Role of Glycosyltransferase 25 Domain 1 in Type I Collagen Glycosylation and Molecular Phenotypes

Desmoplastic tumors correspond to a unique tissue structure characterized by the abnormal deposition of extracellular matrix. Breast tumors are a typical example of this type of lesion, a property that allows its palpation and early detection. Fibrillar type I collagen is a major component of tumor desmoplasia and its accumulation is causally linked to tumor cell survival and metastasis. For many years, the desmoplastic phenomenon was considered to be a reaction and response of the host tissue against tumor cells and, accordingly, designated as “desmoplastic reaction”. This notion has been challenged in the last decades when desmoplastic tissue was detected in breast tissue in the absence of tumor. This finding suggests that desmoplasia is a preexisting condition that stimulates the development of a malignant phenotype. With this perspective, in the present review, we analyze the role of extracellular matrix remodeling in the development of the desmoplastic response. Importantly, during the discussion, we also analyze the impact of obesity and cell metabolism as critical drivers of tissue remodeling during the development of desmoplasia. New knowledge derived from the dynamic remodeling of the extracellular matrix may lead to novel targets of interest for early diagnosis or therapy in the context of breast tumors.

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Type I collagen from sea cucumber (Stichopus japonicus) and the role of matrix metalloproteinase-2 in autolysis

Food Bioscience ◽

10.1016/j.fbio.2021.100959 ◽

2021 ◽

Vol 41 ◽

pp. 100959

Author(s):

Long-Jie Yan ◽

Le-Chang Sun ◽

Kai-Yuan Cao ◽

Yu-Lei Chen ◽

Ling-Jing Zhang ◽

...

Keyword(s):

Matrix Metalloproteinase ◽

Sea Cucumber ◽

Type I Collagen ◽

Matrix Metalloproteinase 2 ◽

Type I ◽

Stichopus Japonicus

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Role of the amino-terminal extrahelical region of type I collagen in directing the 4D overlap in fibrillogenesis

Biopolymers ◽

10.1002/bip.1979.360181208 ◽

1979 ◽

Vol 18 (12) ◽

pp. 3005-3014 ◽

Cited By ~ 93

Author(s):

Donald L. Helseth ◽

Joseph H. Lechner ◽

Arthur Veis

Keyword(s):

Type I Collagen ◽

Type I ◽

Amino Terminal

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Carotid intima-media thickness and bone turnover: the role of C-terminal telopeptide of type I collagen

Internal and Emergency Medicine ◽

10.1007/s11739-010-0356-y ◽

2010 ◽

Vol 5 (2) ◽

pp. 127-134 ◽

Cited By ~ 7

Author(s):

Christian Leli ◽

Leonella Pasqualini ◽

Gaetano Vaudo ◽

Stefano Gaggioli ◽

Anna Maria Scarponi ◽

...

Keyword(s):

Bone Turnover ◽

Type I Collagen ◽

Intima Media Thickness ◽

Carotid Intima Media Thickness ◽

Type I ◽

Media Thickness

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Tissue inhibitor of metalloproteinases (TIMP) regulates extracellular type I collagen degradation by chondrocytes and endothelial cells

Journal of Cell Science ◽

10.1242/jcs.87.2.357 ◽

1987 ◽

Vol 87 (2) ◽

pp. 357-362

Author(s):

J. Gavrilovic ◽

R.M. Hembry ◽

J.J. Reynolds ◽

G. Murphy

Keyword(s):

Endothelial Cells ◽

Type I Collagen ◽

Model System ◽

Collagen Degradation ◽

Type I ◽

Tissue Inhibitor Of Metalloproteinases ◽

Regulatory Factor ◽

Tissue Inhibitor ◽

Cells Cultured

A specific antiserum to purified rabbit tissue inhibitor of metalloproteinases (TIMP) was raised in sheep, characterized and used to investigate the role of TIMP in a model system. Chondrocytes and endothelial cells cultured on 14C-labelled type I collagen films and stimulated to produce collagenase were unable to degrade the films unless the anti-TIMP antibody was added. The degradation induced was inhibited by a specific anti-rabbit collagenase antibody. It was concluded that TIMP is a major regulatory factor in cell-mediated collagen degradation.

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Fibrillar type I collagens enhance platelet-dependent thrombin generation via glycoprotein VI with direct support of α2β1 but not αIIbβ3 integrin

Thrombosis and Haemostasis ◽

10.1160/th04-12-0783 ◽

2005 ◽

Vol 94 (07) ◽

pp. 107-114 ◽

Cited By ~ 21

Author(s):

Christelle Lecut ◽

Martine Jandrot-Perrus ◽

Marion A. H. Feijge ◽

Judith M. E. M. Cosemans ◽

Johan W. M. Heemskerk

Keyword(s):

Thrombin Generation ◽

Type I Collagen ◽

Platelet Rich Plasma ◽

Procoagulant Activity ◽

Type I ◽

Platelet Surface ◽

Glycoprotein Vi ◽

Collagen Receptors ◽

Fibrillar Collagens

SummaryThe role of collagens and collagen receptors was investigated in stimulating platelet-dependent thrombin generation. Fibrillar type-I collagens, including collagen from human heart, were most potent in enhancing thrombin generation, in a way dependent on exposure of phosphatidylserine (PS) at the platelet surface. Soluble, non-fibrillar type-I collagen required pre-activation of integrin α2β1 with Mn2+ for enhancement of thrombin generation. With all preparations, blocking of glycoprotein VI (GPVI) with 9O12 antibody abrogated the collagen-enhanced thrombin generation, regardless of the α2β1 activation state. Blockade of α2β1 alone or antagonism of autocrine thromboxane A2 and ADP were less effective. Blockade of αIIbβ3 with abciximab suppressed thrombin generation in platelet-rich plasma, but this did not abolish the enhancing effect of collagens. The high activity of type-I fibrillar collagens in stimulating GPVI-dependent procoagulant activity was confirmed in whole-blood flow studies, showing that these collagens induced relatively high expression of PS. Together, these results indicate that: i) fibrillar type-I collagen greatly enhances thrombin generation, ii) GPVI-induced platelet activation is principally responsible for the procoagulant activity of fibrillar and non-fibrillar collagens, iii) α2β1 and signaling via autocrine mediators facilitate and amplify this GPVI activity, and iv) αIIbβ3 is not directly involved in the collagen effect.

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Role of Erythromycin-Regulated Histone Deacetylase-2 in Benign Tracheal Stenosis

Canadian Respiratory Journal ◽

10.1155/2020/4213807 ◽

2020 ◽

Vol 2020 ◽

pp. 1-10

Author(s):

Zhenjie Huang ◽

Peng Wei ◽

Luoman Gan ◽

Tonghua Zeng ◽

Caicheng Qin ◽

...

Keyword(s):

Histone Deacetylase ◽

Tracheal Stenosis ◽

Type I Collagen ◽

Rabbit Model ◽

Immunohistochemical Method ◽

Type Iii Collagen ◽

Type I ◽

Histone Deacetylase 2 ◽

Budesonide Group

Objective. This study aims to explore the role of erythromycin-regulated histone deacetylase-2 in benign tracheal stenosis. Methods. The rabbit model of tracheal stenosis was established. The rabbits were randomly divided into 8 groups. Histone deacetylase-2 (HDAC2) expression was detected by immunofluorescence. The expression of type I collagen and type III collagen was detected by immunohistochemical method. The expression of TGF-β1, VEGF and IL-8 in serum and alveolar lavage fluid was detected by ELISA. The expression of HDAC2, TGF-β1, VEGF and IL-8 in bronchi of each group was detected by Western blotting method. Results. In Erythromycin (ERY) group, ERY + Budesonide group, ERY + Vorinostat group and ERY + Budesonide + Vorinostat group, the degree of bronchial stenosis was alleviated, and the mucosal epithelium was still slightly proliferated. The effect of ERY combined with other drugs was more obvious. The HDAC2 protein expression increased significantly in ERY group, ERY + Budesonide group and ERY + Budesonide + Vorinostat group and decreased significantly in Vorinostat group, the expression of collagen I and III decreased significantly in ERY group, ERY + Budesonide group and ERY + Budesonide + Vorinostat group (P<0.05). The TGF-β1, IL-8 and VEGF levels decreased significantly in ERY group, ERY + Budesonide group, ERY + Vorinostat group and ERY + Budesonide + Vorinostat group (P<0.05). Conclusions. Erythromycin inhibited inflammation and excessive proliferation of granulation tissue after tracheobronchial mucosal injury by up-regulating the expression of HDAC2, it promoted wound healing and alleviated tracheobronchial stenosis. When combined with budesonide, penicillin and other glucocorticoids and antibiotics, it had a good synergistic effect. However, vorinostat could attenuate erythromycin’s effect by down-regulating the expression of HDAC2. It may have good clinical application prospects in the treatment of tracheal stenosis.

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Role of Osteoglycin in the Linkage between Muscle and Bone

Journal of Biological Chemistry ◽

10.1074/jbc.m111.292193 ◽

2012 ◽

Vol 287 (15) ◽

pp. 11616-11628 ◽

Cited By ~ 72

Author(s):

Ken-ichiro Tanaka ◽

Erika Matsumoto ◽

Yoshiko Higashimaki ◽

Takenobu Katagiri ◽

Toshitsugu Sugimoto ◽

...

Keyword(s):

Transcriptional Activity ◽

Type I Collagen ◽

C2c12 Cells ◽

Type I ◽

Mrna Levels ◽

Humoral Factors ◽

Anabolic Activity ◽

Morphogenetic Protein ◽

Muscle Tissues

The interaction between muscle tissues and bone metabolism is incompletely understood. We hypothesized that there might be some humoral factors that are produced in muscle tissues and exhibit bone anabolic activity. We, therefore, performed comparative DNA microarray analysis between mouse myoblastic C2C12 cells transfected with either stable empty vector or ALK2 (R206H), the mutation that constitutively activates the bone morphogenetic protein (BMP) receptor, to search for muscle-derived bone anabolic factors. Twenty-five genes whose expression was decreased to <1/4, were identified; these included osteoglycin (OGN). Stable overexpression of OGN significantly decreased the levels of Runx2 and Osterix mRNA compared with those in cells transfected with vector alone in MC3T3-E1 cells. On the other hand, it significantly enhanced the levels of alkaline phosphatase (ALP), type I collagen (Col1), and osteocalcin (OCN) mRNA as well as β-catenin and mineralization. A reduction in endogenous OGN level showed the opposite effects to those of OGN overexpression in MC3T3-E1 and mouse calvarial osteoblastic cells. Transient OGN overexpression significantly suppressed the levels of Runx2, Osterix, ALP, Col1, and OCN mRNA induced by BMP-2 in C2C12 cells. The conditioned medium from OGN-overexpressed and OGN-suppressed myoblastic cells enhanced and decreased, respectively, the levels of ALP, Col1, and β-catenin in MC3T3-E1 cells. Moreover, OGN increased Smad3/4-responsive transcriptional activity as well as Col1 mRNA levels independently of endogenous TGF-β in these cells. In conclusion, this study suggests that OGN may be a crucial humoral bone anabolic factor that is produced by muscle tissues.

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Binding of Brucella protein, Bp26, to select extracellular matrix molecules

BMC Molecular and Cell Biology ◽

10.1186/s12860-019-0239-7 ◽

2019 ◽

Vol 20 (1) ◽

Cited By ~ 4

Author(s):

Yasmin ElTahir ◽

Amna Al-Araimi ◽

Remya R. Nair ◽

Kaija J. Autio ◽

Hongmin Tu ◽

...

Keyword(s):

Extracellular Matrix ◽

Type I Collagen ◽

Host Cells ◽

Mouse Serum ◽

Enzyme Linked Immunosorbent Assay ◽

Target Cells ◽

Type I ◽

Dependent Manner ◽

Biolayer Interferometry

Abstract Background Brucella is a facultative intracellular pathogen responsible for zoonotic disease brucellosis. Little is known about the molecular basis of Brucella adherence to host cells. In the present study, the possible role of Bp26 protein as an adhesin was explored. The ability of Brucella protein Bp26 to bind to extracellular matrix (ECM) proteins was determined by enzyme-linked immunosorbent assay (ELISA) and biolayer interferometry (BLI). Results ELISA experiments showed that Bp26 bound in a dose-dependent manner to both immobilized type I collagen and vitronectin. Bp26 bound weakly to soluble fibronectin but did not bind to immobilized fibronectin. No binding to laminin was detected. Biolayer interferometry showed high binding affinity of Bp26 to immobilized type I collagen and no binding to fibronectin or laminin. Mapping of Bp26 antigenic epitopes by biotinylated overlapping peptides spanning the entire sequence of Bp26 using anti Bp26 mouse serum led to the identification of five linear epitopes. Collagen and vitronectin bound to peptides from several regions of Bp26, with many of the binding sites for the ligands overlapping. The strongest binding for anti-Bp26 mouse serum, collagen and vitronectin was to the peptides at the C-terminus of Bp26. Fibronectin did not bind to any of the peptides, although it bound to the whole Bp26 protein. Conclusions Our results highlight the possible role of Bp26 protein in the adhesion process of Brucella to host cells through ECM components. This study revealed that Bp26 binds to both immobilized and soluble type I collagen and vitronectin. It also binds to soluble but not immobilized fibronectin. However, Bp26 does not bind to laminin. These are novel findings that offer insight into understanding the interplay between Brucella and host target cells, which may aid in future identification of a new target for diagnosis and/or vaccine development and prevention of brucellosis.

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