prognostic Biomarkers for Gastric Cancer Based on Bioinformatic Analysis

Niu

Ren²,

et al. 2022

Front. Genet.

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Background: Gastric cancer (GC) is one of the most prevalent cancers all over the world. The molecular mechanisms of GC remain unclear and not well understood. GC cases are majorly diagnosed at the late stage, resulting in a poor prognosis. Advances in molecular biology techniques allow us to get a better understanding of precise molecular mechanisms and enable us to identify the key genes in the carcinogenesis and progression of GC.Methods: The present study used datasets from the GEO database to screen differentially expressed genes (DEGs) between GC and normal gastric tissues. GO and KEGG enrichments were utilized to analyze the function of DEGs. The STRING database and Cytoscape software were applied to generate protein–protein network and find hub genes. The expression levels of hub genes were evaluated using data from the TCGA database. Survival analysis was conducted to evaluate the prognostic value of hub genes. The GEPIA database was involved to correlate key gene expressions with the pathological stage. Also, ROC curves were constructed to assess the diagnostic value of key genes.Results: A total of 607 DEGs were identified using three GEO datasets. GO analysis showed that the DEGs were mainly enriched in extracellular structure and matrix organization, collagen fibril organization, extracellular matrix (ECM), and integrin binding. KEGG enrichment was mainly enriched in protein digestion and absorption, ECM-receptor interaction, and focal adhesion. Fifteen genes were identified as hub genes, one of which was excluded for no significant expression between tumor and normal tissues. COL1A1, COL5A2, P4HA3, and SPARC showed high values in prognosis and diagnosis of GC.Conclusion: We suggest COL1A1, COL5A2, P4HA3, and SPARC as biomarkers for the diagnosis and prognosis of GC.

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Section: Discussionmentioning

confidence: 99%

Identification of Potential Diagnostic and Prognostic Biomarkers for Gastric Cancer Based on Bioinformatic Analysis

Niu

Ren²,

et al. 2022

Front. Genet.

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“…Proline and lysine hydroxylation, catalyzed by collagen prolyl 4‐hydroxylases (C‐P4Hs) and lysyl hydroxylases (LHs), are necessary for type I collagen secretion. C‐P4Hs and LHs are highly expressed in a variety of cancers 241,242 . These enzymes promote cancer progression by enhancing type I collagen maturation.…”

Section: The Regulation Of Type I Collagen Expressionmentioning

confidence: 99%

“…These enzymes promote cancer progression by enhancing type I collagen maturation. Suppressing the activity of C‐P4Hs and LHs has been proposed as a strategy to block cancer progression 241,242 . Another molecule required for collagen maturation is the heat shock protein 47 (HSP47), a collagen‐specific chaperone indispensable for collagen synthesis 243 .…”

Section: The Regulation Of Type I Collagen Expressionmentioning

confidence: 99%

Targeting type I collagen for cancer treatment

Shi

Zhang

Zhu

et al. 2022

Intl Journal of Cancer

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Collagen is the most abundant protein in animals. Interactions between tumor cells and collagen influence every step of tumor development. Type I collagen is the main fibrillar collagen in the extracellular matrix and is frequently upregulated during tumorigenesis. The binding of type I collagen to its receptors on tumor cells promotes tumor cell proliferation, epithelial-mesenchymal transition and metastasis. Type I collagen also regulates the efficacy of tumor therapies, such as chemotherapy, radiotherapy and immunotherapy. Furthermore, type I collagen fragments are diagnostic markers of metastatic tumors and have prognostic value. Inhibition of type I collagen synthesis has been reported to have antitumor effects in animal models. However, collagen has also been shown to possess antitumor activity. Therefore, the roles that type I collagen plays in tumor biology are complex and tumor type-dependent. In this review, we discuss the expression and regulation of synthesis of type I collagen, as well as the role upregulated type I collagen plays in various stages of cancer Abbreviations: *OH, hydroxyl radical; 5 0 UTR, 5 0 untranslated region; 5 0 SL, 5 0 stem-loop; ABC, ATP binding cassette; AKT, v-Akt murine thymoma viral oncogene homolog; BLCA, bladder urothelial

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“…The hydroxylation of proline residues on collagen, catalysed by collagen prolyl 4-hydroxylase (C-P4H), is essential for the stability of the collagen triple helix. C-P4H is an α2β2 tetramer consisting of three isoenzymes differing in the catalytic α-subunits, which are encoded by P4HA1 , P4HA2 and P4HA3 genes and a β-subunit, which is encoded by a single gene, P4HB [ 60 ]. The expressions of P4HAs are regulated by multiple cellular factors, including miRNAs [ 60 ].…”

Section: Collagen Formationmentioning

confidence: 99%

“…C-P4H is an α2β2 tetramer consisting of three isoenzymes differing in the catalytic α-subunits, which are encoded by P4HA1 , P4HA2 and P4HA3 genes and a β-subunit, which is encoded by a single gene, P4HB [ 60 ]. The expressions of P4HAs are regulated by multiple cellular factors, including miRNAs [ 60 ]. miR-124-3p inhibits the collagen synthesis of vascular smooth muscle cells (VSMC) by directly targeting P4HA1 [ 32 ].…”

Section: Collagen Formationmentioning

confidence: 99%

The Regulation of Collagen Processing by miRNAs in Disease and Possible Implications for Bone Turnover

Lehmann

Guderska

Kałek

et al. 2021

IJMS

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This article describes several recent examples of miRNA governing the regulation of the gene expression involved in bone matrix construction. We present the impact of miRNA on the subsequent steps in the formation of collagen type I. Collagen type I is a main factor of mechanical bone stiffness because it constitutes 90–95% of the organic components of the bone. Therefore, the precise epigenetic regulation of collagen formation may have a significant influence on bone structure. We also describe miRNA involvement in the expression of genes, the protein products of which participate in collagen maturation in various tissues and cancer cells. We show how non-collagenous proteins in the extracellular matrix are epigenetically regulated by miRNA in bone and other tissues. We also delineate collagen mineralisation in bones by factors that depend on miRNA molecules. This review reveals the tissue variability of miRNA regulation at different levels of collagen maturation and mineralisation. The functionality of collagen mRNA regulation by miRNA, as proven in other tissues, has not yet been shown in osteoblasts. Several collagen-regulating miRNAs are co-expressed with collagen in bone. We suggest that collagen mRNA regulation by miRNA could also be potentially important in bone metabolism.

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Collagen prolyl 4-hydroxylases modify tumor progression

Cited by 32 publications

References 117 publications

Identification of Potential Diagnostic and Prognostic Biomarkers for Gastric Cancer Based on Bioinformatic Analysis

Identification of Potential Diagnostic and Prognostic Biomarkers for Gastric Cancer Based on Bioinformatic Analysis

Targeting type I collagen for cancer treatment

The Regulation of Collagen Processing by miRNAs in Disease and Possible Implications for Bone Turnover

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