Collagen Diversity, Synthesis and Assembly

Hulmes, David J.S.

doi:10.1007/978-0-387-73906-9_2

Cited by 146 publications

(181 citation statements)

References 116 publications

(125 reference statements)

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“…The temperature of denaturation in corneal samples was not different between young mature (Y-C) and ageing (A-C) groups (Table 1). Accounting for the fact that after maturation of the tissue the only possible change in crosslinking profile of collagen can be caused by glycation [2,3], a similarly low level of advanced glycation end products (AGEs) in both age groups could be inferred. That conclusion is confirmed by fluorescence intensity which was very low in samples from both young mature and ageing rabbits (Fig.…”

Section: Discussionmentioning

confidence: 99%

“…Formation of all collagen fibres is based on similar biochemical pathways-posttranslational modifications of lysine residues [2,3]. However, both the extent of hydroxylation of lysine in the molecules and the presence of other matrix constituents result in the diversity of structures among collagen based tissues.…”

Section: Introductionmentioning

confidence: 99%

“…However, both the extent of hydroxylation of lysine in the molecules and the presence of other matrix constituents result in the diversity of structures among collagen based tissues. Even though the primary sequence of a type I collagen molecule is identical in different tissues, a broad variety of possible dimensions and arrangements of fibres results in very different structures, such as tendon, skin, bones, cornea or fibrocartilage [1,2]. Moreover, the structure of collagenous matrix in the same tissue changes during maturation and ageing as a result of enzymatic and non-enzymatic crosslinking residues.…”

Section: Introductionmentioning

confidence: 99%

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Thermal stability of collagen in naturally ageing and in vitro glycated rabbit tissues

Trębacz

Szczęsna

Arczewska

2018

J Therm Anal Calorim

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The aim of the work was to compare glycation-related changes in thermal denaturation of collagen in naturally ageing and in vitro ribosylated tissues. Samples of cornea, meniscus and Achilles tendon from young adult and from ageing rabbits were compared. Moreover, in vitro glycated samples (ribose, 100 mg mL -1 , 14 days) were prepared for both age groups. Collagen in tissues was characterized in terms of thermal denaturation parameters obtained from differential scanning calorimetry. The level of pentosidine and other fluorescent advanced glycation end products (AGEs) in the papain-digested tissue samples was evaluated using spectrofluorimetry (k ex/em : 335/385 and 370/440 nm). In naturally ageing tissues, changes in properties of extracellular matrix collagen expressed in terms of parameters of thermal denaturation and fluorescent AGEs levels were tissue dependent and were related to differences in organization of matrix components. No signs of increased level of AGEs were found in the naturally ageing cornea, unlike in the tendon and meniscus. In vitro ribation proved by gains of fluorescent AGEs affected thermal stability of collagen in all tissues, both in young adult and in the ageing ones. The effects of ribation were considerably greater than the effects of natural ageing. The increase in denaturation temperature was similarly strong in all tissues and did not correlate with the increase in fluorescent AGEs. As a conclusion, parameters of collagen thermal denaturation are tissue and age dependent and an amount of fluorescent AGEs is not the only determinant of increasing thermal stability of glycated collagen.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Thermal stability of collagen in naturally ageing and in vitro glycated rabbit tissues

Trębacz

Szczęsna

Arczewska

2018

J Therm Anal Calorim

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“…Types I, II, and III form the basic structural units of collagen fibrils and fibers along with some minor types of collagen including types V, IX and XII [9]. Type I collagen is found in tendons, skin, cornea, bone, lung and vessel walls [10]. This collagen is thought to give rise to the high tensile strengths of collagen fibers in tissues; in addition, it actively is involved in other physiologic processes such mechanotransduction [2].…”

Section: Collagen Molecular Structurementioning

confidence: 99%

Mechanical Analysis of Multi-Component Tissues

Silver¹,

Shah²

2017

WJM

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Collagen is the major structural fiber found in mammalian tissues. It is a protein in the form of a triple-helix which is found in several subfamilies, the most abundant of which is the fiber forming group containing Types I, II and III. Type I collagen is found in tendons, skin, cornea, bone, lung and vessel walls. This collagen is thought to give rise to the high tensile strengths of collagen fibers in tissues; in addition, it is actively involved in other physiologic processes such mechanotransduction. However, the non-linear mechanical behavior and viscoelasticity of collagen fibers make analysis of the mechanical properties of tissues complicated. Mechanistically, during mechanical loading, a tensional increase in the D period is observed with increasing strain that is associated with: 1) molecular elongation at the triple-helical level of structure; 2) increases in the gap distance between the end of one triple-helix and the start of the next one in the microfibril; and 3) molecular slippage. In this paper, we discuss the relationship between collagen hierarchical structure and its non-linear mechanical properties. Using vibrational analysis and optical coherence tomography, it is hoped that the mechanical properties of collagenous tissues can be studied in vivo in order to better understand tissue mechanics and to be better able to offer early diagnosis and differentiation of different disease states.

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“…Depending on the tissue type and, thus, function, collagen molecules can form diverse supramolecular arrangements, from dense and rigid nano-/microfibrils to extended branched elastic networks. However, all collagen types share common characteristics (Hulmes 2008): they consist of three polypeptide chains, each of which having at least one domain formed by a repeating -(Gly-X-Y)-n motif, n generally falling in the range 337-343. The Glycine residue provides flexibility to the chains such that the overall macromolecular conformation strongly relies on the nature of the two other amino acids and the extension of this domain.…”

Section: Structural and Chemical Characteristics Of Some Biominerals mentioning

confidence: 99%

Informative Potential of Multiscale Observations in Archaeological Biominerals Down to Nanoscale

Reiche

Gourrier

2016

Nanoscience and Cultural Heritage

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Collagen Diversity, Synthesis and Assembly

Cited by 146 publications

References 116 publications

Thermal stability of collagen in naturally ageing and in vitro glycated rabbit tissues

Thermal stability of collagen in naturally ageing and in vitro glycated rabbit tissues

Mechanical Analysis of Multi-Component Tissues

Informative Potential of Multiscale Observations in Archaeological Biominerals Down to Nanoscale

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