Cattle Tendons Research Articles

Wound Coating Collagen-Based Composites with Ag Nanoparticles: Synthesis, Structure and Biological Activity

The search for materials for a new generation of wound coatings is important due to the increase in antibiotic-resistant microorganisms and the number of patients with untreatable chronic purulent wounds. Metal nanoparticles, specifically silver nanoparticles, have antimicrobial activity and do not induce known bacterial resistance. To obtain new Ag-containing nanocomposites, type I collagen was extracted by an enzyme–acid method from cattle tendons. Silver nanoparticles were obtained by an environmentally safe method, metal-vapor synthesis (MVS), which enables obtaining metal nanoparticles without impurities. For this, metal vapors were cocondensed in a vacuum of 10−2 Pa on the walls of a quartz reactor cooled to 77 K using acetone as an organic dispersion medium. The composition of the collagen surface was determined by XPS using the spectra of C1s, N1s, and O1s. The presence of a peak with a binding energy of approximately 368.57 eV in the Ag 3d5/2 spectrum indicates the state of Ag0 silver atoms in the nanocomposite. SEM images showed that collagen contributes to the effective stabilization of Ag nanoparticles with an average size of 13.0 ± 3.5 nm. It was found that collagen is non-toxic and biocompatible with skin cells and fibroblasts. The collagen–Ag nanoparticle nanocomposites exhibited antimicrobial activity against bacteria Bacillus subtilis, Escherichia coli, and fungi Aspergillus niger.

Travelling through the Natural Hierarchies of Type I Collagen with X-rays: From Tendons of Cattle, Horses, Sheep and Pigs.

Type I collagen physiological scaffold for tissue regeneration is considered one of the widely used biomaterials for tissue engineering and medical applications. It is hierarchically organized: five laterally staggered molecules are packed within fibrils, arranged into fascicles and bundles. The structural organization is correlated to the direction and intensity of the forces which can be loaded onto the tissue. For a tissue-specific regeneration, the required macro- and microstructure of a suitable biomaterial has been largely investigated. Conversely, the function of multiscale structural integrity has been much less explored but is crucial for scaffold design and application. In this work, collagen was extracted from different animal sources with protocols that alter its structure. Collagen of tendon shreds excised from cattle, horse, sheep and pig was structurally investigated by wide- and small-angle X-ray scattering techniques, at both molecular and supramolecular scales, and thermo-mechanically with thermal and load-bearing tests. Tendons were selected because of their resistance to chemical degradation and mechanical stresses. The multiscale structural integrity of tendons' collagen was studied in relation to the animal source, anatomic location and source for collagen extraction.

Effects of Various Processing Methods on the Ultrastructure of Tendon Collagen Fibrils from Qinchuan Beef Cattle Observed with Atomic Force Microscopy

Atomic force microscopy was utilized to study the effects of ultrasound oscillation, microwave heating, water bath cooking, and acid-base soaking on the ultrastructure of collagen fibrils of Qinchuan beef cattle tendons. D-spacing length and roughness of collagen fibrils always showed a 1.02% increment in the group which was processed for 20 min rather than for 10 min under different ultrasound frequencies. Microwave heating had a slight impact on D-spacing length and roughness at lower power (140–560 W), and collagen fibrils always showed a 1.02% increment for 20 min. Then, visible changes were noted with increasing power and time. D-spacing length reduced by 1.01% at 50°C for treatment periods of 10 min, 20 min, and 30 min, and there was no obvious change at 60°C; the periodic structure disappeared after cooking for 20 min, when fibrils had become gelatinized at 70°C. Collagen fibrils became disorganized at pH 3, following acid-base soaking. The present study indicated that acid-base soaking had an outstanding effect on the ultrastructure of collagen fibrils, especially in an acidic environment in consideration of the special structure of collagen.

Differentiation of deer tendons from cattle tendons by a loop-mediated isothermal amplification (LAMP) test and bone remodeling bioassays.

BackgroundDeer tendons are believed more effective than cattle tendons in tonifying kidney yang (shen yang) and enhancing bone and tendons. This study aims to differentiate the two types of tendons by a loop-mediated isothermal amplification (LAMP) test and bone remodeling bioassays.MethodsInternal control primers to detect both types of tendons and specific primers for deer tendons were designed according to a sequence analysis. The LAMP test was set up and the results were analyzed by conventional gel electrophoresis, real-time fluorescence observation, and colorimetric detection. Crude tendon extracts were prepared by water extraction to compare their effects on bone. The anti-osteoclastic effects were investigated on mouse pre-osteoclast Raw264.7 cells by cell viability determination and tartrate-resistant acid phosphatase staining. The osteogenic effects were examined using rat osteoblast-like UMR106 cells by evaluation of cell proliferation, alkaline phosphatase activity, and calcium deposition. The relative gene expressions of bone remodeling-related markers, including nuclear factor of activated T-cells cytoplasmic 1, tartrate-resistant acid phosphatase, cathepsin K, and osteoprotegerin/receptor activator of NF-κB ligand, were determined by real-time PCR.ResultsIn the LAMP test, both deer and cattle tendons were detected in the control reactions, while only deer tendons were amplified by the specific LAMP test. In the bioassays, both tendons inhibited the viability and differentiation of pre-osteoclast Raw264.7 cells, and promoted the proliferation and mineralization of osteoblast-like UMR106 cells. The mRNA expressions of bone remodeling-related markers were consistent with the results of the bioassays.ConclusionThis study demonstrated that the isothermal LAMP test can distinguish between deer tendons and cattle tendons. Both types of tendons exhibited similar beneficial effects on bone remodeling according to the bioassay findings.Electronic supplementary materialThe online version of this article (doi:10.1186/s13020-015-0065-6) contains supplementary material, which is available to authorized users.

Three-Stage Extraction of Gelatines from Tendons of Abattoir Cattle: 1—Reaction Conditions

Short and long tendons of abattoir cattle are collagen by-products of the meat industry. They offer no utilisation at present, being a raw material source of over 90 % protein characteristic. This contribution deals with the three-stage extraction of gelatine from short cattle tendons. The principle of treatment consists in processing degreased tendons in the first processing stage in an environment resulting in the swelling of the starting material. In the second stage, the material is treated with a proteolytic enzyme to produce such disruption of the collagen substrate that makes gelatine extraction when boiling possible in the third stage of the process. In order to study the influence of the significant parameters during the extraction process on gelatine yield, experiments were planned using a factor experiment of 2(3) types. The variables under study were the duration of the second processing stage (5-25 h), temperature in the first and second processing stages (10-40 °C) and the addition of a proteolytic enzyme (1-5 %) on the quantity of the extracted gelatine. The results were processed statistically, and statistical significance of the studied factors was thus found. Contour graphs were plotted to easily survey the influence of the observed factors on gelatine yield. The process achieves up to 71 % efficiency, runs under atmospheric pressure and mild reaction conditions, and is conducive to preparing quality gelatines.

Three-Stage Extraction of Gelatines from Tendons of Abattoir Cattle: 2—Properties of Gelatines

The subject of our previous paper (part 1) was three-stage extraction of gelatines from short cattle tendons. In this paper, we studied influence of extraction conditions on quality of produced gelatines-protein content, ash content, rigidity of gelatine gels, viscosity, and distribution of molecular weights. Ash content of gelatines ranged in limits 3.5-10.5 %. Rigidity of the gels was influenced by extraction conditions and by elastin content in gelatines; highest-quality gels display rigidity of 213 Bloom. Viscosity of gelatines ranged from 2.47 to 12.11 mPa s. Molecular weights of gelatines display a proportion of fractions from 20 to 36 kDa, a quite high proportion of fractions from approximately 50 to 100 kDa, in some cases even fractions above 200 kDa appear. It was found that transition temperature and melting temperature of gelatines extracted from tendons are in accord with data on gelatines obtained by traditional extraction techniques from skins and bones. With respect to efficiency of the whole extraction process and to quality of extracted gelatine, we may recommend extraction conditions as follows: in the 1st processing stage, shaking degreased starting material with water in ratio 1:10 at 25 °C for 5 h; in the 2nd stage, treating the swelled material with 5 % (w/w) added proteolytic enzyme at 40 °C for 25 h; in 3rd stage, extracting gelatine while boiling for 16 min.

A novel, inexpensive and easy to use tendon clamp for in vitro biomechanical testing

Frozen clamps can hold tendons and ligaments tightly and transmit high loads, from 4kN to 13kN, without slippage, yet they are complex and expensive. The existing non-frozen serrated jaw clamp is simple to fabricate and use, but the maximal tensile force it can sustain is only about 2.5kN, which is not enough in many biomechanical tests. In this study, a new type of non-frozen clamp, which has lateral block boards and asymmetrical teeth jaws, was designed. The lateral block boards made of titanium alloy were used to prevent the soft tissues from being squeezed out during compressing, while the asymmetrical teeth jaws made of nylon were used to grip and keep holding soft tissues. The capability of this new type of clamp was tested by stretching five cattle tendons to failure on the tensile and compression testing machine, none of them displayed any slippage before rupture, the maximum tension force was 6.87kN. This non-frozen asymmetrical teeth jaw clamp was designed for gripping tendons in foot and ankle dynamic simulation test, but it can also be applied to other in vitro tests, such as hip and knee dynamic tests.

Isolation of elastin and collagen polypeptides from long cattle tendons as raw material for the cosmetic industry

Long cattle tendons were enzymatically disposed of lipoid and accompanying nitrogenous substances. Collagenous hydrolysate of average molecular mass M(a) = 0.830 +/- 1.206 kDa, suitable for application in skin and hair-care preparations, was obtained through hydrolysis by commercial protease (Bacillus subtilis) under mild conditions. Elastin, hydrolysable with greater difficulty, was subsequently hydrolysed by commercial endopeptidase (Bacillus licheniformis), under more drastic conditions, to a product of average molecular mass M(a) = 0.448 +/- 1.514 kDa. Purity of both hydrolysates was assessed by hydroxyproline and amide nitrogen contents. Aminosaccharides and glycosamino glycans in hydrolysates were not detected.

Collagenous hydrolysates from untraditional sources of proteins. Reaction condition and the yield of enzymatic hydrolysis of short cattle tendons

The effect of reaction conditions on the yield of enzymatic hydrolysis of short cattle tendons was examined using statistical scheme of factorial experiments 2(4). The duration of enzymatic purification of the starting material and of purified material denaturation processes, the protease concentration in reaction mixture and hydrolysis time were considered to be the main sources of reaction yield variation. An attempt was made to find the conditions leading to maximal yield of collagen hydrolysate.

Collagenous hydrolysates from untraditional sources of proteins

Sufficiently pure collagenous hydrolysates, suitable for application in skin and hair care cosmetics, have been prepared through biotechnological methods with the use of commercially available enzymatic preparations from short cattle tendons (musculus extensor communis, musculus flexor digitorum, musculus flexor digitorum profundis). These hydrolysates contain neither lipoid nor aminosaccharide components, content of primary amino groups reaches around 1.1 mmol g(-1) and the average molecular weight of the resulting collagenous hydrolysates does not exceed 2000 g mol(-1) (2.0 kDa). Short cattle tendons represent a relatively pure and easily available source of collagens and are, despite their generally known low nutritional value, used only as a feeding mixture component.

Systemic Connective Tissue Calcification in Cattle Poisoned by Solanum Malacoxylon: A Histological Study

The connective tissue changes seen in the lungs, cardiovascular system and tendons of cattle are described in natural and experimental Solanum malacoxylon poisoning. In the lung the characteristic lesiqns are swelling, fragmentation and calcification of the elastic fibres of the alveolar wall. The other major change in the lung is the disappearance of mucopolysaccharide from the bronchial cartilage, calcification of these cartilages, and their replacement by fibrous connective tissue. Les changements dans les tissus connectifs observés dans les poumons, le système cardiovasculaire et les tendons de bétails sont décrits dans les conditions d’empoisonnements naturels et expérimentaux par Solanum malacoxylon. Dans le poumon, les lésions caractéristiques sont le gonflement, la fragmentation et la calcification des fibres élastiques dans la paroi alvéolaire. L’autre changement majeur dans le poumon est la disparition des mucopolysaccharides du cartilage bonchique, la calcification de ces cartilages, et leur remplacement par des tissus connectifs fibreux. Beschreibung der Bindegeweberveränderungen, die in den Lungen, im Herz und Gefässystem und den Sehnen von Rindern nach natürlicher und experimenteller Vergiftung mit Solanum malacoxylon gefunden wurden. Die charakteristischen Manifestationen in den Lungen sind Schwellung, Fragmentation und Kalzifikation der elastischen Fasern in den Alveolarwänden. Die andere hauptsächliche Veränderung in der Lunge ist das Verschwinden der Monopolysaccharide aus dem Knorpelgewebe der Bronchien, die Kalzifikation der Knorpel und ihre Ersetzung durch fibröses Bindegewebe. Se describen los cambios en el tejido conjuntivo observados en los pulmones, sistema cardiovascular y tendones del ganado con envenenamiento natural y experimental por Solanum ecalacoxylon. En el pulmón, las lesiones características son hinchazón, fragmentación y calcificación de las fibras elásticas de la pared alveolar. El otro cambio importante en los pulmones es la desaparición de mucopolisacáridos del cartílago bronquial, calcificación de estos cartílagos, y su reemplazamiento por tejido conjuntivo fibroso.

THE EXTRUDED COLLAGEN SUTURE: TISSUE REACTION AND ABSORPTION.

As the search for a more desirable suture material for extraocular muscle surgery continues, various products must be used and evaluated. Catgut, made of ovine and bovine intestinal submucosa, has the advantage of complete absorption but has the undesirable quality of frequent large and unsightly granuloma formation. Synthetic suture material such as nylon, Supramid, and Mersilene causes little tissue reaction but must be buried and may subsequently erode through the conjunctiva or remain visible through the overlying conjunctiva.1 An extruded collagen suture * has now been made available. This suture, prepared from the deep flexor tendons of cattle, has the advantages of greater uniformity of size, greater purity, and, because it is more homogeneous, should have more dependable rates of absorption. Miller et al2have reported that the extruded collagen suture is smoother, more pliable, and has greater tensile strength than catgut. They used it successfully in 363 patients

USE OF A PLAIN EXTRUDED COLLAGEN SUTURE: CLINICAL OBSERVATIONS.

CHROMICIZED extruded collagen suture was used successfully in 363 patients who had a wide variety of operations. 1 The suture was strong, smooth, and pliable. Knots could be tied and seated easily because of the good degree of resiliency of the suture. Fraying and breaking occurred infrequently. Greater uniformity of size permitted a smaller size to be used in comparison with catgut suture. The extruded collagen suture gave the surgeon a dependable material which could be used confidently in operations. Many surgeons prefer to use a plain type of suture in the subcutaneous tissues. Although such tissues tolerated the chromicized suture nicely, a study of the plain suture was undertaken to determine if it also was a desirable suture. The plain extruded collagen suture is made in the same way as its chromicized counterpart except that the tanning process is omitted. The deep flexor tendons of cattle are sliced, digested