Structure, Physiology, and Biochemistry of Collagens

Mienaltowski, Michael J.; Birk, David E.

doi:10.1007/978-94-007-7893-1_2

Cited by 185 publications

(178 citation statements)

References 127 publications

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“…48 Vertebrates have 28 different types of collagens that provide tissue-specific structure and function by assembling into a variety of supramolecular structures of the extracellular matrix. 49 Thus, the downregulation of several collagens, as shown in this study, indicates the dysfunction of extracellular matrices during tumor invasion and metastasis. COL5A2 is downregulated in cervical SCC and adenocarcinoma.…”

Section: Discussionsupporting

confidence: 59%

Proteomic identification of potential biomarkers for cervical squamous cell carcinoma and human papillomavirus infection

Song

Tulake

et al. 2017

Tumour Biol.

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It is known that high-risk human papillomavirus infection is the main etiological factor in cervical carcinogenesis. However, human papillomavirus screening is not sufficient for early diagnosis. In this study, we aimed to identify potential biomarkers common to cervical carcinoma and human papillomavirus infection by proteomics for human papillomavirus-based early diagnosis and prognosis. To this end, we collected 76 cases of fresh cervical tissues and 116 cases of paraffin-embedded tissue slices, diagnosed as cervical squamous cell carcinoma, cervical intraepithelial neoplasia II-III, or normal cervix from ethnic Uighur and Han women. Human papillomavirus infection by eight oncogenic human papillomavirus types was detected in tissue DNA samples using a quantitative polymerase chain reaction. The protein profile of cervical specimens from human papillomavirus 16-positive squamous cell carcinoma and human papillomavirus-negative normal controls was analyzed by proteomics and bioinformatics. The expression of candidate proteins was further determined by quantitative reverse transcriptase-polymerase chain reaction and immunohistochemistry. We identified 67 proteins that were differentially expressed in human papillomavirus 16-positive squamous cell carcinoma compared to normal cervix. The quantitative reverse transcriptase-polymerase chain reaction analysis verified the upregulation of ASAH1, PCBP2, DDX5, MCM5, TAGLN2, hnRNPA1, ENO1, TYPH, CYC, and MCM4 in squamous cell carcinoma compared to normal cervix (p < 0.05). In addition, the transcription of PCBP2, MCM5, hnRNPA1, TYPH, and CYC was also significantly increased in cervical intraepithelial neoplasia II-III compared to normal cervix. Immunohistochemistry staining further confirmed the overexpression of PCBP2, hnRNPA1, ASAH1, and DDX5 in squamous cell carcinoma and cervical intraepithelial neoplasia II-III compared to normal controls (p < 0.05). Our data suggest that the expression of ASAH1, PCBP2, DDX5, and hnRNPA1, and possibly MCM4, MCM5, CYC, ENO1, and TYPH, is upregulated during cervical carcinogenesis and potentially associated with human papillomavirus infection. Further validation studies of the profile will contribute to establishing auxiliary diagnostic markers for human papillomavirus-based cancer prognosis. KeywordsCervical carcinoma, isobaric tags for relative and absolute quantitation, proteomics, human papillomavirus infection, cervical specimen Date

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Section: Discussionsupporting

confidence: 59%

Proteomic identification of potential biomarkers for cervical squamous cell carcinoma and human papillomavirus infection

Song

Tulake

et al. 2017

Tumour Biol.

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“…Some of these collagen-binding molecules include fibronectin, elastin, laminin, hyaluronan, chondroitin sulfate, heparan sulfate proteoglycans, fibrilassociated collagens with interrupted triple helices (FACITS), and small leucine-rich proteoglycans (Fig. 3) (Gelse et al 2003;Hulmes 2008;Mienaltowski and Birk 2014). The biological significance of these collagen-binding ECM molecules is that their shielding of intact collagen molecules from the proteolytic activity of interstitial collagenases may retard physiological remodeling of the matrix and may thus contribute to fibrosis.…”

Section: Contribution Of Collagen Synthesis To Fibrosismentioning

confidence: 97%

“…The mature collagen mRNA is transported to the cytosol and, upon entry into the endoplasmic reticulum, the Nterminal signal peptides of collagen mRNAs are removed. The nascent procollagen molecules undergo several posttranslational modifications including hydroxylation of proline and lysine residues, glycosylation of lysine residues, and disulfide bond formation that ultimately leads to the formation of a triple helix consisting of three pro-peptides (Gelse et al 2003;Hulmes 2008;Mienaltowski and Birk 2014). Disulfide bond formation stabilizes and aligns the globular structures of the C-terminal pro-peptides and enables the formation of triple helical collagen molecules.…”

Section: Contribution Of Collagen Synthesis To Fibrosismentioning

confidence: 99%

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Contribution of collagen adhesion receptors to tissue fibrosis

Coelho

McCulloch

2016

Cell Tissue Res

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Fibrosis is the result of a wound-healing response that fails to restore normal tissue structure function. One of the critical hallmarks of fibrosis is disrupted collagen remodeling. In tissue homeostasis, the production, deposition and organization of collagen is balanced by the degradation and remodeling of collagen within the existing matrix. After injury or chronic infection, tissues initiate a wound-healing response that is intended to create a new ECM for restoring tissue structure and function. If the wound-healing response is dysregulated or if the tissue injury or infection is severe or long-lasting, collagen deposition exceeds collagen degradation and the tissue repair process leads to fibrosis. The fibrotic repair response is extraordinarily complex and involves a wide spectrum of cells, signaling pathways and regulatory systems, some of which can be readily disrupted and thereby contribute to fibrotic lesions. The dysregulated collagen remodeling is a common end-point of all fibrotic disorders, and one of the rate-limiting steps of collagen remodeling is the binding of cells to collagen fibrils by specific cell adhesion receptors. In this review, we describe how the expression and function of collagen adhesion receptors contribute to collagen processing events that contribute to tissue fibrosis. Graphical abstract Balance between collagen remodeling in health and disease.

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“…Therefore, genetic defects of collagen formation affect almost every organ system and tissue throughout the body [7]. Among the genomes of vertebrates and higher invertebrates, 28 distinct collagen glycoproteins are encoded by at least 45 genes [8]. The primary structure of a collagen protein consists of GlyXaa-Yaa repeats and forms a left-handed polyproline II-like helix.…”

Section: Introductionmentioning

confidence: 99%

Glt25d2 Knockout Directly Increases CD25+CD69– but Decreases CD25–CD69+ Subset Proliferation and is Involved in Concanavalin-Induced Hepatitis

Hao

Liu

Zhang

et al. 2018

Cell Physiol Biochem

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Background/Aims: The elaborate structure of the extracellular matrix (ECM) and the appropriate surface glycoforms upon it are indispensable to CD4⁺ T cell regulation. Methods: To explore the effects of Glcα1,2Galβ1 glycosylation mediated by GLT25D2 (Colgalt2) for CD4⁺ T cell regulation, we prepared C57BL/6J Glt25d2^-/- mice. In the induction of hepatitis, after concanavalin A (Con A) challenge for 6, 12, and 24 h, more extensive parenchymal injury was noted in Glt25d2^-/- mice than in wild-type (WT) mice at 12 h. Immunohistochemistry and laser scanning confocal microscopy were used to detect GLT25D2 expression, and subsets of CD4⁺T cells was analyzed by flow cytometry. A total of 26 cytokines in serum samples were determined using Luminex technology. Results: The trend in liver injury score variation was consistent with serum alanine aminotransferase and aspartate aminotransferase levels. The levels of interleukin 4 (IL-4), IL-1β, IL-9, and several chemokines such as macrophage inflammatory protein-2, eotaxin, and growth-related oncogene α were significantly increased in Glt25d2^-/- mice compared with WT mice after Con A challenge. A further phenotype analysis of primary Glt25d2^-/- CD4⁺ T cells showed that Glt25d2 knockout increased the frequency of the CD25⁺CD69^- subset but decreased the frequency of the CD25^-CD69⁺ subset after Con A challenge for 6, 12, and 24 h compared with those of WT CD4⁺ T cells. Activation-induced apoptosis was also significantly increased in Glt25d2^-/- CD4⁺ T cells after Con A challenge compared with WT CD4⁺ T cells. Lectin microarray hybridization showed that Glt25d2 knockout increased the binding activity of Narcissus pseudonarcissus lectin to CD4⁺ T cells but Amaranthus caudatus lectin–binding activity was lost during Con A challenge. Conclusion: The present results suggest that collagen glycosylation mediated by GLT25D2 may regulate a subset of CD4⁺ T cells and be involved in the pathogenesis of Con A–induced hepatitis.

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Structure, Physiology, and Biochemistry of Collagens

Cited by 185 publications

References 127 publications

Proteomic identification of potential biomarkers for cervical squamous cell carcinoma and human papillomavirus infection

Proteomic identification of potential biomarkers for cervical squamous cell carcinoma and human papillomavirus infection

Contribution of collagen adhesion receptors to tissue fibrosis

Glt25d2 Knockout Directly Increases CD25+CD69– but Decreases CD25–CD69+ Subset Proliferation and is Involved in Concanavalin-Induced Hepatitis

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