The role of type I collagen in aortic wall strength with a homotrimeric [α1(I)]3 collagen mouse model

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

Biochemistry ◽

10.1021/acs.biochem.8b00984 ◽

2019 ◽

Vol 58 (50) ◽

pp. 5040-5051 ◽

Cited By ~ 4

Author(s):

Masahiko Terajima ◽

Yuki Taga ◽

Marnisa Sricholpech ◽

Yukako Kayashima ◽

Noriko Sumida ◽

...

Keyword(s):

Type I Collagen ◽

Type I ◽

Molecular Phenotypes

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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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