Type V collagen: heterotypic type I/V collagen interactions in the regulation of fibril assembly

Type V collagen is a quantitatively minor fibrillar collagen with a broad tissue distribution. The most common type V collagen isoform is alpha1(V)(2) alpha2(V) found in cornea. However, other isoforms exist, including an [alpha1(V)alpha2(V)alpha3(V)] form, an alpha1(V)(3) homotrimer and hybrid type V/XI forms. The functional role and fibrillar organization of these isoforms is not understood. In the cornea, type V collagen has a key role in the regulation of initial fibril assembly. Type I and type V collagen co-assemble into heterotypic fibrils. The entire triple-helical domain of the type V collagen molecules is buried within the fibril and type I collagen molecules are present along the fibril surface. The retained NH(2)-terminal domains of the type V collagen are exposed at the surface, extending outward through the gap zones. The molecular model of the NH(2)-terminal domain indicates that the short alpha helical region is a flexible hinge-like region allowing the peptide to project away from the major axis of the molecule; the short triple-helical regions serve as an extension through the hole zone, placing the tyrosine-rich domain at the surface. The assembly of early, immature fibril intermediates (segments) is regulated by the NH(2)-terminal domain of type V collagen. These NH(2)-terminal domains alter accretion of collagen molecules onto fibrils and therefore lateral growth. A critical density would favor the initiation of new fibrils rather than the continued growth of existing fibrils. Other type V collagen isoforms are likely to have an important role in non-cornea tissues. This role may be mediated by supramolecular aggregates different from those in the corneal stroma or by an alteration of the interactions mediated by tissue-specific type V collagen domains generated by different isoforms or aggregate structures. Presumably, the aggregate structure or specific domains are involved in the regionalization of fibril-associated macromolecules necessary for the tissue-specific regulation of later fibril growth and matrix assembly stages.     

Fourier transform of the collagen triple-helical structure and its significance

The Fourier transforms of the collagen molecular structure have been calculated taking into consideration various side chain atoms, as well as the presence of bound water molecules. There is no significant change in the calculated intensity distribution on including the side chain atoms of non-imino-acid residues. Taking into account the presence of about two bound water molecules per tripeptide unit, the agreement with the observed x-ray pattern is slightly improved. Fourier transforms have also been calculated for the detailed molecular geometries proposed from other laboratories. It is found that there are no major differences between them, as compared to our structure, either in the positions of peak intensity or in the intensity distribution. Hence it is not possible to judge the relative merits of the various molecular geometries for the collagen triple helix from a comparison of the calculated transforms with the meagre data available from its x-ray fibre pattern. It is also concluded that the collagen molecular structure should be regarded as a somewhat flexible chain structure, capable of adapting itself to the requirements of the different side groups which occur in each local region.     

STEM/TEM studies of collagen fibril assembly

Quantitative scanning transmission electron microscopy (STEM), implemented on a conventional transmission electron microscope with STEM-attachment, has been a primary tool in our laboratory for the quantitative analysis of collagen fibril assembly in vivo and in vitro. Using this technique, a precise measurement of mass per unit length can be made at regular intervals along a fibril to generate an axial mass distribution (AMD). This in turn allows the number of collagen molecules to be calculated for every transverse section of the fibril along its entire length. All fibrils show a near-linear AMD in their tip regions. Only fibrils formed in tissue environments, however, show a characteristic abrupt change in mass slope along their tips. It appears that this tip growth characteristic is common to fibrils from evolutionarily diverse systems including vertebrate tendon and the mutable tissues of the echinoderms. Computer models of collagen fibril assembly have now been developed based on interpretation of the STEM data. Two alternative models have so far been generated for fibril growth by accretion; one is based on diffusion limited aggregation (DLA) and the other based on an interface-limited growth mechanism. Inter-fibrillar fusion can also contribute to the growth of fibrils in vertebrate tissues and STEM data indicates the presence of a tight regulation in this process. These models are fundamental for the hypotheses regarding how cells synthesise and spatially organise an extracellular matrix (ECM), rich in collagen fibrils.     

Influence of saline and pH on collagen type I fibrillogenesis in vitro: fibril polymorphism and colloidal gold labelling

We have produced different collagen type I fibrils by in vitro fibrillogenesis of acetic acid-soluble collagen within the pH range 2.5-9.0, in the presence and absence of 150 mM NaCl. The varying relatively stable molecular assemblies and polymorphic fibrillar end-products produced after 24 h incubation have been assessed and compared by the TEM study of specimens negatively stained with uranyl acetate. In the presence of 150 mM NaCl, the assembly of collagen at low pH (2.5) leads to the formation of initial molecular aggregates that progressively link together at slightly higher pH (5.0) to form sub-fibrils and spindle-shaped D-banded bundles of sub-fibrils. At pH 6.0 these D-banded bundles aggregate into larger spindle-shaped fibrils with lateral misalignment of the D-banding across the bundle. However, at pH 7.0 and 8.0, in the presence of 150 mM NaCl, the characteristic parallel-sided mature D-banded collagen type I fibres are formed. At pH 9.0 more loosely formed parallel-sided D-banded collagen fibrils are present, within which the spindle-shaped sub-fibrils can be defined by negative staining more convincingly than at pH 7-8. In the presence of 50 mM buffer at pH 2.5, but absence of 150 mM NaCl, collagen type I forms disorganized periodic initial molecular aggregates, which have a tendency to link together to form sub-fibrils. Flexuous collagen type I sub-fibrils predominate at pH 5.0, alongside large spindle-shaped fibrils that possess a regular transverse approximately 10 nm periodicity, with an oblique approximately 67 nm periodicity, significantly different to the D-banding periodicity. At pH 7.0 and pH 8 in the absence of saline loosely-formed flexuous and spindle-shaped fibres co-exist, with underlying sub-fibrils visible, but at pH 9.0 only disorganized flexuous fibrillar aggregates are present. Colloidal gold labelling of the characteristic D-banded collagen type I fibrils with 5 nm and 2 nm chemically reactive gold particles reveals a periodic labelling pattern, which is not apparent with 10 nm and 15 nm gold particles, due to steric hindrance. The flexuous and spindle-shaped collagen fibrils also bind 2 nm gold particles in a specific manner. In all cases, the specific chemisorption of gold onto the collagen fibrils is probably determined by the availability of repeating amino acid side chains of the collagen molecules along the fibril surface. The controlled production of varying stable collagen type I fibrillogenesis products is likely to be of value within numerous areas of biotechnology, biology and medicine, including experimental biomineralization.     

The Landau domain structure in superconducting zinc

Experimental data are reported for the dependence of the periodicity of the Landau domain structure in zinc on the fraction of the sample surface in the normal state. The data show good agreement with a modified form of the Landau-Sharvin Theory.     

Honeycomb domain structure

A theory is given of a new structure produced when demagnetizing uniaxial single crystals (e.g. magnetoplumbite) in a field normal to thec axis. The experimental results fully support the theory on the assumption that domain structures produced under normal conditions are metastable. Methods are given by which stable structures can be prepared from such metastable ones. On the basis of these results opinions are expressed as to the nucleation of plate and honeycomb structures, produced either by reducing the field from saturation or by cooling below the Curie point.

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In conclusion the authors would like to thank C. Novák from the Institute of Technical Physics, Czechoslovak Academy of Sciences, for checking the calculation of the harmonic analysis and Z. Málek and J. Eousek for carefully reading the paper and for valuable remarks.     

The surface structure of V(100)

The structure of the clean V(100)?(1×1) surface is determined, based on an r-factor comparison of experimental LEED intensity-energy spectra with the results of multiple-scattering model calculations. Minimization of the r-factor with respect to the calculational variables leads to optimum values of the first and second interlayer spacings of $\text{d}{}_1\text{=1.41 ± 0.01}\text{A}\text{?}$ and $\text{d}{}_2\text{=1.53 ±0.01}\text{A}\text{?}$, corresponding respectively to a contraction of 7% and an expansion of 1% with respect to the bulk value of $\text{d}{}_{\mathrm{<mtext>B</mtext>}}\text{=1.5141}\text{A}\text{?}$. Preliminary studies of the adsorption of O₂ and CO confirm that the V(100)?(5×1) structure observed during the process of cleaning the crystal is not characteristic of the clean surface, as suggested recently by Davies and Lambert (Surface Science 107 (1981) 391), but rather is associated with the presence of a significant concentration of oxygen in the surface region.     

The thickness dependence of the domain structure of magnetoplumbite

The changes in domain structure as a function of the thickness of the crystal are studied on artificial magnetoplumbite crystals. The thickness dependence of the width of the domains is also studied; up to thicknesses of about 10 it follows the theoretical halfpower law. Above 10 the exponent is 0·633. The energy density of the Bloch walls=4·82 erg cm^–2 and the exchange constantA=0·66×10^–6 erg cm^–1 are calculated on the basis of the above measurements.

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. , 10 . 0,633. = =4,82 erg m^–2 =0,66.10^–6 erg cm^–2.

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We thank Z. Málek and V. Janovec for discussions and some remarks.     

Pinning of vortices by the domain structure in a two-layered type II superconductor-ferromagnet system

The effectiveness of magnetic pinning of vortices in a layered system formed by a uniaxial ferromagnet and type II superconductor is considered. It is shown that, irrespective of the saturation magnetization of the ferromagnet, the energy of pinning at the domain structure does not exceed, in order of magnitude, the energy of artificial pinning at a column-type defect. The limitation of pinning energy is caused by the interaction of external vortices with a spontaneous vortex lattice formed in the superconducting film when the magnetization of the ferromagnetic film exceeds the critical value.     

PT/PZT/PT铁电薄膜的铁电畴和畴壁

用sol-gel法制备出了具有良好铁电性、纯钙钛矿结构的PbTiO₃/Pb(Zr_0.3Ti_0.7)O₃/PbTiO₃(PT/PZT/PT)新型夹心结构铁电薄膜.用扫描力显微镜(SFM)的压电响应模式获得了薄膜铁电畴的垂直于膜平面方向(OPP)、膜平面内(IPP)及OPP的相位和幅度图像，结合理论分析指出薄膜的电畴主要由c畴和偏离垂直于膜平面方向上的c畴构成，薄膜取向的复杂性导致了复杂的畴结构.对于［111］取向的薄膜，当偏离垂直于膜平面方向上的c畴在垂直膜平面方向和面内方向都相反时构成180°的畴壁，在垂直膜平面方向上相同、面内方向相反或由垂直膜平面方向上相反、面内方向相同时构成90°畴壁. 关键词： 铁电薄膜 PT/PZT/PT 电畴和畴壁 扫描力显微镜(SFM)     

The structure and the energy of the cross-tie domain walls

The paper gives the model of the cross-tie walls in thin ferromagnetic films. The distance between side walls, in our model, increases for increasing thickness D of the film, which is in accordance to the experimental data.     

The lyapunov exponent near the criticality of type V intermittency

With a piecewise linear map, we show both analytically and numerically that the Lyapunov exponent forms a complete devil's staircase, and that its value follows a 1/In ∈ law when the driving parameter ∈ changes in the vicinity of the criticality of type V intermittency. These conclusions are in good agreement with the experimental observations in an electronic relaxation oscillator.     

The valence band structure of V−Mo solid solutions

The electronic structure of V _x Mo_1–x (x=0.2; 0.4; 0.6; 0.75) solid solutions was studied by XPS and UPS. The density of states at the Fermi energy,N(E _F), deduced from these measurements, shows a minimum as a function of the alloy concentration on the Mo rich side. This behaviour can be explained by band structure calculations and is in good agreement with previous NMR measurements. The relation between the electronic structure at the Fermi level and the superconducting properties is discussed. The band structure of the Mo rich alloys can be understood in terms of a rigid band model.     

The role of collagen in bone structure: an image processing approach

Bone collagen structure in normal and pathological tissues is illustrated using techniques of thin section transmission electron microscopy and computer-assisted analysis. The normal bone collagen types, fibril architecture and diameter are described. In pathological tissue, deviations from normal fine structure are reflected in abnormal arrangements of collagen fibrils and abnormalities in fibril diameter. Computer analyses of normal fibril positive staining patterns are presented in order to provide a basis for comparing such patterns with pathological ones.     

Bianchi type V perfect-fluid space-times

A method is presented to generate exact solutions of the Einstein field equations in Bianchi type V space-times. The energy-momentum tensor is of perfect fluid type. Starting from particular solutions, new classes of solutions are obtained. The geometrical and physical properties of a class of solutions are discussed.     

The magnetic domain structure of gadolinium between 230 and 293 K

The magnetic domain structure of gadolinium has been studied over the temperature range 230 K to 293 K. This temperature range includes the two magnetic phase transitions that exist in gadolinium, that at the Curie temperature, 291 K, and the change in the easy direction of magnetization at 240 K. A clear uniaxial type domain structure was observed to form as the temperature was lowered through the Curie temperature. This structure was found to disappear as the temperature approached 230 K and no further structure was observed at temperatures below 230 K. Calculations of wall parameters using a numerical integration technique indicate that a stable domain structure should be present and the reasons for the non-appearance of a low temperature domain structure in the present work are not clear.