Displaying publications 1 - 20 of 273 in total

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  1. Chowdhury SR, Mh Busra MF, Lokanathan Y, Ng MH, Law JX, Cletus UC, et al.
    Adv Exp Med Biol, 2018 10 26;1077:389-414.
    PMID: 30357700 DOI: 10.1007/978-981-13-0947-2_21
    Collagen type I is the most abundant matrix protein in the human body and is highly demanded in tissue engineering, regenerative medicine, and pharmaceutical applications. To meet the uprising demand in biomedical applications, collagen type I has been isolated from mammalians (bovine, porcine, goat and rat) and non-mammalians (fish, amphibian, and sea plant) source using various extraction techniques. Recent advancement enables fabrication of collagen scaffolds in multiple forms such as film, sponge, and hydrogel, with or without other biomaterials. The scaffolds are extensively used to develop tissue substitutes in regenerating or repairing diseased or damaged tissues. The 3D scaffolds are also used to develop in vitro model and as a vehicle for delivering drugs or active compounds.
    Matched MeSH terms: Collagen; Collagen Type I*
  2. Yuswan MH, A Jalil NH, Mohamad H, Keso S, Mohamad NA, Tengku Md Yusoff TS, et al.
    Food Chem, 2021 Feb 01;337:127762.
    PMID: 32777563 DOI: 10.1016/j.foodchem.2020.127762
    Gelatin and collagen are considered halal-critical ingredients as they are typically derived from either bovine or porcine animals. Current analytical methods for determining the sources of gelatin and collagen suffer from limitations in terms of robustness and false positives in peptide matching. Thus, the aim of this study was to investigate the utility of monitoring hydroxyproline, a signature amino acid for gelatin and collagen, for identifying potentially haram foodstuffs. To determine the hydroxyproline profiles among animal- and plant-based samples, one-way univariate analysis of variance followed by pair-wise comparison was used to establish statistical significance. Multivariate chemometric analysis through principal component analysis revealed a discrete distribution pattern among 59 samples due to hydroxyproline variability. Finally, inter- and intra-laboratory comparisons demonstrated the validity and robustness of hydroxyproline determination according to ISO 17025. Thus, this preliminary identification technique will aid the identification of potentially haram foodstuffs.
    Matched MeSH terms: Collagen/analysis*; Collagen/chemistry
  3. Md Nazir N, Zulkifly AH, Khalid KA, Zainol I, Zamli Z, Sha'ban M
    Tissue Eng Regen Med, 2019 06;16(3):285-299.
    PMID: 31205857 DOI: 10.1007/s13770-019-00191-1
    Background: This study aimed to observe the cartilaginous matrix production in SRY (sex determining region Y)-box 9 (SOX9)- and/or telomerase reverse transcriptase (TERT)-transfected chondrocytes from monolayer to three-dimensional (3D) culture.

    Methods: The genes were transferred into chondrocytes at passage-1 (P1) via lipofection. The post-transfected chondrocytes (SOX9-, TERT- and SOX9/TERT) were analysed at P1, P2 and P3. The non-transfected group was used as control. The 3D culture was established using the chondrocytes seeded in a disc-shaped PLGA/fibrin and PLGA scaffolds. The resulting 3D "cells-scaffolds" constructs were analysed at week-1, -2 and -3. The histoarchitecture was evaluated using haematoxylin and eosin, alcian blue and safranin o stains. The quantitative sulphated glycosaminoglycan (sGAG) content was measured using biochemical assay. The cartilage-specific markers expression were analysed via real-time polymerase chain reaction.

    Results: All monolayer cultured chondrocytes showed flattened, fibroblast-like appearance throughout passages. Proteoglycan and sGAG were not detected at the pericellular matrix region of the chondrocytes. The sGAG content assay indicated the matrix production depletion in the culture. The cartilage-specific markers, COL2A1 and ACAN, were downregulated. However, the dedifferentiation marker, COL1A1 was upregulated. In 3D "cells-scaffolds" constructs, regardless of transfection groups, chondrocytes seeded in PLGA/fibrin showed a more uniform distribution and produced denser matrix than the PLGA group especially at week-3. Both sGAG and proteoglycan were clearly visualised in the constructs, supported by the increment of sGAG content, quantitatively. Both COL2A1 and ACAN were upregulated in SOX9/TERT-PLGA and SOX9/TERT-PLGA/fibrin respectively. While, COL1A1 was downregulated in SOX9/TERT-PLGA.

    Conclusion: These findings indicated that the SOX9/TERT-transfected chondrocytes incorporation into 3D scaffolds facilitates the cartilage regeneration which is viable structurally and functionally.

    Matched MeSH terms: Collagen Type I/genetics; Collagen Type I/metabolism; Collagen Type II/genetics; Collagen Type II/metabolism
  4. Nur Adelina AN, Aminuddin BS, Munirah S, Chua KH, Fuzina NH, Saim L, et al.
    Med J Malaysia, 2004 May;59 Suppl B:188-9.
    PMID: 15468881
    Cartilage is regularly needed for reconstructive surgery. Basic research in tissue engineering is necessary to develop its full potential. We presented here the expression profile of type II collagen gene and type I collagen gene in human auricular monolayer culture expansion. Cultured chondrocytes documented a reduction in the expression level of collagen type II gene whilst collagen type I gene was gradually expressed through all the passages. This study demonstrated that human auricular chondrocytes lose its phenotypic expression during monolayer culture expansion. Further studies are required to enhance cartilage specific gene expression, collagen type II throughout the in vitro culture.
    Matched MeSH terms: Collagen Type I/genetics*; Collagen Type II/genetics*
  5. Yaacob HB
    J Nihon Univ Sch Dent, 1990 Sep;32(3):187-91.
    PMID: 2230962
    The twenty-fifth reported case of squamous odontogenic tumor is presented. The patient was a 39-year-old Chinese Malaysian male. The lesion was asymptomatic and did not recur after excision. It is important to distinguish this type of lesion from squamous odontogenic tumor-like proliferation. The rest of Malassez is thought to be responsible for the histogenesis of the lesion. Better understanding will only be achieved when more cases are reported and studied.
    Matched MeSH terms: Collagen
  6. Rajan Saini, Abdul Rani Samsudin
    MyJurnal
    Desmoplastic ameloblastoma (DA) is a relatively rare histological variant of ameloblastoma. DA do not present with radiographic or clinical features that are typical of other variants of ameloblastoma. On gross examination, DA appears as a solid mass, unlike the conventional ameloblastoma that contains fluid-filled spaces. Although radiographic examination of ameloblastomas usually reveals unilocular or multilocular radiolucency, DA may appear as a mixed radiopaque-radiolucent lesion. Histologically, DA is characterized by small nests and strands of “compressed” odontogenic epithelium supported by pronounced collagenized stroma. This report describes the case of a 30-year-old male with DA of the left mandible.
    Matched MeSH terms: Collagen
  7. Khong NMH, Yusoff FM, Jamilah B, Basri M, Maznah I, Chan KW, et al.
    Food Chem, 2018 Jun 15;251:41-50.
    PMID: 29426422 DOI: 10.1016/j.foodchem.2017.12.083
    Efficiency and effectiveness of collagen extraction process contribute to huge impacts to the quality, supply and cost of the collagen produced. Jellyfish is a potential sustainable source of collagen where their applications are not limited by religious constraints and threats of transmittable diseases. The present study compared the extraction yield, physico-chemical properties and toxicology in vitro of collagens obtained by the conventional acid-assisted and pepsin-assisted extraction to an improved physical-aided extraction process. By increasing physical intervention, the production yield increased significantly compared to the conventional extraction processes (p Collagen extracted using the improved process was found to possess similar proximate and amino acids composition to those extracted using pepsin (p > .05) while retaining high molecular weight distributions and polypeptide profiles similar to those extracted using only acid. Moreover, they exhibited better appearance, instrumental colour and were found to be non-toxic in vitro and free of heavy metal contamination.
    Matched MeSH terms: Collagen/isolation & purification*; Collagen/toxicity; Collagen/chemistry*
  8. Daood U, Matinlinna JP, Fawzy AS
    Dent Mater, 2019 02;35(2):356-367.
    PMID: 30528297 DOI: 10.1016/j.dental.2018.11.031
    OBJECTIVE: Effect of d-alpha-tocopheryl poly(ethyleneglycol)-1000-succinate (VE-TPGS) with riboflavin-5'-phosphate solution on crosslinking of dentine collagen was investigated to analyze collagen's structural integrity.

    METHODS: VE-TPGS was added to RF-solution, at RF/VE-TPGS (w/w) ratios of 0.125/0.250 and 0.125/0.500. Demineralized dentine beams were used (10wt.% phosphoric acid), rinsed using deionized-water and analysed using ELISA (Human MMP2 ELISA; Human CTSK/Cathepsin-K for MMP2 and Cathepsin K analysis). AFM of dentine collagen-fibrils structure was done before and after dentine specimens' placement in mineralization solution and tested after 14days in artificial saliva/collagenase (AS/Co) solution. The specimens were tested after 24h in mineralization solution for surface/bulk elastic modulus. Nano-indentation was carried out for each specimen on intertubular-dentine with lateral spacing of 400nm. Reduced elastic-modulus and nano-hardness were calculated and collagen content was determined using hydroxyproline-assay. Micro-Raman were performed. TEM was carried out to study structural variations of dentine-collagen in artificial-saliva (collagenase). Data were presented as mean±standard deviation and analyzed by SPSS v.15, by analysis of variance.

    RESULTS: Synergetic effect of VE-TPGS was observed with RF through higher structural integrity of dentine collagen-fibrils shown by TEM/AFM. Superior surface/bulk mechanical stability was shown by nano-indentation/mechanical testing. Improvement in collagenase degradation resistance for hydroxyproline release was observed and lower endogenous-protease release of MMP-2/Cathepsin-K. Raman-analysis analysed chemical interactions between RF and collagen confirming structural-integrity of collagen fibrils after crosslinking. After 24h mineralization, AFM showed mineral depositions in close association with dentine-collagen fibrils with RF/VE-TPGS formulations.

    SIGNIFICANCE: Potential synergetic effect of RF/VE-TPGS was observed by reflection of higher structural integrity and conformational-stability of dentine-collagen fibrils.

    Matched MeSH terms: Collagen
  9. Talebi S, Daraghma SMA, Subramaniam RT, Bhassu S, Gnana Kumar G, Periasamy V
    ACS Omega, 2020 Apr 14;5(14):7802-7808.
    PMID: 32309689 DOI: 10.1021/acsomega.9b03831
    Proteins have been increasingly suggested as suitable candidates for the fabrication of biological computers and other biomolecular-based electronic devices mainly due to their interesting structure-related intrinsic electrical properties. These natural biopolymers are environmentally friendly substitutes for conventional inorganic materials and find numerous applications in bioelectronics. Effective manipulation of protein biomolecules allows for accurate fabrication of nanoscaled device dimensions for miniaturized electronics. The prerequisite, however, demands an interrogation of its various electronic properties prior to understanding the complex charge transfer mechanisms in protein molecules, the knowledge of which will be crucial toward development of such nanodevices. One significantly preferred method in recent times involves the utilization of solid-state sensors where interactions of proteins could be investigated upon contact with metals such as gold. Therefore, in this work, proteins (hemoglobin and collagen) were integrated within a two-electrode system, and the resulting electronic profiles were investigated. Interestingly, structure-related electronic profiles representing semiconductive-like behaviors were observed. These characteristic electronic profiles arise from the metal (Au)-semiconductor (protein) junction, clearly demonstrating the formation of a Schottky junction. Further interpretation of the electronic behavior of proteins was done by the calculation of selected solid-state parameters. For example, the turn-on voltage of hemoglobin was measured to occur at a lower turn-on voltage, indicating the possible influence of the hem group present as a cofactor in each subunit of this tetrameric protein.
    Matched MeSH terms: Collagen
  10. Saallah S, Roslan J, Julius FS, Saallah S, Mohamad Razali UH, Pindi W, et al.
    Molecules, 2021 Apr 28;26(9).
    PMID: 33924820 DOI: 10.3390/molecules26092564
    Collagen was extracted from the body wall of sea cucumber (Holothuria scabra) using the pepsin-solubilized collagen method followed by isolation using dialysis and the ultrafiltration membrane. The yield and physicochemical properties of the collagen obtained from both isolation methods, denoted as D-PSC and UF-PSC, were compared. The ultrafiltration method affords a higher yield of collagen (11.39%) than that of the dialysis (5.15%). The isolated collagens have almost the same amino acid composition, while their functional groups, referred to as amide A, B, I, II, and III bands, were in accordance with commercial collagen, as verified by Fourier Transform Infrared (FT-IR) spectroscopy. The UV-Vis absorption peaks at 240 nm and 220 nm, respectively, indicated that the collagens produced are type-I collagen. The D-PSC showed interconnecting sheet-like fibrils, while the UF-PSC exhibited a flaky structure with flat-sheets arranged very close to each other. The higher yield and comparable physicochemical properties of the collagen obtained by ultrafiltration as compared with dialysis indicate that the membrane process has high potential to be used in large-scale collagen production for food and pharmaceutical applications.
    Matched MeSH terms: Collagen/isolation & purification*; Collagen/ultrastructure; Collagen/chemistry*
  11. Shori AB, Hong YC, Baba AS
    Food Res Int, 2021 05;143:110238.
    PMID: 33992351 DOI: 10.1016/j.foodres.2021.110238
    Four types of cheeses were prepared included plain- cheese (control), Codonopsis pilosula (CP)- cheese, plain- cheese with fish collagen (FC; control) and CP- cheese with FC. The effects of cheese samples on acidification, proteolysis of milk proteins using three methods (cadmium-ninhydrin method, O-phthaldialdehyde (OPA) assay, and electrophoresis assay), and angiotensin-converting enzyme (ACE)-inhibitory activity were investigated during 0, 2, & 4 weeks of ripening. In addition, the sensory evaluation was also investigated during 0, 2, 4, & 8 weeks of ripening. The presence of FC in CP- cheese increased the numbers of free amino acids (FAA) at 0 and 2 weeks. The addition of CP both in the presence and absence of FC affected positively (p collagen had similar organoleptic characteristics to plain-cheese. In conclusion, C. pilosula and/or fish collagen may lead to the development in the production and formulation of cheese with anti-ACE activity.
    Matched MeSH terms: Collagen
  12. Abedin MZ, Karim AA, Ahmed F, Latiff AA, Gan CY, Che Ghazali F, et al.
    J Sci Food Agric, 2013 Mar 30;93(5):1083-8.
    PMID: 22936269 DOI: 10.1002/jsfa.5854
    Sea cucumber (Stichopus vastus) is considered an underutilized resource, since only its stomach and intestines are eaten raw as salad in a few countries and the remaining parts, especially the integument rich in collagen, is discarded. Hence a valuable by-product having potential nutraceutical and pharmaceutical applications is wasted. In the present investigation, pepsin-solubilized collagen (PSC) from the integument of S. vastus was isolated, purified and characterized.
    Matched MeSH terms: Collagen/economics; Collagen/isolation & purification; Collagen/metabolism; Collagen/chemistry*; Collagen Type I/economics; Collagen Type I/isolation & purification; Collagen Type I/metabolism; Collagen Type I/chemistry
  13. Sha'ban M, Yoon SJ, Ko YK, Ha HJ, Kim SH, So JW, et al.
    J Biomater Sci Polym Ed, 2008;19(9):1219-37.
    PMID: 18727862 DOI: 10.1163/156856208785540163
    Previously, we have proven that fibrin and poly(lactic-co-glycolic acid) (PLGA) scaffolds facilitate cell proliferation, matrix production and early chondrogenesis of rabbit articular chondrocytes in in vitro and in vivo experiments. In this study, we evaluated the potential of fibrin/PLGA scaffold for intervertebral disc (IVD) tissue engineering using annulus fibrosus (AF) and nucleus pulposus (NP) cells in relation to potential clinical application. PLGA scaffolds were soaked in cells-fibrin suspension and polymerized by dropping thrombin-sodium chloride (CaCl(2)) solution. A PLGA-cell complex without fibrin was used as control. Higher cellular proliferation activity was observed in fibrin/PLGA-seeded AF and NP cells at each time point of 3, 7, 14 and 7 days using the MTT assay. After 3 weeks in vitro incubation, fibrin/PLGA exhibited a firmer gross morphology than PLGA groups. A significant cartilaginous tissue formation was observed in fibrin/PLGA, as proven by the development of cells cluster of various sizes and three-dimensional (3D) cartilaginous histoarchitecture and the presence of proteoglycan-rich matrix and glycosaminoglycan (GAG). The sGAG production measured by 1,9-dimethylmethylene blue (DMMB) assay revealed greater sGAG production in fibrin/PLGA than PLGA group. Immunohistochemical analyses showed expressions of collagen type II, aggrecan core protein and collagen type I genes throughout in vitro culture in both fibrin/PLGA and PLGA. In conclusion, fibrin promotes cell proliferation, stable in vitro tissue morphology, superior cartilaginous tissue formation and sGAG production of AF and NP cells cultured in PLGA scaffold. The 3D porous PLGA scaffold-cell complexes using fibrin can provide a vehicle for delivery of cells to regenerate tissue-engineered IVD tissue.
    Matched MeSH terms: Collagen Type I/genetics; Collagen Type I/metabolism; Collagen Type II/genetics; Collagen Type II/metabolism
  14. Ramachandra SS, Rana R, Reetika S, Jithendra KD
    Cell Tissue Bank, 2014 Sep;15(3):297-305.
    PMID: 24002077 DOI: 10.1007/s10561-013-9395-8
    As esthetics gain importance, periodontal plastic surgical procedures involving soft tissue grafts are becoming commoner both around natural teeth as well as around implants. Periodontal soft tissue grafts are primarily used for the purpose of root coverage and in pre-prosthetic surgery to thicken a gingival site or to improve the crestal volume. Soft tissue grafts are usually harvested from the palate. Periodontal plastic surgical procedures involving soft tissue grafts harvested from the palate have two surgical sites; a recipient site and another donor site. Many patients are apprehensive about the soft tissue graft procedures, especially the creation of the second/donor surgical site in the palate. In the past decade, newer techniques and products have emerged which provide an option for the periodontist/patient to avoid the second surgical site. MucoMatrixX, Alloderm(®), Platelet rich fibrin, Puros(®) Dermis and Mucograft(®) are the various options available to the practicing periodontist to avoid the second surgical site. Use of these soft tissue allografts in an apprehensive patient would decrease patient morbidity and increase patient's acceptance towards periodontal plastic surgical procedures.
    Matched MeSH terms: Collagen/therapeutic use
  15. Busra FM, Chowdhury SR, Saim AB, Idrus RB
    Saudi Med J, 2011 Dec;32(12):1311-2.
    PMID: 22159390
    Matched MeSH terms: Collagen/toxicity*
  16. Baleg SM, Bidin N, Suan LP, Ahmad MF, Krishnan G, Johari AR, et al.
    J Cosmet Dermatol, 2015 Sep;14(3):246-53.
    PMID: 25817596 DOI: 10.1111/jocd.12142
    The aim of this study was to evaluate the effects of multiple pulses on the depth of injury caused by CO2 laser in an in vivo rat model.
    Matched MeSH terms: Collagen/analysis
  17. Lo TS, Lin YH, Yusoff FM, Chu HC, Hsieh WC, Uy-Patrimonio MC
    Sci Rep, 2016 12 19;6:38960.
    PMID: 27991501 DOI: 10.1038/srep38960
    Our aim is to study the inflammatory response towards the collagen-coated and non-coated polypropylene meshes in rats and the urodynamic investigation post-operatively. Forty-two female Sprague Dawley were divided into 7 groups of 6 rats; Control, Day 7 and 30 for Sham, Avaulta Plus (MPC), Perigee (MP). UDS were taken at days 7 and 30. Mesh with the vagina and bladder wall was removed and sent for immunohistochemical examination. Results showed intense inflammatory reaction on day 7 in the study groups which decreased on day 30. IL-1, TNF-α, MMP-2 and CD31 were observed to decrease from day 7 to day 30. NGF was almost normal on day 30 in all groups. UDS showed no difference in voiding pressure. Both Study and Sham groups had shorter voiding interval (VI) on day 7 but significantly lower in MPC. VI had significantly increased on day 30 in all groups. Voided volume was significantly lower in the mesh groups even when an increase was seen on day 30. In conclusion, the higher levels of IL-1, TNF-α and MMP-2 in collagen-coated polypropylene mesh imply greater inflammation than the non-coated polypropylene mesh. Mesh implantation can lead to shorter voiding interval and smaller bladder capacity.
    Matched MeSH terms: Collagen*
  18. Abdullah S, Mohtar F, Abdul Shukor N, Sapuan J
    J Hand Surg Asian Pac Vol, 2017 Dec;22(4):429-434.
    PMID: 29117830 DOI: 10.1142/S0218810417500459
    BACKGROUND: Synthetic scaffold has been used for tissue approximation and reconstructing damaged and torn ligaments. This study explores the ability of tendon ingrowth into a synthetic scaffold in vitro, evaluate growth characteristics, morphology and deposition of collagen matrix into a synthetic scaffold.

    METHODS: Upper limb tendons were harvested with consent from patients with crush injuries and non-replantable amputations. These tendons (both extensor and flexor) measuring 1 cm are sutured to either side of a 0.5 cm synthetic tendon strip and cultured in growth medium. At 2, 4, 6 and 8 weeks, samples were fixed into paraffin blocks, cut and stained with haematoxylin-eosin (H&E) and Masson's trichrome.

    RESULTS: Minimal tendon ingrowth were seen in the first 2 weeks of incubation. However at 4 weeks, the cell ingrowth were seen migrating towards the junction between the tendon and the synthetic scaffold. This ingrowth continued to expand at 6 weeks and up to 8 weeks. At this point, the demarcation between human tendon and synthetic scaffold was indistinct.

    CONCLUSIONS: We conclude that tendon ingrowth composed of collagen matrix were able to proliferate into a synthetic scaffold in vitro.

    Matched MeSH terms: Collagen/analysis
  19. Busra MFM, Lokanathan Y
    Curr Pharm Biotechnol, 2019;20(12):992-1003.
    PMID: 31364511 DOI: 10.2174/1389201020666190731121016
    Tissue engineering focuses on developing biological substitutes to restore, maintain or improve tissue functions. The three main components of its application are scaffold, cell and growthstimulating signals. Scaffolds composed of biomaterials mainly function as the structural support for ex vivo cells to attach and proliferate. They also provide physical, mechanical and biochemical cues for the differentiation of cells before transferring to the in vivo site. Collagen has been long used in various clinical applications, including drug delivery. The wide usage of collagen in the clinical field can be attributed to its abundance in nature, biocompatibility, low antigenicity and biodegradability. In addition, the high tensile strength and fibril-forming ability of collagen enable its fabrication into various forms, such as sheet/membrane, sponge, hydrogel, beads, nanofibre and nanoparticle, and as a coating material. The wide option of fabrication technology together with the excellent biological and physicochemical characteristics of collagen has stimulated the use of collagen scaffolds in various tissue engineering applications. This review describes the fabrication methods used to produce various forms of scaffolds used in tissue engineering applications.
    Matched MeSH terms: Collagen/chemistry*
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