scholarly journals Matrix fully loaded: Assembly and secretion of collagen fibrils

2003 ◽  
Vol 25 (5) ◽  
pp. 11-13
Author(s):  
Karl E. Kadler ◽  
Elizabeth G. Canty ◽  
Yinhui Lu
Keyword(s):  
Extracellular Matrix ◽  
Plasma Membrane ◽  
Secretory Pathway ◽  
Type I Collagen ◽  
Fibril Formation ◽  
Collagen Fibrils ◽  
Type I ◽  
Small Proteins ◽  
Unpublished Work ◽  
Structural Work

The secretory pathway operates like a well-oiled machine when it comes to secreting small proteins. But how does it cope with stiff rod-like molecules such as type I collagen, which spontaneously self-assembles into the millimetre-long collagen fibrils that are characteristic of the extracellular matrix (ECM)? A recent study in our laboratory shows that the secretory pathway adapts exquisitely to intracellular fibril formation by creating tubular vesicles that dock to specialized secretory nozzles in the plasma membrane (E.G. Canty, Y. Lu, R.M. Meadows, M. Shaw, D.F. Holmes and K.E. Kadler, unpublished work). This article gives a brief account of the biochemical and structural work that led up to these new observations.

scholarly journals Stepwise proteolytic activation of type I procollagen to collagen within the secretory pathway of tendon fibroblasts in situ

2011 ◽  
Vol 441 (2) ◽  
pp. 707-717 ◽  
Author(s):  
Elizabeth G. Canty-Laird ◽  
Yinhui Lu ◽  
Karl E. Kadler
Keyword(s):  
Extracellular Matrix ◽  
Secretory Pathway ◽  
Brefeldin A ◽  
Collagen Fibrils ◽  
Proteinase Activity ◽  
Type I ◽  
Proteolytic Activation ◽  
Type I Procollagen ◽  
Tail Tendon

Proteolytic cleavage of procollagen I to collagen I is essential for the formation of collagen fibrils in the extracellular matrix of vertebrate tissues. Procollagen is cleaved by the procollagen N- and C-proteinases, which remove the respective N- and C-propeptides from procollagen. Procollagen processing is initiated within the secretory pathway in tendon fibroblasts, which are adept in assembling an ordered extracellular matrix of collagen fibrils in vivo. It was thought that intracellular processing was restricted to the TGN (trans-Golgi network). In the present study, brefeldin A treatment of tendon explant cultures showed that N-proteinase activity is present in the resulting fused ER (endoplasmic reticulum)–Golgi compartment, but that C-proteinase activity is restricted to the TGN in embryonic chick tendon fibroblasts. In late embryonic and postnatal rat tail and postnatal mouse tail tendon, C-proteinase activity was detected in TGN and pre-TGN compartments. Preventing activation of the procollagen N- and C-proteinases with the furin inhibitor Dec-RVKR-CMK (decanoyl-Arg-Val-Lys-Arg-chloromethylketone) indicated that only a fraction of intracellular procollagen cleavage was mediated by newly activated proteinases. In conclusion, the N-propeptides are removed earlier in the secretory pathway than the C-propeptides. The removal of the C-propeptides in post-Golgi compartments most probably indicates preparation of collagen molecules for fibril formation at the cell–matrix interface.

scholarly journals Matrix metalloproteinase 14 is required for fibrous tissue expansion

eLife ◽  
2015 ◽  
Vol 4 ◽  
Author(s):  
Susan H Taylor ◽  
Ching-Yan Chloé Yeung ◽  
Nicholas S Kalson ◽  
Yinhui Lu ◽  
Paola Zigrino ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Collagen Fibril ◽  
Type I Collagen ◽  
Fibrous Tissue ◽  
Tissue Expansion ◽  
Collagen Fibrils ◽  
Collagen I ◽  
Type I ◽  
Tendon Development

Type I collagen-containing fibrils are major structural components of the extracellular matrix of vertebrate tissues, especially tendon, but how they are formed is not fully understood. MMP14 is a potent pericellular collagenase that can cleave type I collagen in vitro. In this study, we show that tendon development is arrested in Scleraxis-Cre::Mmp14 lox/lox mice that are unable to release collagen fibrils from plasma membrane fibripositors. In contrast to its role in collagen turnover in adult tissue, MMP14 promotes embryonic tissue formation by releasing collagen fibrils from the cell surface. Notably, the tendons grow to normal size and collagen fibril release from fibripositors occurs in Col-r/r mice that have a mutated collagen-I that is uncleavable by MMPs. Furthermore, fibronectin (not collagen-I) accumulates in the tendons of Mmp14-null mice. We propose a model for cell-regulated collagen fibril assembly during tendon development in which MMP14 cleaves a molecular bridge tethering collagen fibrils to the plasma membrane of fibripositors.

scholarly journals The Dynamic Interaction between Extracellular Matrix Remodeling and Breast Tumor Progression

Cells ◽  
2021 ◽  
Vol 10 (5) ◽  
pp. 1046
Author(s):  
Jorge Martinez ◽  
Patricio C. Smith
Keyword(s):  
Extracellular Matrix ◽  
Type I Collagen ◽  
Cell Metabolism ◽  
Breast Tumors ◽  
Extracellular Matrix Remodeling ◽  
Type I ◽  
Matrix Remodeling ◽  
Desmoplastic Reaction ◽  
The Impact

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.

scholarly journals Thermal (In)Stability of Type I Collagen Fibrils

2009 ◽  
Vol 102 (4) ◽  
Author(s):  
S. G. Gevorkian ◽  
A. E. Allahverdyan ◽  
D. S. Gevorgyan ◽  
A. L. Simonian
Keyword(s):  
Type I Collagen ◽  
Collagen Fibrils ◽  
Type I

Detection of type I collagen fibrils formation and dissociation by a fluorescence method based on thioflavin T

2016 ◽  
Vol 92 ◽  
pp. 1175-1182 ◽  
Author(s):  
Meilian Zou ◽  
Huan Yang ◽  
Haibo Wang ◽  
Haiyin Wang ◽  
Juntao Zhang ◽  
...  
Keyword(s):  
Type I Collagen ◽  
Collagen Fibrils ◽  
Fluorescence Method ◽  
Thioflavin T ◽  
Type I

scholarly journals Mechanical Properties of Native and Cross-linked Type I Collagen Fibrils

2008 ◽  
Vol 94 (6) ◽  
pp. 2204-2211 ◽  
Author(s):  
Lanti Yang ◽  
Kees O. van der Werf ◽  
Carel F.C. Fitié ◽  
Martin L. Bennink ◽  
Pieter J. Dijkstra ◽  
...  
Keyword(s):  
Mechanical Properties ◽  
Type I Collagen ◽  
Collagen Fibrils ◽  
Type I

The ultrastructure of type I collagen at nanoscale: large or small D-spacing distribution?

Nanoscale ◽  
2014 ◽  
Vol 6 (14) ◽  
pp. 8134-8139 ◽  
Author(s):  
Hai-Nan Su ◽  
Li-Yuan Ran ◽  
Zhi-Hua Chen ◽  
Qi-Long Qin ◽  
Mei Shi ◽  
...  
Keyword(s):  
Type I Collagen ◽  
Collagen Fibrils ◽  
Type I ◽  
Spacing Distribution ◽  
Large Distribution

The large distribution ofD-spacing values of type I collagen fibrils was due to image drift during measurement, and theD-spacing values were nearly identical both within a single fibril bundle and in different fibril bundles, exhibiting only a narrow distribution of 2.5 nm.

Regulation of extracellular matrix production by chemically synthesized subfragments of type I collagen carboxy propeptide

Biochemistry ◽  
1991 ◽  
Vol 30 (29) ◽  
pp. 7097-7104 ◽  
Author(s):  
Kou Katayama ◽  
Jerome M. Seyer ◽  
Rajendra Raghow ◽  
Andrew H. Kang
Keyword(s):  
Extracellular Matrix ◽  
Type I Collagen ◽  
Type I ◽  
Extracellular Matrix Production ◽  
Matrix Production
Sign in / Sign up

Export Citation Format

Share Document