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Biomedical subjects

F H Silver

Publications and source records attributed to F H Silver.

At least 19 recordsLinked to original sources
PubMed2001

Molecular basis for elastic energy storage in mineralized tendon.

Animals store elastic energy in leg and foot tendons during locomotion. In the turkey, much of the locomotive force generated by the gastrocnemius muscle is stored as elastic energy during tendon deformation. Little energy storage occurs within the muscle. During growth of some avians, including the turkey, leg tendons mineralize in the portions distal to the attached muscle and show increased tensile strength and modulus as a result. The purpose of this study is to test the hypothesis that the degree of elastic energy storage in mineralizing turkey tendon is directly related to the tendon mineral content. To test this hypothesis, the stress-strain behavior of tendons was separated into elastic and viscous components. Both the elastic spring constant and the elastic energy stored, calculated up to a strain of 20%, were found to be proportional to tendon mineral content. It is concluded that mineralization is an efficient means for increasing the amount of elastic energy storage that is required for increased load-bearing ability needed for locomotion of adult birds. Examination of molecular models of the hole region, where mineralization is initiated within the collagen fibril, leads to the hypothesis that elastic energy is stored in the tendon by direct stretching of the flexible regions. Flexible regions within the collagen molecule fall within the positively stained bands of the collagen D period. It is proposed that mineralization increases the stored elastic energy by preventing flexible regions within the positively stained bands from stretching. These observations suggest that mineralization begins in the hole region due to the large number of charged amino acid residues found in the d and e bands.

Animals↗
PubMed2001

Viscoelastic properties of human skin and processed dermis.

BACKGROUND/AIMS: The purpose of this work is to attempt to determine the elastic spring constant for collagen and elastic fibers (elastin) in skin and to determine if the values of these elastic constants are similar to those reported for other tissues. METHODS: We studied the viscoelastic mechanical properties of human skin and dermis by measuring the incremental stress-strain behavior. Elastic stress-strain curves were used to obtain the elastic spring constant of elastin and collagen while the collagen fibril length was obtained from the slope of viscous stress-strain curves. RESULTS: Our results suggest that the elastic spring constant for elastin is about 4.0 MPa while that for collagen is about 4.4 GPa. The former value is similar to that calculated for ligamentum nuchae while the latter value is about 70% of the value found for tendon and self-assembled type I collagen fibers. The differences between the elastic constants for collagen molecules in tendon and skin is hypothesized to reflect the higher molecular tilt angle and lower D period found in skin compared to tendon as well as a shorter fibril length. CONCLUSION: The differences in the collagen types present in skin and tendon may influence collagen self-assembly and the resulting viscoelastic properties.

Aged↗
PubMed2001

Characterization of radial forces in Z stents.

RATIONAL AND OBJECTIVES: The purpose of this study was to evaluate the effects of variation in design parameters on the resultant radial force. We evaluated the influence of wire gauge, leg length, and number of bends on the radial force produced by z stents and compared these with radial forces produced by commercial stents. A second goal was to develop an engineering model for predicting radial forces generated by z stents. METHODS: Z stents were fashioned by hand using stainless steel wire and solder that connected the ends. The radial force was measured as a function of wire gauge, vessel diameter, leg length, and number of bends and compared with the theoretical values of radial force calculated by combining Castigliano's theorem and the law of Laplace. RESULTS: Theoretically predicted radial forces were within 8% of each observed value of radial force up to 70% spring compression. CONCLUSIONS: These results suggest that the z-stent model can be used to build custom stents with preselected values of radial force for clinical use. In addition, they can be used to design model investigational stents made of similar materials and surface areas to test the effects of radial force on biological response.

Biomechanical Phenomena↗
PubMed2001

Viscoelasticity of the vessel wall: the role of collagen and elastic fibers.

The aortic wall contains collagen fibrils, smooth muscle cells, and elastic fibers as the primary load-bearing components. It is well known that the collagen fibrils bear loads in the circumferential direction, whereas elastic fibers provide longitudinal as well as circumferential support. Stiffening of the vessel wall is associated with loss of elastic tissue and increases in the collagen content: however, little is known about the mechanism of vessel wall stiffening with age. The purpose of this review is to attempt to relate structural changes that occur to the collagen and elastic fibers to changes in the viscoelastic behavior that are associated with aging. Analysis of the viscoelastic mechanical properties of collagen fibrils from tendon, skin, and aortic wall suggest that the collagen fibrils of aortic wall are different than those of other tissues. The elastic spring constant of the collacen fibrils in vessel walls is significantly less than that found in tendon, suggesting that the presence of type III collagen in aortic wall increases the flexibility of the collagen fibrils. Furthermore, it is hypothesized that changes in the interface between collagen fibrils, elastic fibers, and smooth muscle during aging and in connective tissue disorders leads to changes in the viscoelasticity of the vessel wall.

Aorta↗
PubMed2001

Relationship among biomechanical, biochemical, and cellular changes associated with osteoarthritis.

Articular cartilage that lines the surface of long bones is a multilayered material. The superficial layer consists of collagen fibrils and chondrocytes that run parallel to the joint surface. In the deeper layers, the collagen fibrils are more randomly arranged and support vertical units termed chondrons containing rows of chondrocytes. In the deepest layers, the collagen fibrils run almost vertically and ultimately insert into the underlying subchondral bone. Osteoarthritis (OA) is a disease that affects articular cartilage and is characterized by enzymatic and mechanical breakdown of the extracellular matrix, leading to cartilage degeneration, exposure of subchondral bone, pain, and limited joint motion. Changes in mechanical properties of articular cartilage associated with OA include decreases in modulus and ultimate tensile strength. These changes parallel the changes observed after enzymatic degradation of either collagen or proteoglycans in cartilage. Results of recent viscoelastic studies on articular cartilage suggest that the elastic modulus of collagen and fibril lengths decrease in OA and are associated with a loss of the superficial zone and a decreased ability of articular cartilage to store elastic energy during locomotion. It is suggested that osteoarthritic changes to cartilage involve enzymatic degradation of matrix components and fibril fragmentation that is promoted by subsequent mechanical loading.

Animals↗
PubMed2001

Viscoelastic behavior of osteoarthritic cartilage.

We have studied the incremental stress-strain behavior of human articular cartilage in tension in an attempt to understand the molecular basis for fibrillation and fissure formation in osteoarthritis. Our results indicate that the elastic spring constant for collagen in the direction per pendicular to the cleavage line pattern is about 1.6 GPa (2.3 GPa after correction for the collagen content) and the collagen fibril length is between 0.558 pm at low strains and 1.24 pm at high strains for normal cartilage. Values for the elastic spring constant and collagen fibril length were both found to decrease in OA. The value of the elastic spring constant for collagen perpendicular to the cleavage line pattern is similar to that calculated based on stress-strain curves reported by Kempson. Our results indicate that the elastic spring constant for collagen and the collagen fibril length decrease as the extent of fibrillation and fissure formation increase. Decreases in the elastic spring constant of collagen are consistent with loss of the superficial layer, degradation of proteoglycans and collagen, and subsequent mechanical fatigue. However, changes in the polymer volume fraction are consistent with enzymatic degradation preceding mechanical disruption. It is concluded that osteoarthritic changes to cartilage involve enzymatic degradation of matrix components and fibril fragmentation that is promoted by subsequent mechanical loading.

Aged↗
PubMed2000

Assembly of type I collagen: fusion of fibril subunits and the influence of fibril diameter on mechanical properties.

Structural stability of the extracellular matrix is primarily a consequence of fibrillar collagen and the extent of cross-linking. The relationship between collagen self-assembly, consequent fibrillar shape and mechanical properties remains unclear. Our laboratory developed a model system for the preparation of self-assembled type I collagen fibers with fibrillar substructure mimicking the hierarchical structures of tendon. The present study evaluates the effects of pH and temperature during self-assembly on fibrillar structure, and relates the structural effects of these treatments on the uniaxial tensile mechanical properties of self-assembled collagen fibers. Results of the analysis of fibril diameter distributions and mechanical properties of the fibers formed under the different incubation conditions indicate that fibril diameters grow via the lateral fusion of discrete approximately 4 nm subunits, and that fibril diameter correlates positively with the low strain modulus. Fibril diameter did not correlate with either the ultimate tensile strength or the high strain elastic modulus, which suggests that lateral aggregation and consequently fibril diameter influences mechanical properties during small strain mechanical deformation. We hypothesize that self-assembly is mediated by the formation of fibrillar subunits that laterally and linearly fuse resulting in fibrillar growth. Lateral fusion appears important in generating resistance to deformation at low strain, while linear fusion leading to longer fibrils appears important in the ultimate mechanical properties at high strain.

Animals↗
PubMed2000

The role of mineral in the storage of elastic energy in turkey tendons.

Mammals elastically store energy in leg and foot tendons during locomotion. In the turkey, much of the force generated by the gastrocnemius muscle is stored as elastic energy during tendon deformation and not within the muscle. During growth, avian tendons mineralize in the portions distal to the muscle and show increased tensile strength and modulus as a result. The purpose of this study was to evaluate the viscoelastic behavior of turkey tendons and self-assembled collagen fiber models to determine the molecular basis for tendon deformation. The stress-strain behavior of tendons and self-assembled collagen fibers was broken into elastic and viscous components. The elastic component was found to be to a first approximation independent of source of the collagen and to depend only on the extent of cross-linking. In the absence of cross-links the elastic component of the stress was found to be negligible for self-assembled type I collagen fibers. In the presence of cross-links the behavior approached that found for mineralized turkey tendons. The elastic constant for turkey tendon was shown to be between 5 and 7.75 GPa while it was about 6.43 GPa for self-assembled collagen fibers aged for 6 months at 22 degrees C. The viscous component for mineralized turkey tendons was about the same as that of self-assembled collagen fibers aged for 6 months, a result suggesting that addition of mineral does not alter the viscous properties of tendon. It is concluded that elastic energy storage in tendons involves direct stretching of the collagen triple-helix, nonhelical ends, and cross-links between the molecules and is unaffected by mineralization. Furthermore, it is hypothesized that mineralization of turkey tendons is an efficient means of preserving elastic energy storage while providing for increased load-bearing ability required for locomotion of adult birds.

Animals↗
PubMed2000

Role of storage on changes in the mechanical properties of tendon and self-assembled collagen fibers.

Fibrous collagen networks are the major elements that provide mechanical integrity to tissues; they are composed of fiber forming collagens in combination with proteoglycans (PGs). Using uniaxial tensile tests we have studied the viscoelastic mechanical properties of rat tail tendon (RTT) fibers and self-assembled collagen fibers that were stored at 22 degrees C and 1 atm of pressure. Our results indicate that storage of RTT and self-assembled type I collagen fibers results in increased elastic and viscous components of the stress-strain behavior consistent with the hypothesis that storage causes the introduction of crosslinks. Analysis of the elastic and viscous mechanical data suggests that the elastic constant of the collagen molecule in RTT is about 7.7 GPa. Measurement of the viscous component of the stress-strain curves for RTTs and self-assembled collagen fibers suggests that PGs may increase the viscous component and effectively increase the collagen fibril length.

Animals↗
PubMed1997

Self-assembly of collagen fibers. Influence of fibrillar alignment and decorin on mechanical properties.

Collagen is the primary structural element in extracellular matrices. In the form of fibers it acts to transmit forces, dissipate energy, and prevent premature mechanical failure in normal tissues. Deformation of collagen fibers involves molecular stretching and slippage, fibrillar slippage, and, ultimately, defibrillation. Our laboratory has developed a process for self-assembly of macroscopic collagen fibers that have structures and mechanical properties similar to rat tail tendon fibers. The purpose of this study is to determine the effects of subfibrillar orientation and decorin incorporation on the mechanical properties of collagen fibers. Self-assembled collagen fibers were stretched 0-50% before cross-linking and then characterized by microscopy and mechanical testing. Results of these studies indicate that fibrillar orientation, packing, and ultimate tensile strength can be increased by stretching. In addition, it is shown that decorin incorporation increases ultimate tensile strength of uncross-linked fibers. Based on the observed results it is hypothesized that decorin facilitates fibrillar slippage during deformation and thereby improves the tensile properties of collagen fibers.

Animals↗
PubMed1995

Performance standards for medical device approvals.

As a result of the controversy concerning the safety of silicone and other permanent implants, the Food and Drug Administration's Center for Drug Evaluation and Research has conducted a rereview of a small sample of applications by manufacturers. The Food and Drug Administration's "Final Report of the Committee for Clinical Review" found that clinical trials were carried out with little planning or attention to the purpose of the study. It is urged that the medical profession assist in the establishment of complication rates associated with each type of implant and surgical procedure and that surgeons and professional societies need to be more critically involved in the setting up of performance standards for implants prior to their approval by the Food and Drug Administration. To avoid a repeat of the silicone gel-filled breast implant problem, scientists and clinicians are urged to take a more proactive position on the development of performance standards for implants currently being used.

Device Approval↗
PubMed1995

Preparation of fibrin glue: a study of chemical and physical methods.

Concentrated fibrinogen was prepared from whole blood by cryoprecipitation or chemical precipitation and combined with thrombin to make fibrin glue (FG). Surgical applications of FG include control of bleeding, adhesion of tissues, and sealing of tissue defects. The purpose of this study was to compare cryoprecipitation (cryo) of fibrinogen to precipitation using ethanol, ammonium sulfate (AS), and poly(ethylene glycol) (PEG). Our results suggest that AS precipitation is as effective as cryo in yielding fibrin glues with high bond strengths and is more effective than ethanol and PEG precipitation. In addition, the volume of FG per milliliter of plasma is greater after AS precipitation than after a single freeze-thaw cycle. It is concluded that AS is an efficient means for preparing FG from autologous blood.

Fibrin Tissue Adhesive↗
PubMed1995

A study of the relationship between mineral content and mechanical properties of turkey gastrocnemius tendon.

The vertebrate skeletal system undergoes adaptation in response to external forces, but the relation between the skeletal changes and such forces is not understood. In this context, the variation in the amount and location of calcification has been compared with changes in mechanical properties of the normally mineralizing turkey gastrocnemius tendon using ash weight measurements, X-ray radiography, and mechanical testing. Radiographic evidence from 12- to 17-week-old birds showed calcification in only portions of gastrocnemius tendons proximal to the tarsometatarsal joint. Mechanical testing of these dissected proximal regions demonstrated an increased ultimate stress and modulus and a decreased maximum strain that appeared to parallel calcification. Further, stress-strain curves of portions of uncalcified turkey gastrocnemius tendon were shaped similar to those of other typical unmineralized tendon curves while highly calcified tendons yielded curves resembling those of bone. The proximal portions of the gastrocnemius where mineralization begins were observed to have a decreased tendon cross-sectional area compared with distal portions which do not mineralize. Based on the resultant measures of mineral content and location and mechanical properties, it is hypothesized that increased calcification is a result of increased stresses at certain locations of the tendon, perhaps the consequence of the natural forces exerted by the large leg muscles of the bird into which the gastrocnemius inserts. More specifically, tendon calcification may be the result of stress-induced exposure of charged sites on the surfaces of collagen molecules, fibrils, or fibers so that deposition of mineral and subsequent mechanical reinforcement occur in the tissue.(ABSTRACT TRUNCATED AT 250 WORDS)

Analysis of Variance↗
PubMed1995

Preparation and use of fibrin glue in surgery.

Fibrin glue (FG) is used to control bleeding, to adhere tissues together, and to seal tissue defects. FG is prepared from platelet-rich plasma or by mixing concentrated fibrinogen solutions with thrombin. Concentrated fibrinogen solutions are produced by cryoprecipitation or by chemical precipitation of plasma. The literature on FG preparation is reviewed in order to compare the advantages and disadvantages of the different products reported and to summarize the clinical applications. It is concluded that additional studies are needed to fully evaluate the advantages and disadvantages of fibrinogen concentrated using cryoprecipitation and chemical precipitation and that specific advantages exist for use of both pooled homologous and autologous blood.

Ammonium Sulfate↗
PubMed1995

Cartilage wound healing. An overview.

Cartilage wound healing is a tentative balance between deposition of type I collagen in the form of scar tissue and repair by expression of type II collagen and proteoglycans. Small full-thickness cartilage defects are replaced by fibrocartilage, whereas partial-thickness defects are normally repaired by deposition of fibrous scar tissue. The mechanism of fibrocartilaginous repair appears to be mediated by proliferation and differentiation of mesenchymal cells of the marrow. Biologic grafts such as perichondrium have been successfully used to repair full-thickness defects, probably because they contain progenitor cells that can differentiate into chondroblasts. Other grafts composed of fibrocartilage, such as meniscus, appear potentially useful because they serve as a source for chondrocytes. When graft material is unavailable or cannot be easily fashioned to fit the defect, cell-cultured materials containing chondrocytes or progenitor cells appear promising. Finally, growth factors such as somatomedin-C have growth-promoting effect on cartilage and offer a future means of promoting cartilage repair.

Cartilage↗
PubMed1994

Physical properties of model viscoelastic materials.

Previous observations on polysaccharides used as viscoelastic agents in ophthalmic surgery suggest that the pseudoplasticity of solutions of hyaluronan (HA) and the low surface tension of hydroxypropylmethylcellulose (HPMC) solutions are physical properties that make these solutions useful clinically. Our laboratories are interested in correlating the physical properties of macromolecular solutions with the ability of these molecules to protect ocular structures during eye surgery. The purpose of this study is to compare the physical properties of model viscoelastics with the properties of HA and HPMC. The results of these studies suggest that polysaccharides that form extended structures in solution at low shear rates and that are characterized by large decreases in the axial ratio at high shear rates, exhibit pseudoplastic behavior. In this study pseudoplasticity is exhibited by polysaccharides with molecular weights in excess of 450 000, and is insensitive to the backbone chemistry for linear macromolecules. In addition, low surface tension is associated with charged macromolecules that have a high positive second virial coefficient.

Aqueous Humor↗
PubMed1994

Collagen fibres with improved strength for the repair of soft tissue injuries.

Our laboratory has developed a process for self-assembly of high strength collagen fibres in vitro which exhibit the characteristic D period. These fibres can be cross-linked by severe dehydration (dehydrothermal cross-linking) at elevated temperature and formulated into devices used to repair soft tissues. This study was conducted to evaluate the effects of dehydrothermal cross-linking time and temperature on the tensile mechanical properties of collagen fibres. The results discussed indicate that the tensile strength of reconstituted collagen fibres is optimized by cross-linking for 5 d at 110 degrees C. Tensile strength and modulus values of 91.8 and 896 MPa are reported for fibres cross-linked in this manner. High tensile strength and modulus values are especially important in developing biodegradable materials that promote healing of orthopaedic structures.

Animals↗