PubMed Health⌕ Search

Biomedical subjects

N Roveri

Publications and source records attributed to N Roveri.

15 recordsLinked to original sources
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↗
PubMed1979

X-ray diffraction study of bovine lens capsule collagen.

The wide angle X-ray diffraction pattern of air-dried lens capsule collagen under tension is the same as the tendon collagen diffraction pattern with regard to the main reflections, and indicates that lens capsule collagen has the characteristic three-stranded helical structure with an axial repeat of 0.29 nm as tendon collagen. The low angle X-ray diffraction pattern shows several weak diffraction maxima corresponding to the meridional reflections of capsule collagen which show orders of 63.0 nm periodicity. This is an evidence of quarter staggered molecular assembly typical of tendon collagen even if less ordered. The results are consistent with the existence in lens capsule collagen of clearly defined molecular units, which can be oriented by stress and are packed in a poor-ordered fibrillar assembly.

Animals↗
PubMed1978

X-ray diffraction and electron microscope study of osteons during calcification.

To obtain information on the changes in the inorganic bone fraction during calcification, low- and wide-angle X-ray diffraction techniques and electron microscopy have been applied to single osteon samples. The samples were cylindrically shaped and their axes corresponded to the axes of the Haversian canals. The selection was made according to the degree of calcification and the orientation of collagen bundles and inorganic particles. Osteons at both the initial and final stages of calcification were chosen. Arrangements of fiber bundles and inorganic particles in successive lamellae characteristic of three types of osteon were selected, that is, longitudinally structured osteons, transversely structured osteons, and alternately structured osteons. The results indicate that in osteonic lamellar bone there are two types of inorganic particles: (1) granules arranged in linear or needle-shapred entities with maximum width 40-45 A, which are regularly distributed at the level of the main band of the collagen fibrils where their maximum length reaches the length of the main band itself; that is , about 400 A; and (2) very long crystallites, with a diameter of 40-45 A, which grow with their crystallographic c-axis parallel to the collagen fibrils and cover much more than a major collagen period.

Adolescent↗
PubMed1978

Structural organization of collagen fibrils in media aortic wall.

Small-angle X-ray diffraction patterns of bovine, human and porcine media aortic wall show meridional reflections corresponding to a periodicity which suggest a molecular packing typical of tendon collagen. However the meridional intensity distribution of stretched air dried aortic samples appears different from that of air-dried tendon, probably because of the presence of a large amount of type III collagen with the environment, which are specific for aortic tissue. The stretched wet aortic samples show a marked decrease in intensity, revealing an extensive disorder in the axially-projected structure of the fibrils. When a loading system simulating the effect of blood pressure is applied to a ring of aorta, no evidence of orientation of collagen is seen by X-ray diffraction, as would be expected if collagen fibrils had an isotropic distribution inside the aorta media. Scanning electroni microscopy supports the existence of a network of collagen fibrils surrounding elastic lamellae.

Adult↗
PubMed1977

X-ray diffraction and scanning electron microscopy of bovine media aortic wall.

Scanning electron microscopy and high angle X-ray diffraction were used to define the relationship between collagen and elastin of bovine aortic wall. The diffraction pattern shows on one hand that the broad rings at 4.5 A and 9 A, due to elastin, do not orient on stretching and on the other hand, that the collagen rings at 11 A and 2.9 A start to orient at low elongations. These data together with scanning electron microscopy suggest a tight structural relationship between collagen and elastin that should influence the mechanics of deformation at all degrees of elongation.

Animals↗