Hierarchical structures in fibrillar collagens

Ottani, Vittoria; Martini, Désirèe; Franchi, Martino V.; Ruggeri, Alessandro; Raspanti, Mario

doi:10.1016/s0968-4328(02)00033-1

Cited by 275 publications

(243 citation statements)

References 56 publications

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“…Based on these data and numerous studies demonstrating that the ECM can potently regulate cellular differentiation [53][54][55][56][57], where possible we incorporated our periostin treatments into the collagen substrate, rather than simply amending the tissue culture media, to more closely replicate in vivo conditions. Periostin has been shown to promote collagen fibrillogenesis and alter the deposition of ECM proteins in other systems [58] and larger scale microarray studies have identified COL1A1 mRNA, encoding the collagen α1 component of heterotrimeric and homotrimeric type-1 collagen [59], as up-regulated in DD cord [11,12]. Excess collagen deposition and changes in ECM components are established hallmarks of DD [11,[60][61][62] and collagen in DD cords has been previously reported to feature increased levels of hydroxylysine and reducible cross-links, features also evident in scar tissue and indicative of abnormal deposition [63].…”

Section: Discussionmentioning

confidence: 99%

Periostin differentially induces proliferation, contraction and apoptosis of primary Dupuytren's disease and adjacent palmar fascia cells

Vi¹,

Feng²,

Zhu³

et al. 2009

Experimental Cell Research

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Dupuytren's disease, (DD), is a fibroproliferative condition of the palmar fascia in the hand, typically resulting in permanent contracture of one or more fingers. This fibromatosis is similar to scarring and other fibroses in displaying excess collagen secretion and contractile myofibroblast differentiation. In this report we expand on previous data demonstrating that POSTN mRNA, which encodes the extra-cellular matrix protein periostin, is up-regulated in Dupuytren's disease cord tissue relative to phenotypically normal palmar fascia. We demonstrate that the protein product of POSTN, periostin, is abundant in Dupuytren's disease cord tissue while little or no periostin immunoreactivity is evident in patient-matched control tissues. The relevance of periostin up-regulation in DD was assessed in primary cultures of cells derived from diseased and phenotypically unaffected palmar fascia from the same patients. These cells were grown in type-1 collagen-enriched culture conditions with or without periostin addition to more closely replicate the in vivo environment. Periostinwas found to differentially regulate the apoptosis, proliferation, α smooth muscle actin expression and stressed Fibroblast Populated Collagen Lattice contraction of these cell types. We hypothesize that periostin, secreted by disease cord myofibroblasts into the extra-cellular matrix, promotes the transition of resident fibroblasts in the palmar fascia toward a myofibroblast phenotype, thereby promoting disease progression.

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Section: Discussionmentioning

confidence: 99%

Periostin differentially induces proliferation, contraction and apoptosis of primary Dupuytren's disease and adjacent palmar fascia cells

Vi¹,

Feng²,

Zhu³

et al. 2009

Experimental Cell Research

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“…1) A comparable 29.7-ml volume of water was calculated to lie in the 14 g of collagen fibers in the column bed (see Table 1). 2) Collagen fibers consist of densely packed collagen fibrils (5,6), and it has been demonstrated that most or all of the water in collagen fibers lies within the individual collagen fibrils (see Ref. 22 and references therein).…”

Section: Test Molecule Massmentioning

confidence: 99%

“…This result is even more surprising when one considers that these small molecules must attain this equivalent concentration in the Ͻ10-ms interval in which a given concentration of solute is in contact with the fibril. 5 As a first step to understanding the molecular basis for the ability of small molecules to reach concentration equilibrium with all of the water within the collagen fibril, we have constructed a model of the lateral structure of a typical collagen fibril in the fully hydrated and dry states (Fig. 4).…”

Section: Test Molecule Massmentioning

confidence: 99%

“…Most present evidence shows that the mineral in bone is located primarily within the type I collagen fibril (1)(2)(3)(4)(5)(6), that the fibril is formed first and then mineralized (1,2), and that mineralization replaces water within the fibril with mineral (1,3,4). The collagen fibril therefore plays an important role in mineralization, providing the aqueous compartment in which mineral grows.…”

mentioning

confidence: 95%

“…The fibril is composed of collagen molecules, each 1.1 ϫ 300 nm in size and formed by the association of two ␣1 and one ␣2 polypeptide chains to create a rope-like triple helical structure. The fibril assembles by the noncovalent association of collagen molecules, each offset by 67 nm with respect to its lateral neighbors (5)(6)(7). An axial repeat is 5 ϫ 67 ϭ 335 nm in length, which is longer than the 300 nm collagen molecule.…”

mentioning

confidence: 99%

See 2 more Smart Citations

The Size Exclusion Characteristics of Type I Collagen

Toroian

Lim

Price

2007

Journal of Biological Chemistry

219

113

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The mineral in bone is located primarily within the collagen fibril, and during mineralization the fibril is formed first and then water within the fibril is replaced with mineral. The collagen fibril therefore provides the aqueous compartment in which mineral grows. Although knowledge of the size of molecules that can diffuse into the fibril to affect crystal growth is critical to understanding the mechanism of bone mineralization, there have been as yet no studies on the size exclusion properties of the collagen fibril. To determine the size exclusion characteristics of collagen, we developed a gel filtration-like procedure that uses columns containing collagen from tendon and bone. The elution volumes of test molecules show the volume within the packed column that is accessible to the test molecules, and therefore reveal the size exclusion characteristics of the collagen within the column. These experiments show that molecules smaller than a 6-kDa protein diffuse into all of the water within the collagen fibril, whereas molecules larger than a 40-kDa protein are excluded from this water. These studies provide an insight into the mechanism of bone mineralization. Molecules and apatite crystals smaller than a 6-kDa protein can diffuse into all water within the fibril and so can directly impact mineralization. Although molecules larger than a 40-kDa protein are excluded from the fibril, they can initiate mineralization by forming small apatite crystal nuclei that diffuse into the fibril, or can favor fibril mineralization by inhibiting apatite growth everywhere but within the fibril.

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Other Biopolymers and Synthetic Polymers of Biological Interest

Kaltashov

Eyles

2012

Mass Spectrometry in Structural Biology and Biophysics

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Hierarchical structures in fibrillar collagens

Cited by 275 publications

References 56 publications

Periostin differentially induces proliferation, contraction and apoptosis of primary Dupuytren's disease and adjacent palmar fascia cells

Periostin differentially induces proliferation, contraction and apoptosis of primary Dupuytren's disease and adjacent palmar fascia cells

The Size Exclusion Characteristics of Type I Collagen

Other Biopolymers and Synthetic Polymers of Biological Interest

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