Collagen structure: Evidence for a helical organization of the collagen fibril

Lillie, John H.; MacCallum, Donald K.; Scaletta, Lawrence J.; Occhino, Joseph C.

doi:10.1016/s0022-5320(77)90025-9

Cited by 72 publications

(30 citation statements)

References 18 publications

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“…The direction oftilt is fixed relative to the radially oriented 3.8-nm spacing. Therefore, the molecules appear to follow a "helical" path around the fibril (25,(27)(28)(29)(30)(31)(32)(33) …”

Section: Resultsmentioning

confidence: 99%

“…D-periodic filaments of the appropriate width have been observed (26) but, because oftheir unknown depth, unequivocal evidence for the existence of a microfibril is still unavailable, and thus the exact nature of the observed filaments remains obscure. Finally, electron microscopy of freeze-fractured preparations (27)(28)(29)(30)(31) or ultrathin sections of either inertly dehydrated (25) or chemically treated (32,33) tissues indicates a helical filamentous arrangement in collagen fibrils.…”

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confidence: 99%

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Electron microscopy shows periodic structure in collagen fibril cross sections.

Hulmes¹,

Jésior²,

Miller³

et al. 1981

Proc. Natl. Acad. Sci. U.S.A.

100

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X-ray diffraction was used to monitor the effects of electron microscope fixation, staining, and embedding procedures on the preservation of the three-dimensional crystalline order in collagen fibrils of rat tail tendon. A procedure is described in which the characteristic 3.8-nm lateral spacing is preserved, with increased contrast, in the diffraction pattern ofthe embedded fiber. This spacing is correlated with the separation between the tangentially oriented equally spaced lines of density observed in electron microscope ultrathin fibril cross sections of the same material. Optical diffraction of electron micrographs gives an objective measure of the periodicity and suggests that the fibril is composed of concentrically oriented crystalline domains. These observations, when combined with a recent interpretation of the native x-ray diffraction data [Hulmes, D. J. Nature (London) 282, 878-880] suggest a tentative model for the three-dimensional structure of collagen fibrils.The one-dimensional or axially projected structure of collagen fibrils is well understood, to the resolution of individual amino acids (1-5), in terms of the modified "quarter stagger" theory for the molecular packing (6, 7). However, the way in which this scheme is extended into three dimensions remains controversial (for review, see refs. 8 and 9). X-ray diffraction from tendon fibers (10-12) indicates three-dimensional crystallinity in the molecular packing although, in some specimens, only the onedimensional 67-nm (D) axial periodicity has been observed (13,14). Collagen fibrils are somewhat analogous to liquid crystals (15)(16)(17), and the one-dimensionally ordered and three-dimensionally ordered phases may correspond to a smectic A -) B transition. Several interpretations have been suggested for the near-equatorial (i.e., perpendicular to the fiber axis) crystalline x-ray data (8, 9), but recently both the observed spacings and the general intensity distribution have been accounted for by quasi-hexagonal packing of straight tilted molecules (9, 18). In contrast to most of the tetragonal packing schemes, the quasihexagonal model does not require the presence ofthe rope-like intermediate substructures, a few molecules in cross section, called microfibrils.Electron microscopy, particularly on negatively stained specimens, indicates that collagen fibrils have a filamentous substructure (19,20). Filaments have also been observed during in vitro collagenfibrillogenesis (21-23). Estimates of filament width vary from 1.5 nm to 4 nm, and so it has been suggested that these filaments correspond to either individual molecules (18,19) To date, no concerted attempt has been made to correlate electron microscopic data with the x-ray diffraction observations that indicate three-dimensional crystallinity in collagen fibrils. So far, there has been no evidence from electron microscopy for long-range lateral order in the native molecular packing. In this paper, we describe the initial results of an extensive joint x-ray diffraction-electron ...

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Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

Electron microscopy shows periodic structure in collagen fibril cross sections.

Hulmes¹,

Jésior²,

Miller³

et al. 1981

Proc. Natl. Acad. Sci. U.S.A.

100

View full text Add to dashboard Cite

show abstract

“…The analysis of serial sections performed in the present study, showed that the subfibrils present on the surface of thick fibrils have a spiral counterclockwise direction, whose meaning, however, is unknown to us. Spiral arrangement of collagen fibrils has been observed after exposition of tissues to 4 M guanidinium chloride (Marchini et al, 1986) or other dissociative solvents such as 8 M urea (Lillie et al, 1977). The images suggest that the ridges could result, at least in part, from the lateral aggregation of collagen fibrils on already formed collagen fibrils.…”

Section: Discussionmentioning

confidence: 99%

Arrangement and fine structure of collagen fibrils in the decidualized mouse endometrium

Carbone

Pinto

Abrahamsohn

et al. 2006

Microscopy Res & Technique

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The adaptations of the mouse uterus to pregnancy include extensive modifications of the cells and extracellular matrix of the endometrial connective tissue that surround the embryos. Around each implanted embryo this tissue redifferentiates into a transient structure called decidua, which is formed by polygonal cells joined by intercellular junctions. In the mouse, thick collagen fibrils with irregular profile appear in decidualized areas of the endometrium but not in the nondecidualized stroma and interimplantation sites. The fine organization of these thick fibrils has not yet been established. This work was addressed to understand the arrangement and fine structure of collagen fibrils of the decidua of pregnant mice during the periimplantation stage. Major modifications occurred in collagen fibrils that surrounded decidual cells: (1) the fibrils, which were arranged in parallel bundles in nonpregnant animals, became organized as baskets around decidual cells; (2) very thick collagen fibrils with very irregular profiles appeared around decidual cells. Analysis of replicas and serial sections suggests that the thick collagen fibrils form by the lateral aggregation of thinner fibrils to a central fibril resulting in very irregular profile observed in cross sections of thick fibrils. The sum of modifications of the collagen fibrils seem to represent an adaptation of the endometrium to better support the decidual cells while they hold the embryos during the beginning of their development. The deposition of thick collagen fibrils in the decidua may contribute to form a barrier that impedes leukocyte migration within the decidua, preventing immunological rejection of genetically dissimilar embryonic tissues.

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“…Treatment with disruption agents such as 8 M urea has been recommended for exposing collagen epitopes, (Fleischmajer et al, 1990a). According to Lillie et al (1977), the urea disrupts collagen fibrils by breaking their hydrogen bonds. The degree of dissociation depends on intra-and intermolecular cross-links and is usually extensive in embryonic skin and to varying degrees in the adult skin.…”

Section: Discussionmentioning

confidence: 99%

Collagen types I, III, and V constitute the thick collagen fibrils of the mouse decidua

Spiess

Zorn

2006

Microscopy Res & Technique

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A mammal's endometrium is deeply remodeled while receiving and implanting an embryo. In addition to cell proliferation and growth, endometrial remodeling also comprises synthesis and degradation of several molecular components of the extracellular matrix. All of these events are orchestrated by a precise sequence of ovarian hormones and influenced by several types of cytokines. As we have previously reported, an intriguing and rapid increase in collagen fibril diameter occurs in the decidualized areas of the endometrium, surrounding the implantation crypt, whereas collagen fibrils situated far from the embryo remain unchanged. Collagen fibrilogenesis is a complex molecular process coordinated by a number of factors, such as the types and amounts of glycosaminoglycans and proteoglycans associated with collagen molecules. Collagen genetic type, mechanical stress, aging, and other factors not yet identified also contribute to this development. A recent study suggests that thick fibrils from mouse decidua are formed, at least in part, by aggregation of thin fibrils existing in the stroma before the onset of decidualization. In the present ultrastructural study using single and double immunogold localization, we showed that both thin and thick collagen fibrils present in the mouse pregnant endometrium endometrium are heterotypic structures formed at least by type I, type III, and type V collagens. However, type V collagen predominates in the thick collagen fibrils, whereas it is almost absent of the thin collagen fibrils. The putative role of type V homotrimer in the rapid increase of the diameter of collagen fibrils of the mouse decidua is discussed.

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Collagen structure: Evidence for a helical organization of the collagen fibril

Cited by 72 publications

References 18 publications

Electron microscopy shows periodic structure in collagen fibril cross sections.

Electron microscopy shows periodic structure in collagen fibril cross sections.

Arrangement and fine structure of collagen fibrils in the decidualized mouse endometrium

Collagen types I, III, and V constitute the thick collagen fibrils of the mouse decidua

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