Biomedical subjects

N Roveri

Publications and source records attributed to N Roveri.

At least 37 records · Page 2Linked to original sources

PubMed1997

Chemical and structural characterization of the mineral phase from cortical and trabecular bone.

X-ray diffraction, infrared spectroscopy and chemical investigations have been carried out on the inorganic phases from rat cortical and trabecular bone. Although both inorganic phases consist of poorly crystalline B carbonated apatite, several significant differences have been observed. In particular, trabecular bone apatite displays reduced crystallite sizes, Ca/P molar ratio, and carbonate content, and exhibits a greater extent of thermal conversion into beta-tricalcium phosphate than cortical bone apatite. These differences can be related to the different extents of collagen posttranslational modifications exhibited by the two types of bone, in agreement with their different biological functions.

Animals↗

PubMed1996

X-ray diffraction study of in vitro calcification of tendon collagen.

Decalcified samples of turkey leg tendon were submitted to in vitro calcification in the presence of metastable solutions of calcium phosphate at different concentrations. The structural relationship between apatitic deposits and collagen fibrils was examined by high- and small-angle X-ray diffraction using conventional and synchrotron radiation sources. At high supersaturation the apatitic crystallites were deposited on the collagen fibrils with their crystallographic c-axis preferentially oriented parallel to the fibril axis. At lower supersaturation, a fraction of the apatitic crystallites also grew with the c-axis preferentially oriented parallel to the collagen fibril axis, whereas other exhibited a preferential orientation perpendicular to the fibril axis. The analysis of the small-angle X-ray diffraction data indicates that the deposition of the apatitic phase in the sample stored in solution at lower supersaturation induced modifications of the collagen electron density distribution in the axial direction, which can be attributed to the deposition of the inorganic crystallites inside the gap region of the collagen structure.

Animals↗

PubMed1995

Ultrastructural and biochemical modifications of collagen from tissue of Morbus Dupuytren patients.

Small angle X-ray diffraction and biochemical analyses were carried out on normal palmar aponeurosis and on tissue from patients suffering from Dupuytren contractures (MD). Pathological tissue exhibits a higher overall content of collagen III. Type I collagen extracted from pathological tissue has a melting point of 0.8 degrees C higher than that of normal collagen. The only chemical differences compared to normal collagen I are 50% overhydroxylation of lysyl residues and a reduced amount of diglycosylated hydroxylysine residues. Analysis of the electron density distribution inside the collagen repeating period of MD-samples reveals disordered molecular packing in MD samples compared to in normal collagen. The disorder, which is higher in the gap region, is considerably reduced upon stretching.

Carbohydrate Sequence↗

PubMed1992

The role of magnesium on the structure of biological apatites.

X-ray diffraction, infrared absorption spectroscopy, and chemical investigation have been carried out on deproteinated samples of turkey leg tendon at different degrees of calcification. The inorganic phase consists of poorly crystalline B carbonated apatite. On increasing calcification, the apatite crystal size, as well as its thermal stability, increase while the relative magnesium content is reduced. On the other hand, synchrotron X-ray diffraction data clearly indicate that apatite lattice parameters do not change as the crystals get larger. At the last stage of calcification the crystal size, chemical composition, and thermal conversion of the apatite crystallites approximate those of bone samples, which have been examined for comparison. The results provide a quantitative relationship between relative magnesium content and extent of apatite conversion into B-tricalcium phosphate by heat treatment. Furthermore, they suggest that the smaller crystallites laid down inside the gap region of the collagen fibrils are richer in magnesium than the longer ones that fill the space between collagen fibrils.

Animals↗

PubMed1991

Structural analysis of turkey tendon collagen upon removal of the inorganic phase.

Calcified leg flexor tendons in which the inorganic phase content had been lowered by progressive demineralization were studied by small angle X-ray diffraction and thermogravimetry. The X-ray diffraction results agree very well with the data previously obtained on calcified turkey tendon indicating that the method used to decalcify tendons provides good correspondence with the process of calcification. Up to five thermal processes can be detected in the thermogravimetric scans: (1) water release; (2) collagen decomposition; (3 and 4) combustion of the residual organic components; (5) carbonate removal from the apatitic phase. The temperature of collagen decomposition decreases at lower inorganic phase content in agreement with the higher thermal stability of calcified collagen fibrils compared with uncalcified ones. The decrease of collagen thermal stability upon decalification is paralleled by a decrease of the structural order of the collagen fibrils as indicated by small angle X-ray diffraction data. Decalcification down to about 40% wt of inorganic phase does not significantly alter the inorganic blocks that are regularly arranged inside the gap zone of the collagen. Further removal of inorganic phase down to about 15% wt provokes a variation of the intensity distribution of the small angle meridional reflections that can be ascribed to a reduction of the mean height of the inorganic blocks. At inorganic phase contents below 15% wt the gap region is more free to contract upon air drying as a result of the reduction of the mean length of the inorganic blocks.

Animals↗

PubMed1991

Collagen structural organization in uncalcified and calcified human anterior longitudinal ligament.

Collagen structure and collagen-apatite structural relationship has been investigated in human anterior ligament, where the mineral deposition occurs on collagen fibrils morphologically different from those of bone and tendons. Ultrastructural observations made on replicas of cryoprotected and freeze fractured uncalcified samples display a "helicoidal" morphology of the collagen fibrils. X-ray diffraction analysis carried out using conventional and synchrotron radiation sources revealed that the D-axial spacing is 65.0 nm and the electron density distribution inside the repeating period is very similar to those of tendon collagen in the same conditions of hydration. The short D-period can be interpreted as due to a greater angle of molecular crimping and/or molecular tilt compared to that of tendon. Air drying does not cause any appreciable variation in the D-axial period and induces an increase of the gap/overlap ratio that can be ascribed to telopeptide disorder. In spite of the different morphology of the collagen fibrils, the structural relationship between collagen and the mineral phase in calcified ligament is very close to that observed in bone and tendons. The apatitic phase is laid down in blocks along the collagen fibrils with the same axial periodicity, D = 65.0 nm, as that of uncalcified collagen fibrils. The mean height of the mineral blocks, which are 0.45D long, is even higher than in bone and masks any further fluctuation of the electron density due to the organic matrix.

Calcinosis↗

PubMed1990

Thermal conversion of octacalcium phosphate into hydroxyapatite.

The thermal conversion of octacalcium phosphate into hydroxyapatite has been investigated by a crystallographic, thermogravimetric, and calorimetric study. The conversion of octacalcium phosphate takes place through the remotion of three of its five water molecules and yields a poor crystalline apatitic phase. The three water molecules are lost in two steps. The first one, which is reversible, corresponds to the remotion of one water molecule and induces a slight contraction of the unit cell of OCP. The successive remotion of two water molecules, which provokes the structural conversion of OCP into apatite, is in irreversible process. The mechanism of the water loss of OCP is explained in terms of its crystal structure.

Calcium Phosphates↗

PubMed1988

Structural and chemical characterization of gallstones resistant to dissolution therapy.

X-ray diffraction, i.r. spectroscopic, and chemical analyses have been carried out on radiolucent gallstones resistant to dissolution therapy. Cholesterol represents the main component of all the examined stones, while the ratio between the amounts of pigmented material and calcium carbonate is about 1 in the inner and outer layers of the stones and 3 in the medial layer. Calcium carbonate is present in two distinct crystalline forms: vaterite, which is the main inorganic crystalline phase, and calcite. The cell parameters of vaterite and calcite are shorter in the inner and outer layers of the stones than in the medial layer. The observed variation of the cell parameters has been related to the substitution of copper to calcium in the carbonate structures, on the basis of the data obtained on vaterite and calcite synthesized in presence of different copper concentrations in solution. The results indicate that the failure of the dissolution therapy can be related to the inhomogeneous distribution in the stones of calcium carbonate and calcium bilirubinate.

Calcium↗

PubMed1988

Structural and chemical characterization of inorganic deposits in calcified human mitral valve.

X-ray diffraction, i.r. absorption, and chemical analyses have been carried out on the mineral deposits of calcified human mitral valves and glutaraldehyde-preserved porcine aortic grafts. The mineral deposits isolated from highly calcified mitral valves and porcine aortic grafts are constituted of type B-carbonate apatite. Magnesium substituted beta-tricalcium phosphate is present, together with an apatitic phase similar to dahllite, in the ashes of poorly calcified mitral valves. The contraction of the unit cell of beta-tricalcium phosphate due to magnesium incorporation is compared with the variation of the lattice constants of synthetic beta-tricalcium phosphate at different degree of magnesium substitution for calcium. The results reveal the important role of magnesium on the calcification of human valves. In fact, the apatitic phase deposited at the beginning of the calcification process, when there is a high magnesium content, converts completely into beta-tricalcium phosphate by heat treatment at 1,000 degrees C. On the other hand, when the calcification becomes massive, magnesium content appears highly reduced, and the deposited apatitic phase is characterized by a high thermal stability.

Calcinosis↗

PubMed1986

Differences in the fibril structure of corneal and tendon collagen. An electron microscopy and X-ray diffraction investigation.

A detailed analysis of the D-period and axial electron density distribution of cornea and tendon collagen was carried out by means of X-ray diffraction and electron microscopy. Ultrastructural observations were made on replicas of freeze fractured and deep-etched specimens. Synchrotron radiation was used to obtain high resolution small angle X-ray diffraction patterns. The data provide evidence that D-period and intraperiod distances in cornea are shorter than in tendon collagen fibrils. The observed different banding observed is interpreted on the basis of the different morphological arrangement of the microfibrils in the two tissues: "helicoidal" in cornea and "straight" in tendon microfibrils.

Animals↗

PubMed1985

A low-angle X-ray diffraction analysis of osteonic inorganic phase using synchrotron radiation.

Using synchrotron radiation the low-angle X-ray diffraction method has been applied to single osteon samples to yield new data on the texture of the inorganic bone fraction. Two sample types--cylindrically shaped osteonic samples and osteonic radial hemisections--were prepared from longitudinal and alternate osteons at both the initial and final stages of calcification. The results indicate that the diffraction pattern is due to the inorganic phase, which reveals the same axial periodicity as native collagen fibrils and fits into the main band. No change is appreciable as osteons pass from the initial to the final stage of calcification. This means that when crystallites covering much more than a collagen axial period are observed under the electron microscope, they do not appreciably affect the calcified banding of collagen fibrils. The osteonic axis corresponds to the main direction of collagen orientation both in longitudinal and alternate osteons. The degree of orientation, however, is lower in alternate osteons than in longitudinal ones, where only few thin, incomplete transversal lamellae are found.

Adult↗

PubMed1984

Thermal behavior of bone and synthetic hydroxyapatites submitted to magnesium interaction in aqueous medium.

The thermal behavior of the products obtained from magnesium interaction with powdered femoral bone and carbonate containing synthetic hydroxyapatite under conditions of pH fluctuation in aqueous medium has been investigated. The products, heat treated at different temperatures from 100 to 1300 degrees C, have been characterized by infrared spectroscopy and X-ray diffraction technique. The results show that the interaction with magnesium ion destabilizes the apatitic structure and favours its thermal conversion into beta-tricalcium phosphate (beta-TCP). The replacement of magnesium with calcium in the beta-TCP crystal lattice hinders its subsequent thermal conversion into the alpha form. The influence of magnesium on the thermal stability is much more evident for carbonate-containing synthetic hydroxyapatite than for bone apatite.

Animals↗

PubMed1983

Arrangement of microfibrils in collagen fibrils of tendons in the rat tail. Ultrastructural and x-ray diffraction investigation.

The microfibrillar arrangement in collagen fibrils of tendons in the tail of the rat was examined by electron microscopy and X-ray diffraction. Fresh and air-dried collagen fibers were examined in unstretched and stretched conditions. The results demonstrate that the microfibrils have a course parallel to the longitudinal axis of the collagen fibrils. The influence of stretching and hydration of the samples on the orientation of fibrils and microfibrils is also assessed.

Animals↗

PubMed1983

X-ray diffraction analysis of transversal osteonic lamellae.

When isolated osteon samples are submitted to wide-angle X-ray diffraction, it is not possible to detect any preferential orientation of the hydroxyapatite crystallites of the lamellae with transversally arranged fiber bundles. So a complete and exhaustive X-ray diffraction analysis of an osteon needs adequately prepared osteonic subunits. For the present investigation, 2 types of samples were prepared from longitudinal and alternate osteons: osteonic radial sections and isolated straightened transversal lamellae. An X-ray diffraction microcamera has been used with a rotating anode X-ray generator. In accordance with the data provided by the polarizing microscope, the orientation of crystallites runs parallel to the osteon axis in longitudinally structured osteons, whereas in alternate osteons the orientation changes by about 90 degrees in successive lamellae. Neither crystallites associated with the collagen fibrils that run alongside the osteocyte canaliculi nor those associated with the fibrils that run transversally in longitudinally structured osteons are revealed by X-ray diffraction, because there are so few of them.

Crystallization↗

PubMed1983

Light microscopy, electron microscopy, and X-ray diffraction analysis of glycerinated collagen fibers.

Light microscopy, transmission electron microscopy (freeze-fracture replicas and thin sections), and X-ray diffraction techniques were used to investigate the structure of rat tail tendon collagen fibers subjected to one of the following treatments: water, phosphate buffer, glutaraldehyde, glutaraldehyde followed by glycerol, glycerol, and glycerol followed by phosphate buffer. As seen by light microscopy, only treatment with glycerol induces a remarkable swelling of the native (untreated) collagen specimens. Replicas and thin sections show that this swelling is due to an expansion of the interfibrillar space, and to a dissociation of the collagen fibrils into microfibrils. X-Ray diffraction analysis reveals great disorder in the glycerol-swollen collagen fibers. However, this does not appreciably involve the microfibrillar and molecular structure. Light and electron microscopy as well as X-ray diffraction techniques show that the collagen fiber swelling induced by glycerol is an almost completely reversible process.

Animals↗

PubMed1982

Carotid wall as an isotropic mechanical system.

The morphological organization of the structural components in the dog carotid wall is investigated by X-ray diffraction and microscopic analysis. Histological analysis confirms an anisotropic morphology of smooth muscle cells and elastic fibers in the tissue. Collagen fibers, as revealed by X-ray diffraction technique, are organized in an isotropic network in the unstretched carotid media. Collagen fibers stretch without a preferential direction of orientation when a carotid segment is deformed in the physiological range under intraluminal pressure. A mathematical model which takes into account the isotropic distribution of the collagen fibers is developed. The validity of this model has been tested by computing several mechanical parameters using Anliker's data on the axial and radial oscillation obtained for carotids of living dogs. In spite of the anisotropic morphology of the main constituents of the carotid media layer, from a mechanical point of view the tissue can be considered as an isotropic material for the random distribution of the collagen fibers which represent the component of higher tensile strength.

Animals↗

PubMed1980

[X-ray diffraction analysis of collagen fibers processed with glutaraldehyde and glycerol].

Rat tail tendon collagen fixed with glutaraldehyde and treated with glycerol has been studied by X-ray diffraction technique. The evaluation of the distribution of the areas at higher and less density of molecular packing in the collagen fibrils has been carried out through the analysis of the intensity distribution of the low angle X-ray diffraction maxima. The results show that this treatment usually employed in the freeze-etching technique induces a modification of the degree of order in specific regions inside the axial period D.

Aldehydes↗

PubMed1980

[Study of rat tail tendon by x-ray diffraction and freeze-etching technics].

Rat tail tendon collagen processed according to different fixation and cryoprotection treatments has been examined by small angle X-ray diffraction and freeze-etching techniques. The results show some differences in the axial period and in the degree of disorder of the molecular packing as a function of the applied treatment.

Animals↗