Journal Articles
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Item Insights into the pathogenesis of catastrophic spontaneous humeral fractures in first-lactation dairy cows(CSIRO Publishing, Australia, 2025-05-06) Wehrle-Martinez AS; Lawrence KE; Back PJ; Rogers CW; Gibson MJ; Dittmer KE; Eastwood CSpontaneous humeral fractures in first-lactation dairy cows have introduced significant challenges to the dairy industry in New Zealand, impacting animal welfare, farm economics, and veterinary practices. This review synthesizes current knowledge on the pathogenesis of these fractures and identifies potential key risk factors. The majority of bones from affected first-lactation dairy cows have osteoporosis, which is associated with inadequate bone formation and increased bone resorption. In addition, low total collagen content in bones from most affected dairy cows supports the hypothesis that inadequate bone formation is an important risk factor associated with humeral fractures in these cows. Spectroscopic analyses further confirmed a significant reduction in bone quality and strength. Novel findings suggest that low liver copper concentration in many of the affected cows' results from the mobilisation of copper to the bone. Although limited, the accumulated evidence suggests that to mitigate the incidence of catastrophic fractures, adequate nutrition (especially protein-energy) should be supplied during important growth periods. While significant progress has been made in understanding the cause of these fractures, many uncertainties and areas requiring further research remain.Item Gelatin and Collagen from Sheepskin.(MDPI (Basel, Switzerland), 2024-05-31) Matinong AME; Pickering KL; Waterland MR; Chisti Y; Haverkamp RG; Yu L; Popa MAbattoirs dispose of sheepskins as solid waste due to low price and poor demand for sheepskin leather. In principle, as an alternative to being disposed of in landfill, sheepskins can serve as a source of the protein collagen or the hydrolysis product, gelatin. In this research, sheepskins collected from abattoirs were used as a source of collagen. Three extraction methods were compared: acid extraction, acid with enzymes, and alkali extraction. The extracted material was characterized using scanning electron microscopy (SEM) and Fourier-transform infrared spectroscopy (FTIR), small angle X-ray scattering (SAXS), and sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The collagen and gelatin extraction yield ranged from 3.1% to 4.8% with the product purity determined by hydroxyproline, ranging from 7.8% for the alkali process to 59% and 68% for the acid and acid-enzyme processes. SDS PAGE showed that the acid process produced fragments with molecular weights in the range 100 to >250 kDa, while acid-enzyme resulted in smaller fragments, below 30 kDa. The FTIR region of the amide I band at 1800-1550 cm-1, which was used as an indicator of the collagen and gelatin content, showed that the gelatin dominated in the acid extracts, and the alkaline extract contained a large portion of keratin. SAXS was found to be a sensitive method for showing the presence of intact collagen fibrils in materials from all of the extraction methods, albeit at low concentrations. Herein, sheepskin is shown to be a useful source for collagen-gelatin material of varying molecular weights.Item Impact of Gut Recolonization on Liver Regeneration: Hepatic Matrisome Gene Expression after Partial Hepatectomy in Mice.(MDPI (Basel, Switzerland), 2023-06-28) Amin AR; Hairulhisyam NM; Aqilah RNF; Nur Fariha MM; Mallard BL; Shanahan F; Wheatley AM; Marlini M; Neuman M; Malnick SThe hepatic matrisome is involved in the remodeling phase of liver regeneration. As the gut microbiota has been implicated in liver regeneration, we investigated its role in liver regeneration focusing on gene expression of the hepatic matrisome after partial hepatectomy (PHx) in germ-free (GF) mice, and in GF mice reconstituted with normal gut microbiota (XGF). Liver mass restoration, hepatocyte proliferation, and immune response were assessed following 70% PHx. Hepatic matrisome and collagen gene expression were also analyzed. Reduced liver weight/body weight ratio, mitotic count, and hepatocyte proliferative index at 72 h post PHx in GF mice were preceded by reduced expression of cytokine receptor genes Tnfrsf1a and Il6ra, and Hgf gene at 3 h post PHx. In XGF mice, these indices were significantly higher than in GF mice, and similar to that of control mice, indicating normal liver regeneration. Differentially expressed genes (DEGs) of the matrisome were lower in GF compared to XGF mice at both 3 h and 72 h post PHx. GF mice also demonstrated lower collagen expression, with significantly lower expression of Col1a1, Col1a2, Col5a1, and Col6a2 compared to WT mice at 72 h post PHx. In conclusion, enhanced liver regeneration and matrisome expression in XGF mice suggests that interaction of the gut microbiota and matrisome may play a significant role in the regulation of hepatic remodeling during the regenerative process.Item In Vitro Assessment of Hydrolysed Collagen Fermentation Using Domestic Cat (Felis catus) Faecal Inocula(MDPI (Basel, Switzerland), 2022-02-17) Butowski CF; Thomas DG; Cave NJ; Bermingham EN; Rosendale DI; Hea S-Y; Stoklosinski HM; Young W; Ebani VVThe gastrointestinal microbiome has a range of roles in the host, including the production of beneficial fermentation end products such as butyrate, which are typically associated with fermentation of plant fibres. However, domestic cats are obligate carnivores and do not require carbohydrates. It has been hypothesised that in the wild, collagenous parts of prey-the so-called animal-derived fermentable substrates (ADFS) such as tendons and cartilage-may be fermented by the cat's gastrointestinal microbiome. However, little research has been conducted on ADFS in the domestic cat. Faecal inoculum was obtained from domestic cats either consuming a high carbohydrate (protein:fat:carbohydrate ratio of 35:20:28 (% dry matter basis)) or high protein (protein:fat:carbohydrate ratio of 75:19:1 (% dry matter basis)) diet. ADFS (hydrolysed collagen, cat hair, and cartilage) were used in a series of static in vitro digestions and fermentations. Concentrations of organic acids and ammonia were measured after 24 h of fermentation, and the culture community of microbes was characterised. The type of inoculum used affected the fermentation profile produced by the ADFS. Butyrate concentrations were highest when hydrolysed collagen was fermented with high protein inoculum (p < 0.05). In contrast, butyrate was not detectable when hydrolysed collagen was fermented in high carbohydrate inoculum (p < 0.05). The microbiome of the domestic cat may be able to ferment ADFS to provide beneficial concentrations of butyrate.Item Collagen Extraction from Animal Skin(MDPI (Basel, Switzerland), 13/06/2022) Matinong AME; Chisti Y; Pickering KL; Haverkamp RGCollagen is the most abundant structural protein in animals. It is the major component of skin. It finds uses in cosmetics, medicine, yarn production and packaging. This paper reviews the extraction of collagen from hides of most consumed animals for meat with the focus on literature published since 2000. The different pretreatment and extraction techniques that have been investigated for producing collagen from animal skins are reviewed. Pretreatment by enzymatic, acid or alkaline methods have been used. Extraction by chemical hydrolysis, salt solubilization, enzymatic hydrolysis, ultrasound assisted extraction and other methods are described. Post-extraction purification methods are also explained. This compilation will be useful for anyone wishing to use collagen as a resource and wanting to further improve the extraction and purification methods.Item Novel Assessment of Collagen and Its Crosslink Content in the Humerus from Primiparous Dairy Cows with Spontaneous Humeral Fractures Due to Osteoporosis from New Zealand.(23/09/2022) Wehrle-Martinez A; Naffa R; Back P; Rogers CW; Lawrence K; Loo T; Sutherland-Smith A; Dittmer KNumerous cases of spontaneous humeral fracture in primiparous dairy cows from New Zealand have prompted the study of the condition to establish probable causes or risk factors associated with the condition. Previous studies identified inadequate protein-calorie malnutrition as an important contributory factor. Earlier case studies also reported that ~50% of cows have low liver and/or serum copper concentration at the time of humeral fracture. Because copper is so closely associated with the formation of collagen cross-links, the aim of this study was to compare collagen and collagen crosslink content in the humerus from primiparous cows with and without humeral fractures and to determine the role of copper in the occurrence of these fractures. Humeri were collected from cows with and without humeral fractures, ground, and the collagen and collagen cross-link content measured using high-performance liquid chromatography. Collagen content was significantly higher in the humeri of cows without humeral fractures, while total collagen crosslink content was significantly higher in the humerus of cows with humeral fractures. These results indicate other factor/s (e.g., protein-calorie undernutrition) might be more important than the copper status in the occurrence of humeral fractures in dairy cows in New Zealand.Item Relative orientation of collagen molecules within a fibril: A homology model for homo sapiens type I collagen.(Taylor & Francis, 30/01/2018) Collier TA; Nash A; Birch HL; de Leeuw NHType I collagen is an essential extracellular protein that plays an important structural role in tissues that require high tensile strength. However, owing to the molecule’s size, to date no experimental structural data are available for the Homo sapiens species. Therefore, there is a real need to develop a reliable homology model and a method to study the packing of the collagen molecules within the fibril. Through the use of the homology model and implementation of a novel simulation technique, we have ascertained the orientations of the collagen molecules within a fibril, which is currently below the resolution limit of experimental techniques. The longitudinal orientation of collagen molecules within a fibril has a significant effect on the mechanical and biological properties of the fibril, owing to the different amino acid side-chains available at the interface between the molecules.Item Structure and Strength of Bovine and Equine Amniotic Membrane(MDPI (Basel, Switzerland), 2022-08) Wells HC; Sizeland KH; Kirby N; Haverkamp RGThin, strong scaffold materials are needed for surgical applications. New materials are required, particularly those readily available, such as from non-human sources. Bovine amniotic membrane (antepartum) and equine amniotic membrane (postpartum) were characterized with tear and tensile tests. The structural arrangement of the collagen fibrils was determined by small-angle X-ray scattering, scanning electron microscopy, and ultrasonic imaging. Bovine amnion had a thickness-normalized tear strength of 12.6 (3.8) N/mm, while equine amnion was 14.8 (5.3) N/mm. SAXS analysis of the collagen fibril arrangement yielded an orientation index of 0.587 (0.06) and 0.681 (0.05) for bovine and equine, respectively. This may indicate a relationship between more highly aligned collagen fibrils and greater strength, as seen in other materials. Amnion from bovine or equine sources are strong, thin, elastic materials, although weaker than other collagen tissue materials commonly used, that may find application in surgery as an alternative to material from human donors.