Collagen: Structure, Function and Biomaterial Properties

1986 ◽  
pp. 365-383
Author(s):  
Marcel E. Nimni
Keyword(s):  
Structure Function ◽  
Collagen Structure

scholarly journals Collagen – structure, function and distribution in orodental tissues

2020 ◽  
Vol 2 ◽  
pp. 134-139
Author(s):  
Zaneta D’souza ◽  
Tabita Joy Chettiankandy ◽  
Manisha S. Ahire (Sardar) ◽  
Arush Thakur ◽  
Sarang G. Sonawane ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Cell Adhesion ◽  
Structure Function ◽  
Large Family ◽  
The Body ◽  
Collagen Structure ◽  
Basic Framework ◽  
Helical Proteins ◽  
And Function

Collagens are a large family of triple helical proteins which are found extensively throughout the body. They form the basic framework of the extracellular matrix providing support and form to cells and tissues. They are important for various functions such as angiogenesis, morphogenesis, cell adhesion, repair, and regeneration. In this article, we have focused our discussion to the structure, the synthesis, and the degradation of collagen followed by its distribution and function in various oral tissues.

HIF pathway activation is a core regulator of collagen structure-function in lung fibrosis

2020 ◽  
Author(s):  
Christopher J Brereton ◽  
Robert Ridley ◽  
Franco Conforti ◽  
Liudi Yao ◽  
Aiman Alzetani ◽  
...  
Keyword(s):  
Structure Function ◽  
Lung Fibrosis ◽  
Collagen Structure ◽  
Pathway Activation ◽  
Hif Pathway

scholarly journals Collagen Structure-Function Mapping Informs Applications for Regenerative Medicine

2020 ◽  
Vol 8 (1) ◽  
pp. 3
Author(s):  
James D. San Antonio ◽  
Olena Jacenko ◽  
Andrzej Fertala ◽  
Joseph P.R.O. Orgel
Keyword(s):  
Structure Function ◽  
Cancer Metastasis ◽  
Type I Collagen ◽  
Tissue Injury ◽  
Tissue Remodeling ◽  
Type Iii Collagen ◽  
Type I ◽  
Collagen Structure ◽  
Interaction Domain ◽  
Functional Sites

Type I collagen, the predominant protein of vertebrates, assembles into fibrils that orchestrate the form and function of bone, tendon, skin, and other tissues. Collagen plays roles in hemostasis, wound healing, angiogenesis, and biomineralization, and its dysfunction contributes to fibrosis, atherosclerosis, cancer metastasis, and brittle bone disease. To elucidate the type I collagen structure-function relationship, we constructed a type I collagen fibril interactome, including its functional sites and disease-associated mutations. When projected onto an X-ray diffraction model of the native collagen microfibril, data revealed a matrix interaction domain that assumes structural roles including collagen assembly, crosslinking, proteoglycan (PG) binding, and mineralization, and the cell interaction domain supporting dynamic aspects of collagen biology such as hemostasis, tissue remodeling, and cell adhesion. Our type III collagen interactome corroborates this model. We propose that in quiescent tissues, the fibril projects a structural face; however, tissue injury releases blood into the collagenous stroma, triggering exposure of the fibrils’ cell and ligand binding sites crucial for tissue remodeling and regeneration. Applications of our research include discovery of anti-fibrotic antibodies and elucidating their interactions with collagen, and using insights from our angiogenesis studies and collagen structure-function model to inform the design of super-angiogenic collagens and collagen mimetics.

scholarly journals Author response: Nanoscale dysregulation of collagen structure-function disrupts mechano-homeostasis and mediates pulmonary fibrosis

2018 ◽  
Author(s):  
Mark G Jones ◽  
Orestis G Andriotis ◽  
James JW Roberts ◽  
Kerry Lunn ◽  
Victoria J Tear ◽  
...  
Keyword(s):  
Pulmonary Fibrosis ◽  
Structure Function ◽  
Author Response ◽  
Collagen Structure

scholarly journals Nanoscale dysregulation of collagen structure-function disrupts mechano-homeostasis and mediates pulmonary fibrosis

eLife ◽  
2018 ◽  
Vol 7 ◽  
Author(s):  
Mark G Jones ◽  
Orestis G Andriotis ◽  
James JW Roberts ◽  
Kerry Lunn ◽  
Victoria J Tear ◽  
...  
Keyword(s):  
Pulmonary Fibrosis ◽  
Structure Function ◽  
Ex Vivo ◽  
Lysyl Oxidase ◽  
Cross Linking ◽  
Collagen Structure ◽  
Tissue Stiffness ◽  
Collagen Concentration ◽  
Dual Inhibition

Matrix stiffening with downstream activation of mechanosensitive pathways is strongly implicated in progressive fibrosis; however, pathologic changes in extracellular matrix (ECM) that initiate mechano-homeostasis dysregulation are not defined in human disease. By integrated multiscale biomechanical and biological analyses of idiopathic pulmonary fibrosis lung tissue, we identify that increased tissue stiffness is a function of dysregulated post-translational collagen cross-linking rather than any collagen concentration increase whilst at the nanometre-scale collagen fibrils are structurally and functionally abnormal with increased stiffness, reduced swelling ratio, and reduced diameter. In ex vivo and animal models of lung fibrosis, dual inhibition of lysyl oxidase-like (LOXL) 2 and LOXL3 was sufficient to normalise collagen fibrillogenesis, reduce tissue stiffness, and improve lung function in vivo. Thus, in human fibrosis, altered collagen architecture is a key determinant of abnormal ECM structure-function, and inhibition of pyridinoline cross-linking can maintain mechano-homeostasis to limit the self-sustaining effects of ECM on progressive fibrosis.

scholarly journals Pseudohypoxic HIF pathway activation dysregulates collagen structure-function in human lung fibrosis

2021 ◽  
Author(s):  
Christopher J Brereton ◽  
Liudi Yao ◽  
Yilu Zhou ◽  
Milica Vukmirovic ◽  
Joseph A Bell ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Structure Function ◽  
Lung Fibrosis ◽  
Human Lung ◽  
Ex Vivo ◽  
Fibrillar Collagen ◽  
Collagen Structure ◽  
Critical Pathway ◽  
Pathway Activation ◽  
Hif Pathway

Extracellular matrix (ECM) stiffening with downstream activation of mechanosensitive pathways is strongly implicated in fibrosis. We previously reported that altered collagen nanoarchitecture is a key determinant of pathogenetic ECM structure-function in human fibrosis (Jones et al., 2018). Here, through human tissue, bioinformatic and ex vivo studies we show that hypoxia-inducible factor (HIF) pathway activation is a critical pathway for this process regardless of oxygen status (pseudohypoxia). Whilst TGFβ increased rate of fibrillar collagen synthesis, HIF pathway activation was required to dysregulate post-translational modification of fibrillar collagen, promoting 'bone-type' cross-linking, altering collagen nanostructure, and increasing tissue stiffness. In vitro, knock down of Factor Inhibiting HIF (FIH) or oxidative stress caused pseudohypoxic HIF activation in normal fibroblasts. In contrast, endogenous FIH activity was reduced in fibroblasts from patients with lung fibrosis in association with significantly increased normoxic HIF pathway activation. In human lung fibrosis tissue, HIF mediated signalling was increased at sites of active fibrogenesis whilst subpopulations of IPF lung mesenchymal cells had increases in both HIF and oxidative stress scores. Our data demonstrate that oxidative stress can drive pseudohypoxic HIF pathway activation which is a critical regulator of pathogenetic collagen-structure function in fibrosis.

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