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

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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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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Atrial natriuretic peptide, B-type natriuretic peptide, and serum collagen markers after acute myocardial infarction

Journal of Applied Physiology ◽

10.1152/japplphysiol.00557.2003 ◽

2004 ◽

Vol 96 (4) ◽

pp. 1306-1311 ◽

Cited By ~ 24

Author(s):

Jarkko Magga ◽

Mikko Puhakka ◽

Seppo Hietakorpi ◽

Kari Punnonen ◽

Paavo Uusimaa ◽

...

Keyword(s):

Myocardial Infarction ◽

Acute Myocardial Infarction ◽

Atrial Natriuretic Peptide ◽

Natriuretic Peptide ◽

Type I Collagen ◽

Left Ventricular ◽

Type I ◽

Amino Terminal ◽

Collagen Markers ◽

Atrial Natriuretic

Experimental data suggest that atrial natriuretic peptide (ANP) and B-type natriuretic peptide (BNP) act locally as antifibrotic factors in heart. We investigated the interrelationships of natriuretic peptides and collagen markers in 93 patients receiving thrombolytic treatment for their first acute myocardial infarction (AMI). Collagen formation following AMI, evaluated as serum levels of amino terminal propeptide of type III procollagen, correlated with NH2-terminal proANP ( r = 0.45, P < 0.001), BNP ( r = 0.55, P < 0.001) and NH2-terminal proBNP ( r = 0.50, P < 0.01) on day 4 after thrombolysis. Levels of intact amino terminal propeptide of type I procollagen decreased by 34% ( P < 0.001), and levels of carboxy terminal cross-linked telopeptide of type I collagen (ICTP) increased by 65% ( P < 0.001). ICTP levels correlated with NH2-terminal proBNP ( r = 0.25, P < 0.05) and BNP ( r = 0.28, P < 0.05) on day 4. Our results suggest that ANP and BNP may act as regulators of collagen scar formation and left ventricular remodeling after AMI in humans. Furthermore, degradation of type I collagen is increased after AMI and may be regulated by BNP.

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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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Collagen fibrillogenesis in vitro: interaction of types I and V collagen regulates fibril diameter

Journal of Cell Science ◽

10.1242/jcs.95.4.649 ◽

1990 ◽

Vol 95 (4) ◽

pp. 649-657 ◽

Cited By ~ 2

Author(s):

D.E. Birk ◽

J.M. Fitch ◽

J.P. Babiarz ◽

K.J. Doane ◽

T.F. Linsenmayer

Keyword(s):

Type I Collagen ◽

Small Diameter ◽

Collagen Molecule ◽

Type I ◽

Collagen Types ◽

Type V Collagen ◽

Amino Terminal ◽

Type V ◽

Fibril Diameter

The small-diameter fibrils of the chick corneal stroma are heterotypic, composed of both collagen types I and V. This tissue has a high concentration of type V collagen relative to other type I-containing tissues with larger-diameter fibrils, suggesting that heterotypic interactions may have a regulatory role in the control of fibril diameter. The interactions of collagen types I and V were studied using an in vitro self-assembly system. Collagens were purified from lathyritic chick embryos in the presence of protease inhibitors. The type V collagen preparations contained higher molecular weight forms of the alpha 1(V) and alpha 2(V) chains constituting 60–70% of the total. Rotary-shadow electron micrographs showed a persistence of a small, pepsin-sensitive terminal region in an amount consistent with that seen by electrophoresis. In vitro, this purified type V collagen formed thin fibrils with no apparent periodicity, while type I collagen fibrils had a broad distribution of large diameters. However, when type I collagen was mixed with increasing amounts of type V collagen a progressive and significant decrease in both the mean fibril diameter and the variance was observed for D periodic fibrils. The amino-terminal domain of the type V collagen molecule was required for this regulatory effect and in its absence little diameter reducing activity was observed. Electron microscopy using collagen type-specific monoclonal antibodies demonstrated that the fibrils formed were heterotypic, containing both collagen types I and V. These data indicate that the interaction of type V with type I collagen is one mechanism modulating fibril diameter and is at least partially responsible for the regulation of collagen fibril formation.

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Radioimmunoassay for the pyridinoline cross-linked carboxy-terminal telopeptide of type I collagen: a new serum marker of bone collagen degradation

Clinical Chemistry ◽

10.1093/clinchem/39.4.635 ◽

1993 ◽

Vol 39 (4) ◽

pp. 635-640 ◽

Cited By ~ 393

Author(s):

J Risteli ◽

I Elomaa ◽

S Niemi ◽

A Novamo ◽

L Risteli

Keyword(s):

Type I Collagen ◽

Polyacrylamide Gel Electrophoresis ◽

Sodium Dodecyl ◽

Bone Collagen ◽

Collagen Molecule ◽

Type I ◽

Serum Samples ◽

Amino Terminal ◽

Wide Range ◽

Carboxy Terminal

Abstract We developed a radioimmunoassay (RIA) for the carboxy-terminal telopeptides of type I collagen (ICTP), cross-linked with the helical domain of another type I collagen molecule, after isolation from human femoral bone. The cross-linked peptide was liberated by digesting insoluble, denatured bone collagen either with bacterial collagenase or with trypsin, and purified by two successive reversed-phase separations on HPLC, with monitoring of pyridinoline-specific fluorescence. The purity of the peptide was verified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and its origin in the type I collagen fibers was determined by amino-terminal amino acid sequencing. Polyclonal antibodies and a separation reagent containing second antibody and polyethylene glycol are used in the RIA. An immunologically identical, somewhat larger antigen is present in human serum; its concentration increases in multiple myeloma and in rheumatoid arthritis. The ICTP antigen seems to be cleared from the circulation by the kidneys, because glomerular filtration rates that are two-thirds of normal or less are associated with increased circulating ICTP concentrations. The CVs of the method are between 3% and 8% for a wide range of concentrations. The analysis of 40 serum samples can be completed in 4 h.

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