Twisted Fibrils are a Structural Principle in the Assembly of Interstitial Collagens, Chordae Tendineae Included

Folkhard, W.; Christmann, Daniela; Geercken, W.; Knörzer, E.; Koch, Michel H. J.; Mosler, E.; Nemetschek-Gansler, H.; Nemetschek, Th.

doi:10.1515/znc-1987-11-1225

Cited by 20 publications

(11 citation statements)

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“…The effect of helicoidal molecular packing results in the plane of lateral molecular packing to be displaced at an angle from the perpendicular to the fibril axis; i.e., a molecular tilt is introduced (Folkhard et al, 1987). Since the path of the molecules is relative to a common axis, this ensures that the molecular plane is of a constant angle, but the orientation of the plane varies with respect to the fibril axis.…”

Section: Angular Deviation Of Equatorial Scatteringmentioning

confidence: 99%

“…Several angles have been reported in the literature for such helicoidal fibrils, with the data coming mainly from electron microscopy: 9° ( Folkhard et al, 1987); 12° (Brodsky and Eikenberry, 1982); 12-13° (Itoh et al, 1996); 14 -17° (Katz and David, 1992); 18° (Ruggeri et al, 1979). X-ray diffraction provides strong evidence for molecular inclination and is capable of estimating the variability of inclination angle within an assembly of fibrils.…”

Section: Angular Deviation Of Equatorial Scatteringmentioning

confidence: 99%

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Structure of Type I and Type III Heterotypic Collagen Fibrils: An X-Ray Diffraction Study

Cameron

Alberts

Laing

et al. 2002

Journal of Structural Biology

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Section: Angular Deviation Of Equatorial Scatteringmentioning

confidence: 99%

Section: Angular Deviation Of Equatorial Scatteringmentioning

confidence: 99%

Structure of Type I and Type III Heterotypic Collagen Fibrils: An X-Ray Diffraction Study

Cameron

Alberts

Laing

et al. 2002

Journal of Structural Biology

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“…There has also been discussion of whether there is a causal relationship between the presence of type III collagen and the twisted arrangement of collagen fibrils or a shorter D period, on the basis of data from the vessel wall and other connective tissues containing type I and type III collagen. However, there is experimental evidence indicating that collagen fibrils of aorta described are also formed in the absence of collagen III, as shown for a patient with type IV Ehlers-Danlos syndrome [41]. Studies on lamprey tissues seem to confirm that tilted fibrils and a reduced D period had already evolved before type III collagen was established during evolution [31].…”

Section: Figure 5 Amino Acid Sequences Of C-telopeptides From α1(i) Amentioning

confidence: 89%

Cross-link analysis of the C-telopeptide domain from type III collagen

Henkel

1996

Biochemical Journal

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Several peptides were isolated from tryptic digests of insoluble calf aorta matrix by chromatography. Reductive pyridylethylation of a tryptic 15 kDa pool released fragments deriving from the C-terminus of type III collagen. A 50-residue peptide Tc(III) was shown by sequence analysis to be the C-terminal peptide from the alpha 1(III)-chain, containing a helical and non-helical region of equal sizes. The peptide was further digested with collagenase to give Colc(III), comprising the complete C-terminal non-helical region of alpha 1(III) including a hydroxylysine in position 16c. The peptide Tc(III) x TN(III) was isolated, demonstrating covalent cross-linking between the C-terminal non-helical region of one type III molecule and the N-terminal helical cross-linking region of another. Its digestion with cyanogen bromide yielded the small fragments alpha 1(III)CB3B* and alpha 1(III)CB3C, confirming TN(III) as an N-terminal helical crosslink site. Sequence analysis of both Tc(III) x TN(III) and its collagenase-derived cross-linked peptide Colc(III) x TN(III) established the 4D-staggered alignment of adjacent collagen III molecules. The cross-link structure of both peptides was mainly dihydroxylysinonorleucine with a small amount of hydroxylysinonorleucine, indicating that the lysine residues involved in formation of the cross-links are both hydroxylated. No pyridinoline or histidinohydroxylysinonorleucine cross-links were found within the non-reduced C-telopeptide region of type III collagen.

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“…Then the tendon exhibits a linear region of elongation that involves either extension of the individual collagen components or relative sliding between them [35,42]. In particular, sincrotone X-ray diffraction studies of the tendon matrix demonstrated that only 40% of tendon elongation occurs at the molecular level, whereas about 60% of tendon extension is due to sliding between one or more of the structural levels of collagen [43,44,45]. Interfibrillar sliding is related to the interfibrillar proteoglycans.…”

Section: Discussionmentioning

confidence: 99%

Contribution of Glycosaminoglycans to the Microstructural Integrity of Fibrillar and Fiber Crimps in Tendons and Ligaments

Franchi

Pasquale

Martini

et al. 2010

The Scientific World JOURNAL

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The biomechanical roles of both tendons and ligaments are fulfilled by the extracellular matrix of these tissues. In particular, tension is mainly transmitted and resisted by protein (collagen, elastin) fibers, whereas compression is opposed by water-soluble glycosaminoglycans (GAGs). GAGs spanning the interfibrillar spaces and interacting with fibrils through the interfibrillar proteoglycans also seem to play a part in transmitting and resisting tensile stresses. Both tendons and ligaments showing similar composition, but different functional roles and collagen array, exhibit periodic undulations of collagen fibers or crimps. Each crimp is composed of many knots of each single fibril or fibrillar crimps. Fibrillar and fiber crimps play a mechanical role in absorbing the initial loading during elongation of both tendons and ligaments, and in recoiling fibrils and fibers when tissues have to return to their original length. This study investigated whether GAGs covalently attached to proteoglycan core proteins directly affect the 3D microstructural integrity of fibrillar crimp regions and fiber crimps in both tendons and ligaments. Achilles tendons and medial collateral ligaments of the knee from eight female Sprague-Dawley rats (90 days old) incubated in a chondroitinase ABC solution to remove GAGs were observed under a scanning electron microscope (SEM). In addition, isolated fibrils of these tissues obtained by mechanical disruption were analyzed by a transmission electron microscope (TEM). Both Achilles tendons and medial collateral ligaments of the rats after chemical or mechanical removal of GAGs still showed crimps and fibrillar crimps comparable to tissues with a normal GAG content. All fibrils in the fibrillar crimp region always twisted leftwards, thus changing their running plane, and then sharply bent, changing their course on a new plane. These data suggest that GAGs do not affect structural integrity or fibrillar crimp functions that seem mainly related to the local fibril leftward twisting and the alternating handedness of collagen from a molecular to a supramolecular level.

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Twisted Fibrils are a Structural Principle in the Assembly of Interstitial Collagens, Chordae Tendineae Included

Cited by 20 publications

References 0 publications

Structure of Type I and Type III Heterotypic Collagen Fibrils: An X-Ray Diffraction Study

Structure of Type I and Type III Heterotypic Collagen Fibrils: An X-Ray Diffraction Study

Cross-link analysis of the C-telopeptide domain from type III collagen

Contribution of Glycosaminoglycans to the Microstructural Integrity of Fibrillar and Fiber Crimps in Tendons and Ligaments

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