Search PubMed⌕ Search

Biomedical subjects

M Raspanti

Publications and source records attributed to M Raspanti.

At least 19 recordsLinked to original sources
PubMed2003

Detachment of titanium and fluorohydroxyapatite particles in unloaded endosseous implants.

The shape, surface composition and morphology of orthopaedic and endosseous dental titanium implants are key factors to achieve post-surgical and long-term mechanical stability and enhance implant osteointegration. In this study a comparison was made between 12 titanium screws, plasma-spray-coated with titanium powders (TPS), and 12 screws with an additional coating of fluorohydroxyapatite (FHA-Ti). Screws were implanted in the femoral and tibial diaphyses of two mongrel sheep and removed with peri-implant tissues 12 weeks after surgery. The vibrational spectroscopic, ultrastructural and morphological analyses showed good osteointegration for both types of implants in host cortical bone. The portion of the FHA-Ti implants in contact with the medullary canal showed a wider area of newly formed peri-implant bone than that of the TPS implants. Morphological and EDAX analyses demonstrated the presence of small titanium debris in the bone medullary spaces near the TPS surface, presumably due to the friction between the host bone and the implant during insertion. Few traces of titanium were detected around FHA-Ti implants, even if smaller FHA debris were present. The present findings suggest that the FHA coating may act as a barrier against the detachment of titanium debris stored in the medullary spaces near the implant surface.

Animals↗
PubMed2002

Electromagnetic stimulation on the bone growth using backscattered electron imaging.

The events at the hydroxyapatite implant material/tissue interface following electromagnetic stimulation were studied in the rabbit. Two kinds of hydroxyapatite were used: natural (NA) and synthetic (HA) both with a grain size of <50 microm. Bone defects, artificially created in rabbit tibiae, were filled with the material examined. One group of animals was exposed immediately after surgery and every 12h thereafter to 30-min treatments with electromagnetic fields (PEMFs). A second group was used as a control (untreated). Two and 4 weeks after implantation, animals were sacrificed and bone samples processed for LM, TEM and SEM using a backscatter electron detector for the evaluation of bone growth. This study indicates that HA has more osteoconductivity than NA, and shows that PEMF-treatment results in a benefit in accelerating bone formation at early time periods.

Animals↗
PubMed2002

Hierarchical structures in fibrillar collagens.

The collagen family includes several large transcripts, usually exceeding 1000 amino acid residues per single chain. As a group, they make up 1/3 of all the protein of the body and are responsible for modelling the framework of connective tissues; individually, they show both a wide variety and a complex hierarchy of mutual interactions, and form a range of functional aggregates including a variety of fibrils, microfibrils and basal membranes. Of the collagens, the fibril-forming types (i.e. the types I, II III, V and XI) are the most abundant and the most extensively studied. At the primary structure level, the amino acid sequence of all collagens is now known in detail and it shows a distinctive domain organization, its composition being dominated by the amino acid glycine (roughly 1/3 of all residues) and by post-translational hydroxylation of proline and lysine residues. Collagen secondary and tertiary structure, which together give origin to a classic triple helix, were painstakingly determined in the 1950s and 1960s. In contrast with the primary, secondary and tertiary structure, the supramolecular arrangement within collagen fibres seems to be far more elusive, and none of the models so far advanced can be said to be universally accepted. Half a century of research and debate spawned numerous mutually incompatible models, most of them focussing either on a quasi-crystalline supramolecular array or on several forms of microfibrillar aggregates, while radial fibrils, epitaxial fibrils and other structural models have almost been ignored. In many cases, data gained with a single technique from a single tissue were arbitrarily given a general legitimacy, whilst other well-documented morphological evidence went virtually unnoticed by the scientific community.Moreover, in recent years there has been a growing interest in the multiple interactions of collagens with the other macromolecules of the extra-cellular matrix, as their structure and their functional role become known. It is now indisputable that collagen interacts and forms functional entities with several other macromolecules of the extracellual matrix. This paper will succinctly review some current concepts on the structural biology of collagen higher-order structures.

Animals↗
PubMed2001

Contemporaneous anatomic collections and scientific papers from the 19th century school of anatomy of Bologna: preliminary report.

Recently, a strict relationship was demonstrated between scientific pathology reports of the 19th century and a large number of specimens from the museum of pathology 'Cesare Taruffi' of Bologna. Such an experience suggested verifying whether a similar relationship exists between the 19th-century collections of the museum of anatomy and the contemporaneous anatomic scientific literature. The purpose of this preliminary report is to illustrate the first documented samples recovered in Bologna in order to promote such an inventory of old anatomic and pathologic specimens in other museums.

Anatomy↗
PubMed2001

Tapping-mode atomic force microscopy in fluid of hydrated extracellular matrix.

Fragments of native, hydrated rat tail tendon were imaged by tapping-mode atomic force microscopy while immersed in fluid. The specimens were soft and sensitive to the operating parameters, and with minimal imaging pressure the collagen fibrils appeared covered by irregular blobs or by filamentous material. A slight increase in pressure caused the underlying fibril surface to appear, with an evident D-period, gap- and overlap-zones and three intraperiod ridges. Fibrils often ran parallel and in phase, implying some coupling mechanism. Longitudinal subfibrils, 8-9 nm thick, occasionally appeared. The simultaneous acquisition of the "tapping amplitude" along with the usual "height" channel clearly confirmed the presence of longitudinal subfibrils, indicative of the inner architecture of the fibril.

Animals↗
PubMed2001

Collagen structure and functional implications.

The bio-mechanical requirements to which the connective tissue is subjected suggest that a causal correlation exist between the substructure and the collagen fibril function. We discuss the relationship between the inner structure of collagen fibrils, their diameter, their spatial layout and the functional requirements they have to withstand, and suggest that collagen fibrils may belong to two different forms indicated as "T-type" and "C-type". The first class, consisting of large, heterogeneous fibrils, parallely tightly packed, subjected to tensile stress along their axis is found in highly tensile structures such as tendons, ligaments and bone. The other class, consisting of small, homogeneous fibrils, helically arranged, resisting multidirectional stresses, is mostly present within highly compliant tissues such as blood vessel walls, skin and nerve sheaths. What causes these architectures to appear is discussed in detail in this review.

Animals↗
PubMed2000

A histological and electron-microscopic study of the architecture and ultrastructure of human periodontal tissues.

The structure of periodontal tissues is still far less understood than their clinical relevance would demand. Here the periodontal ligament and radicular cementum in healthy human teeth were studied by light microscopy, transmission and scanning electron microscopy. These observations showed that the extracellular matrix of periodontal ligament is composed of a loose plexus of wavy collagen fibrils immersed in a highly hydrated interfibrillar matrix. Only close to their cemental insertion do these fibrils gather in thick, parallel fascicles (Sharpey's fibres). As these cross the mineralization front, they become infiltrated by the mineral phase and continue directly with the cementum matrix. Sharpey's fibres, "extrinsic" and "intrinsic" fibres all appear to be the same fibres, which bend and branch repeatedly during their course within the thickness of the cementum. Because of its physical continuity with the cementum, a limited portion of the periodontal ligament approximately corresponding to the length of Sharpey's fibres remains unaffected by enzymatic digestion of the interfibrillar matrix while the rest of the ligament is completely dissolved. The findings here indicate that the periodontal ligament and dental cementum join by a continuity rather than a contiguity of structures; that the collagen-mineral relation in cementum has distinctive features in comparison to other hard tissues; that extrinsic and intrinsic fibres of cementum and the adjoining portion of periodontal ligament form a structural, mechanical and metabolic unit distinct from the central, more metabolically active portion of the periodontal ligament.

Collagen↗
PubMed2000

Different patterns of collagen-proteoglycan interaction: a scanning electron microscopy and atomic force microscopy study.

The extracellular matrix of unfixed, unstained rat corneal stroma, visualized with high-resolution scanning electron microscopy and atomic force microscopy after minimal preliminary treatment, appears composed of straight, parallel, uniform collagen fibrils regularly spaced by a three-dimensional, irregular network of thin, delicate proteoglycan filaments. Rat tail tendon, observed under identical conditions, appears instead made of heterogeneous, closely packed fibrils interwoven with orthogonal proteoglycan filaments. Pre-treatment with cupromeronic blue just thickens the filaments without affecting their spatial layout. Digestion with chondroitinase ABC rids the tendon matrix of all its interconnecting filaments while the corneal stroma architecture remains virtually unaffected, its fibrils always being separated by an evident interfibrillar spacing which is never observed in tendon. Our observations indicate that matrix proteoglycans are responsible for both the highly regular interfibrillar spacing which is distinctive of corneal stroma, and the strong interfibrillar binding observed in tendon. These opposite interaction patterns appear to be distinctive of different proteoglycan species. The molecular details of proteoglycan interactions are still incompletely understood and are the subject of ongoing research.

Animals↗
PubMed1999

Structural and functional macrophages alterations by ceramics of different composition.

Biomaterials may initiate several and complex biological reactions in host tissues, and the cell-biomaterial interactions can determine the release of mediators including monocytes and lymphocytes chemotactic factors. The present work was aimed to investigate in vitro the macrophage biological reactions of a natural apatite obtained by heat treatment at 400 degrees C of bovine bone, compared to other ceramics usually used for dental and orthopedic applications, using synthetic apatite and three types of alumina as controls. Particles chemotactic activity and powders oxidative burst evidenced no monocyte macrophages sensitivity reaction for natural and synthetic hydroxyapatite powders at great granulometry (> 50 microm); data were confirmed by ultrastructural observations; electron microscopy analysis showed macrophages with the features of healthy cells in the presence of both natural and synthetic apatites while macrophages grown in the presence of alumina seemed to be negatively affected. In conclusion, among all ceramics tested, natural apatite displayed a good compatibility with living cells, being better tolerated than synthetic hydroxyapatite which in turn is better tolerated than alumina.

Aluminum Oxide↗
PubMed1999

How to defuse compliance time bombs. Part 2: Six hypothetical allegations. Panel discussion.

In the second and final part of this series, a panel of legal experts discusses more hypothetical allegations against a fictional laboratory, including billing for additional indices, using expired reagents, and falsifying the results of employee competency tests. Learn how to handle these dilemmas before they explode into full-blown legal violations.

Clinical Laboratory Techniques↗
PubMed1997

Direct visualization of collagen-bound proteoglycans by tapping-mode atomic force microscopy.

Most studies on the interaction of collagen with proteoglycans, two universal components of connective tissues, use technical approaches which substantially modify the shape and size of the proteoglycans themselves. In the present study unfixed, untreated collagen fibrils from rat tail tendon were dehydrated and observed by tapping-mode atomic force microscopy. The surface of collagen fibrils immediately reveals a periodic alternation of gap and overlap zones. A thin, transverse ridge decorates the gap zone, while other filamentous structures run on the fibril surface, either parallel or perpendicular to the fibril axis. These surface structures are much enhanced by Cupromeronic Blue preincubation, while pretreatment with chondroitinase ABC removes them completely, leaving barely detectable transverse ridges. The ridge and filaments are likely to represent, respectively, the core protein and the glycosaminoglycan side chains of proteoglycans, displayed with a far better resolution than with conventional histochemical or immunohistochemical techniques. Our data suggest that proteoglycan molecules are capable of different, multiple interactions with the collagen fibril surface as well as with each other.

Animals↗
PubMed1996

Collagen fibril surface: TMAFM, FEG-SEM and freeze-etching observations.

Native, unfixed collagen fibrils from rat tail tendon were dehydrated following different procedures and observed under a FEG-SEM and an AFM operated in Tapping Mode (TMAFM). Freeze-etched, untreated fibrils from the same tissue were also observed for comparison. The most notable features of the fibril surface, i.e., the gap/overlap alternation and three prominent intraperiod ridges, were simultaneously visible only in freeze-etched specimens, while under the SEM and the TMAFM their appearance was dependent on both the dehydration procedure and the visualization technique. The different susceptibility of the collagen fibril surface structures to various treatments clearly implies the existence of domains of different composition. Moreover, identical specimens were imaged differently by SEM and TMAFM, highlighting instrument-specific advantages and limitations. The onset of dehydration-dependent, procedure-specific artifacts should be considered in high-resolution studies of connective tissues. As for any biological specimen, the final aspect of collagen fibrils is determined no less by the preliminary treatments than by the visualization approach.

Animals↗
PubMed1996

Collagen fibril patterns in compact bone: preliminary ultrastructural observations.

A comparative study of the Haversian architecture was carried out on compact bone derived from the anterior and posterior edges of the diaphysis of horse radius, regions which have different mechanical requirements in vivo. Samples were heat-deproteinated prior to SEM analysis, a treatment which effectively removes cells and vascular structures as well as exposing large areas of the mineralization front along the walls of the haversian canals. Bone subject to tensile stress revealed a prevalent alignment of its collagen fibrils in the stress direction, and the vast majority of its osteons were composed of fibrils running almost parallel and crossing at very acute angles. Bone subject to compressive forces showed either an orthogonal alternation of collagen lamellae or a multidirectional arrangement corresponding to the twisted plywood pattern described by other authors. Our observations substantiate both the classical model of the osteon and the twisted plywood concept, and suggest that osteon ultrastructure is modulated according to biomechanical requirements.

Animals↗
PubMed1995

Low-temperature heat-deproteinated compact bone to heal large bone defects.

The potential of low-temperature (400 degrees C), heat-treated bone matrix in osteorepair has been evaluated in vivo by implantation into defects artificially created in rodent tibia. Histological and ultrastructural analysis of the bone--implant interface has been carried out on samples obtained at 1 to 6 weeks from operation. The obtained data showed that calcined bone is well tolerated and does not cause acute or chronic inflammatory reactions. Osteoid tissue, tightly adhered to the implant, appears within 2 weeks of the operation, while after 6 weeks newly formed bone surrounds and infiltrates the implant. Of greater note, the detection of good adhesion between bone and implant ultrastructurally is demonstrated by the absence of fibrillar connective tissue at the interface. For these reasons, our preliminary observations suggest that low-temperature calcined bone (biological apatite or heat-deproteinated bone) may have a rightful place among the osteointegrators.

Animals↗
PubMed1995

Different fibrillar architectures coexisting in Haversian bone.

Samples of compact bone were deproteinated by heat treatment and analysed by SEM. This technique removes very effectively cells and vascular structures and brings into full view the mineralization front along the wall of the Havers canal. The present study was confined to samples of equine bone that are known to be subjected to different functional requirements. Bone subjected to high tensile stress exhibited collagen fibrils substantially aligned with the stress direction, and the vast majority of its osteons appeared made of almost parallel fibrils crossing at very narrow angles. On the contrary, bone subjected to prevalent compressive forces showed either an orthogonal alternation of collagen lamellae, or a multidirectional arrangement corresponding to the twisted plywood described by other authors. Our observations substantiate the classical concept of the osteon structure as well as the twisted plywood; they indicate that several osteon architectures coexist in the same specimen, and that the different structures have a different preferential distribution in different parts of the same bone; and suggest that the relative distribution of the osteon ultrastructure across the bone matrix is modulated by mechanical factors.

Animals↗
PubMed1994

Ultrastructure of heat-deproteinated compact bone.

Heat-deproteinated bone (calcined bone) is a natural candidate for an osteoreproductive biomaterial. Ultrastructural investigation has pointed out an important aspect of the preparation technique. Treatment of bone at temperatures exceeding 500 degrees C causes complete disruption of the tissue architecture and the reorganization of the mineral phase into tightly packed, dense crystals. At 500 degrees C or less the structure and distribution of the mineral phase remain unaffected, so that cross-banded 'shadows' of collagen fibrils are still readily observable, although collagen is no longer present in the samples. By its excellent structural preservation and natural porosity, low-temperature calcined bone seems to be a promising alternative for osteoreproduction.

Animals↗
PubMed1994

Correlations between amino acid hydrophobicity scales and stain exclusion capacity of type 1 collagen fibrils.

The relationship between the negative staining band pattern of type 1 native collagen fibrils and the amino acid distribution along the fibril axis was studied by comparing averaged microdensitograms with theoretical traces calculated on the basis of different amino acid parameters. As well as the spatial parameter "bulkiness" (volume/length, ratio), various literature-reported scales of "hydrophobicity" were tested. Two "hydrophobicity" sets allowed a better fit with the actual patterns than "bulkiness" values. However, a general improvement in simulations was achieved by associating most "hydrophobicity" sets with the "bulkiness" set. These results suggest that amino acid "hydrophobicity" plays a key role in the appearance of negative staining patterns but a composite mechanism would seem to occur: the accessibility of available intermolecular interstices may be conditioned by molecular hindrance, corresponding to amino acid "bulkiness" as well as by water-repulsion effect, which correlates with amino acid "hydrophobicity." Moreover, a detailed comparison of actual and simulated patterns suggests that a modulation exists in the effectiveness of these two factors along each D-period according to the different molecular packing and concentration of hydrophobic amino acid clusters within overlap regions and gap regions, respectively.

Amino Acids↗