Stress transfer in collagen fibrils reinforcing connective tissues: Effects of collagen fibril slenderness and relative stiffness

2007 ◽  
Vol 245 (2) ◽  
pp. 305-311 ◽  
Author(s):  
Kheng Lim Goh ◽  
Judith R. Meakin ◽  
Richard M. Aspden ◽  
David W.L. Hukins
Keyword(s):  
Collagen Fibril ◽  
Stress Transfer ◽  
Collagen Fibrils ◽  
Connective Tissues ◽  
Relative Stiffness

scholarly journals Lumican Regulates Collagen Fibril Assembly: Skin Fragility and Corneal Opacity in the Absence of Lumican

1998 ◽  
Vol 141 (5) ◽  
pp. 1277-1286 ◽  
Author(s):  
Shukti Chakravarti ◽  
Terry Magnuson ◽  
Jonathan H. Lass ◽  
Karl J. Jepsen ◽  
Christian LaMantia ◽  
...  
Keyword(s):  
Collagen Fibril ◽  
Significant Proportion ◽  
Keratan Sulfate ◽  
Corneal Opacity ◽  
Collagen Fibrils ◽  
Mutant Mice ◽  
Connective Tissues ◽  
Ehlers Danlos Syndrome ◽  
Transmission Electron ◽  
Skin Fragility

Lumican, a prototypic leucine-rich proteoglycan with keratan sulfate side chains, is a major component of the cornea, dermal, and muscle connective tissues. Mice homozygous for a null mutation in lumican display skin laxity and fragility resembling certain types of Ehlers-Danlos syndrome. In addition, the mutant mice develop bilateral corneal opacification. The underlying connective tissue defect in the homozygous mutants is deregulated growth of collagen fibrils with a significant proportion of abnormally thick collagen fibrils in the skin and cornea as indicated by transmission electron microscopy. A highly organized and regularly spaced collagen fibril matrix typical of the normal cornea is also missing in these mutant mice. This study establishes a crucial role for lumican in the regulation of collagen assembly into fibrils in various connective tissues. Most importantly, these results provide a definitive link between a necessity for lumican in the development of a highly organized collagenous matrix and corneal transparency.

A comparison of the size distribution of collagen fibrils in connective tissues as a function of age and a possible relation between fibril size distribution and mechanical properties

1978 ◽  
Vol 203 (1152) ◽  
pp. 305-321 ◽  
Keyword(s):  
Mechanical Properties ◽  
Tensile Strength ◽  
Size Distribution ◽  
Collagen Fibril ◽  
Average Diameter ◽  
Collagen Fibrils ◽  
Diameter Distribution ◽  
Connective Tissues ◽  
Fibril Diameter ◽  
Covalent Crosslinks

Data on the distribution of collagen fibril diameters in various connective tissues have been collected and analysed for common features. The diameter distributions of the collagen fibrils at birth and in the foetal stages of development are unimodal, whereas at maturity the mass-average diameter of the collagen fibrils is generally larger than at birth and the distributions of fibril sizes may be either unimodal or bimodal depending on the tissue. At senescence, few data are available but in most instances both the mean and mass-average diameters of the collagen fibrils are smaller than those at maturity and the fibril distributions are mainly bimodal. The division between tissues showing unimodal or bimodal fibril distributions at maturity does not simply relate to the type I collagen/type II collagen classification, to the distinction between orientated and unorientated material or indeed directly to the levels of stress and strain encountered by the tissue. However, there may prove to be a relation between a bimodal fibril diameter distribution at maturity and the maintenance over long periods of time of either high stress in stretched tissues or low stress in compressed tissues. It has also been noted that the width of the collagen fibril diameter distribution at birth differs between altricious and precocious animals. The ultimate tensile strength of a connective tissue and the mass-average diameter of the constituent collagen fibrils have been shown to have a positive correlation. Further, the form of the collagen fibril diameter distribution can be directly related to the mechanical properties of the tissue. In particular, it is postulated that the size distribution of the collagen fibrils is largely determined by two factors. First, if the tissue is primarily designed to have high tensile strength, then an increase in the diameter of the collagen fibrils will parallel an increase in the potential density of intrafibrillar covalent crosslinks. Consequently large collagen fibrils are predicted to have a greater tensile strength than small fibrils. Secondly, if the tissue is designed to be elastic and hence withstand creep, then a reduction in the diameter of the collagen fibrils will effectively increase the surface area per unit mass of the fibrils thus enhancing the probability of interfibrillar non-covalent crosslinks between the collagen fibrils and the components of the matrix. The idealized description given may indicate how the mechanical properties of a tissue may be interpreted in terms of the collagen fibril diameter distribution.

Towards a fibrous composite with dynamically controlled stiffness: lessons from echinoderms

2000 ◽  
Vol 28 (4) ◽  
pp. 357-362 ◽  
Author(s):  
J. A. Trotter ◽  
J. Tipper ◽  
G. Lyons-Levy ◽  
K. Chino ◽  
A. H. Heuer ◽  
...  
Keyword(s):  
Sea Urchins ◽  
Fibrous Composite ◽  
Stress Transfer ◽  
Collagen Fibrils ◽  
Synthetic Analogue ◽  
Connective Tissues ◽  
Effector Cells ◽  
Elastomeric Matrix ◽  
Linear Viscoelastic ◽  
Cross Links

Sea urchins and sea cucumbers, like other echinoderms, control the tensile properties of their connective tissues by regulating stress transfer between collagen fibrils. The collagen fibrils are spindle-shaped and up to 1 mm long with a constant aspect ratio of approx. 2000. They are organized into a tissue by an elastomeric network of fibrillin microfibrils. Interactions between the fibrils are regulated by soluble macromolecules that are secreted by local, neurally controlled, effector cells. We are characterizing the non-linear viscoelastic properties of sea cucumber dermis under different conditions, as well as the structures, molecules and molecular interactions that determine its properties. In addition, we are developing reagents that will bind covalently to fibril surfaces and reversibly form cross-links with other reagents, resulting in a chemically controlled stress-transfer capacity. The information being developed will lead to the design and construction of a synthetic analogue composed of fibres in an elastomeric matrix that contains photo- or electro-sensitive reagents that reversibly form interfibrillar cross-links.

Banded Structures in the Connective Tissue of Meningioma

1976 ◽  
Vol 34 ◽  
pp. 234-235
Author(s):  
C. N. Sun ◽  
H. J. White
Keyword(s):  
Connective Tissue ◽  
Osmium Tetroxide ◽  
Uranyl Acetate ◽  
Collagen Fibrils ◽  
Lead Citrate ◽  
Connective Tissues ◽  
Native Collagen ◽  
Routine Procedures

Previously, we have reported on extracellular cross-striated banded structures in human connective tissues of a variety of organs (1). Since then, more material has been examined and other techniques applied. Recently, we studied a fibrocytic meningioma of the falx. After the specimen was fixed in 4% buffered glutaraldehyde and post-fixed in 1% buffered osmium tetroxide, other routine procedures were followed for embedding in Epon 812. Sections were stained with uranyl acetate and lead citrate. There were numerous cross striated banded structures in aggregated bundle forms found in the connecfive tissue of the tumor. The banded material has a periodicity of about 450 Å and where it assumes a filamentous arrangement, appears to be about 800 Å in diameter. In comparison with the vicinal native collagen fibrils, the banded material Is sometimes about twice the diameter of native collagen.

Growth and development of collagen fibrils in immature tissues from rat and sheep

1981 ◽  
Vol 212 (1186) ◽  
pp. 85-92 ◽  
Keyword(s):  
Electron Microscope ◽  
Transmission Electron Microscope ◽  
Collagen Fibril ◽  
Growth And Development ◽  
Collagen Fibrils ◽  
Diameter Distribution ◽  
Rat Tissues ◽  
Transmission Electron ◽  
The Mean ◽  
Fibril Diameter

The collagen fibril diameter distribution of four immature tissues from both rat and sheep have been determined from transverse sections observed in the transmission electron microscope. In many instances before birth, the form of the distribution for the tissues is both unimodal and sharp and the mean diameters of the distributions lie close to a multiple of 80 Å. For some tissues, the collagen fibril diameter distributions may be resolved into a number of components, each of which represents a population of fibrils with a diameter close to a multiple of 80 Å (8 nm). These data confirm and extend previous observations by the authors that small collagen fibrils all have diameters that are multiples of about 80 Å and that the fibril growth occurs by the accretion of 80 Å units. The form of the collagen fibril diameter distribution at birth is broad for the sheep tissues but narrow for the rat tissues, thus confirming that the range of fibril diameters at this stage of life reflects the differing degree of development of precocious and altricious animals.

Stress Dependent Collagen Fibril Diameter Distribution in Human Aortic Valves

2007 ◽  
Author(s):  
Angelique Balguid ◽  
Anita Mol ◽  
Niels Driessen ◽  
Carlijn Bouten ◽  
Frank Baaijens
Keyword(s):  
Mechanical Properties ◽  
Collagen Fibril ◽  
Diameter Distribution ◽  
Connective Tissues ◽  
Aortic Valves ◽  
Cross Links ◽  
Fibril Morphology ◽  
Stress Dependent ◽  
Collagenous Tissues ◽  
Fibril Diameter

The mechanical properties of collagenous tissues are known to depend on a wide variety of factors, such as the type of tissue and the composition of its extracellular matrix. Relating mechanical roles to individual matrix components in such a complex system is difficult, if not impossible. However, as collagen is the main load bearing component in connective tissues, the relation between collagen and tissue biomechanics has been studied extensively in various types of tissues. The type of collagen, the amount and type of inter- and intramolecular covalent cross-links and collagen fibril morphology are involved in the tissues mechanical behavior (Beekman et al., 1997; Parry et al., 1978; Avery and Bailey, 2005). From literature it is known that the the collagen fibril diameter distribution can be directly related to the mechanical properties of the tissue. In particular, the diameter distribution of collagen fibrils is largely determined by the tissues requirement for tensile strength and elasticity (Parry et al., 1978).

scholarly journals The endosome is a master regulator of plasma membrane collagen fibril assembly

2021 ◽  
Author(s):  
Joan Chang ◽  
Adam Pickard ◽  
Richa Garva ◽  
Yinhui Lu ◽  
Donald Gullberg ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Circadian Clock ◽  
Collagen Fibril ◽  
Collagen Fibrils ◽  
Protein Mass ◽  
Stage Of Development ◽  
Collagen Secretion ◽  
Total Protein Mass ◽  
Vacuolar Protein ◽  
Membrane Collagen

abstractCollagen fibrils are the principal supporting elements in vertebrate tissues. They account for 25% of total protein mass, exhibit a broad range of size and organisation depending on tissue and stage of development, and can be under circadian clock control. Here we show that the remarkable dynamic pleomorphism of collagen fibrils is underpinned by a mechanism that distinguishes between collagen secretion and initiation of fibril assembly, at the plasma membrane. Collagen fibrillogenesis occurring at the plasma membrane requires vacuolar protein sorting (VPS) 33b (which is under circadian clock control), collagen-binding integrin-α11 subunit, and is reduced when endocytosis is inhibited. Fibroblasts lacking VPS33b secrete soluble collagen without assembling fibrils, whereas constitutive over-expression of VPS33b increases fibril number with loss of fibril rhythmicity. In conclusion, our study has identified the mechanism that switches secretion of collagen (without forming new fibrils) to new collagen fibril assembly, at the plasma membrane.

Ultrastructural Evidence for Proteoglycans Mediating an Attachment of Type VI Collagen to Banded Collagen Fibrils

1997 ◽  
Vol 3 (S2) ◽  
pp. 153-154
Author(s):  
Douglas R. Keene ◽  
Catherine C. Ridgway ◽  
Renato V. Iozzo
Keyword(s):  
Dermatan Sulfate ◽  
Core Protein ◽  
Solid Phase ◽  
Collagen Fibrils ◽  
Binding Assays ◽  
Connective Tissues ◽  
Type Vi Collagen ◽  
Dermatan Sulfate Proteoglycan ◽  
Individual Type ◽  
Solid Phase Binding

Immunolocalizaton studies of type VI collagen in skin have previously demonstrated that type VI collagen forms a flexible network that anchors large interstitial structures such as nerves, blood vessels, and collagen fibers into the surrounding connective tissues matrix. The purpose of this study is to determine if individual type VI collagen microfilaments might be connected to banded collagen fibrils, thereby stabilizing the network.Solid phase binding assays suggest a specific, high affinity interaction between the core protein of the dermatan sulfate proteoglycan decorin and type VI collagen, and immunocytochemical studies in fetal and neonate rabbit cornea suggest an association of decorin with type VI microfilaments. Other studies in skin and perichondrium have localized decorin to a region between the d and e bands of banded collagen fibrils. However, no direct documentation has demonstrated a specific structural interaction between type VI microfilaments and banded collagen fibrils. We, therefore, sought to determine if type VI microfilaments cross banded collagen fibrils between the “d” and “e” bands.

scholarly journals A Critical Role for the Membrane-type 1 Matrix Metalloproteinase in Collagen Phagocytosis

2006 ◽  
Vol 17 (11) ◽  
pp. 4812-4826 ◽  
Author(s):  
Hyejin Lee ◽  
Christopher M. Overall ◽  
Christopher A. McCulloch ◽  
Jaro Sodek
Keyword(s):  
Inflammatory Diseases ◽  
Human Fibroblasts ◽  
Critical Role ◽  
Collagen Fibrils ◽  
Connective Tissues ◽  
Transmission Electron ◽  
Catalytically Active ◽  
Membrane Type ◽  
Collagen Phagocytosis ◽  
Interfering Rna

Degradation of collagen is important for the physiological remodeling of connective tissues during growth and development as well as in wound healing, inflammatory diseases, and cancer cell invasion. In remodeling adult tissues, degradation of collagen occurs primarily through a phagocytic pathway. However, although various steps in the phagocytic pathway have been characterized, the enzyme required to initially fragment collagen fibrils for subsequent phagocytosis has not been identified. We have used laser confocal microscopy, transmission electron microscopy, and biochemical assays to show that human fibroblasts initiate degradation of collagen through the collagenase activity of the membrane-bound metalloproteinase MT1-MMP. Degradation of natural and reconstituted collagen substrates correlated with the expression of MT1-MMP, which was localized at sites of collagen cleavage at the surface of the cells and also within the cells, whereas collagen degradation was abrogated when MT1-MMP expression was blocked by small interfering RNA treatment. In contrast to MT1-MMP, the gelatinolytic activity of MMP-2 was not required for collagen phagocytosis. These studies demonstrate a pivotal role of catalytically active MT1-MMP in preparing collagen fibrils for phagocytic degradation.

Sign in / Sign up

Export Citation Format

Share Document