Displaying publications 21 - 40 of 280 in total

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  1. Nam HY, Murali MR, Ahmad RE, Pingguan-Murphy B, Raghavendran HRB, Kamarul T
    Stem Cells Int, 2020;2020:5385960.
    PMID: 32908542 DOI: 10.1155/2020/5385960
    It has been suggested that mechanical strain may elicit cell differentiation in adult somatic cells through activation of epithelial sodium channels (ENaC). However, such phenomenon has not been previously demonstrated in mesenchymal stromal cells (MSCs). The present study was thus conducted to investigate the role of ENaC in human bone marrow-derived MSCs (hMSCs) tenogenic differentiation during uniaxial tensile loading. Passaged-2 hMSCs were seeded onto silicone chambers coated with collagen I and subjected to stretching at 1 Hz frequency and 8% strain for 6, 24, 48, and 72 hours. Analyses at these time points included cell morphology and alignment observation, immunocytochemistry and immunofluorescence staining (collagen I, collagen III, fibronectin, and N-cadherin), and gene expression (ENaC subunits, and tenogenic markers). Unstrained cells at similar time points served as the control group. To demonstrate the involvement of ENaC in the differentiation process, an ENaC blocker (benzamil) was used and the results were compared to the noninhibited hMSCs. ENaC subunits' (α, β, γ, and δ) expression was observed in hMSCs, although only α subunit was significantly increased during stretching. An increase in tenogenic genes' (collagen1, collagen3, decorin, tenascin-c, scleraxis, and tenomodulin) and proteins' (collagen I, collagen III, fibronectin, and N-cadherin) expression suggests that hMSCs underwent tenogenic differentiation when subjected to uniaxial loading. Inhibition of ENaC function resulted in decreased expression of these markers, thereby suggesting that ENaC plays a vital role in tenogenic differentiation of hMSCs during mechanical loading.
    Matched MeSH terms: Collagen; Collagen Type I
  2. Busra FM, Chowdhury SR, Saim AB, Idrus RB
    Saudi Med J, 2011 Dec;32(12):1311-2.
    PMID: 22159390
    Matched MeSH terms: Collagen/toxicity*
  3. Vasudevan A, Majumder N, Sharma I, Kaur I, Sundarrajan S, Venugopal JR, et al.
    ACS Biomater Sci Eng, 2023 Nov 13;9(11):6357-6368.
    PMID: 37847169 DOI: 10.1021/acsbiomaterials.3c01216
    Immortalized liver cell lines and primary hepatocytes are currently used as in vitro models for hepatotoxic drug screening. However, a decline in the viability and functionality of hepatocytes with time is an important limitation of these culture models. Advancements in tissue engineering techniques have allowed us to overcome this challenge by designing suitable scaffolds for maintaining viable and functional primary hepatocytes for a longer period of time in culture. In the current study, we fabricated liver-specific nanofiber scaffolds with polylactic acid (PLA) along with a decellularized liver extracellular matrix (LEM) by the electrospinning technique. The fabricated hybrid PLA-LEM scaffolds were more hydrophilic and had better swelling properties than the PLA scaffolds. The hybrid scaffolds had a pore size of 38 ± 8 μm and supported primary rat hepatocyte cultures for 10 days. Increased viability (2-fold increase in the number of live cells) and functionality (5-fold increase in albumin secretion) were observed in primary hepatocytes cultured on the PLA-LEM scaffolds as compared to those on conventional collagen-coated plates on day 10 of culture. A significant increase in CYP1A2 enzyme activity was observed in hepatocytes cultured on PLA-LEM hybrid scaffolds in comparison to those on collagen upon induction with phenobarbital. Drugs like acetaminophen and rifampicin showed the highest toxicity in hepatocytes cultured on hybrid scaffolds. Also, the lethal dose of these drugs in rodents was accurately predicted as 1.6 g/kg and 594 mg/kg, respectively, from the corresponding IC50 values obtained from drug-treated hepatocytes on hybrid scaffolds. Thus, the fabricated liver-specific electrospun scaffolds maintained primary hepatocyte viability and functionality for an extended period in culture and served as an effective ex vivo drug screening platform to predict an accurate in vivo drug-induced hepatotoxicity.
    Matched MeSH terms: Collagen/metabolism
  4. 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
  5. 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
  6. Al-Bogami MM, Alkhorayef M, Sulieman A, Bradley D, Jawad AS, Mageed RA
    Appl Radiat Isot, 2024 Sep;211:111373.
    PMID: 38851075 DOI: 10.1016/j.apradiso.2024.111373
    In addition to generalised of bone loss and a higher fracture risk, rheumatoid arthritis (RA) causes periarticular bone erosions. Improvements in bone density/erosion and turnover may not go hand in hand with a positive clinical response to biological anti-inflammatory drugs assesed by disease activity score 28 (DAS28) in RA patients. This study aimed to understand how biologic anti-inflammatory drugs affect bone density, erosion, and turnover in RA patients. We examined bone mineral density (BMD) and bone turnover biomarkers. The study population consisted of 62 RA patients, 49 (79%) of whom were female and 13 (21%) of whom were male. The patients ranged in age from 40 to 79 years old. The patients' BMD was measured using a DEXA scan, and their plasma levels of bone turnover biomarkers CTX and osteocalcin were quantified utilizing an ELISA. BMD of the hip and lumbar spine in responder patients rose after therapy by 0.001g/cm2 (0.11 percent, p0.001 vs. before treatment) and 0.0396g/cm2 (3.96 percent, p0.001 vs. before treatment), respectively. Clinically non-responder patients' DAS28 revealed minor reductions in hip BMD values of -0.008g/cm2 (-0.78 percent, p0.001 vs. before therapy), as well as an improvement in lumbar spine BMD of 0.03g/cm2 (3.03 percent, p0.001 vs. before treatment). After 12 weeks of therapy, the CTX levels in responder patients dropped from 164 125 pg/ml to 131 129 pg/ml. Osteocalcin levels in non-responder patients increased substantially from 11.6 ng/ml to 14.9 ng/ml after 12 weeks of therapy compared to baseline (p = 0.01). Treatment with biologic anti-inflammatory medicines decreases widespread bone loss in RA patients' hip and lumbar spine. The beneficial effects of therapy on BMD were not associated with changes in disease activity of RA patients. Changes in plasma levels of bone turnover biomarkers such as sCTX and osteocalcin confirmed the treatment's beneficial effects.
    Matched MeSH terms: Collagen Type I/blood
  7. Daood U, Abduljabbar T, Al-Hamoudi N, Akram Z
    J Periodontal Res, 2018 Feb;53(1):123-130.
    PMID: 28940417 DOI: 10.1111/jre.12496
    BACKGROUND AND OBJECTIVE: The aim of the present study was to compare clinical periodontal parameters and to assess the release of C-telopeptides pyridinoline cross-links (ICTP) and C-terminal crosslinked telopeptide (CTX) from gingival collagen of naswar (NW) and non-naswar (control) dippers.

    MATERIAL AND METHODS: Eighty-seven individuals (42 individuals consuming NW and 45 controls) were included. Clinical (plaque index, bleeding on probing, probing depth and clinical attachment loss) and radiographic (marginal bone loss) periodontal parameters were compared among NW and control groups. Gingival specimens were taken from subjects in NW and control groups, assessed for ICTP and CTX levels (using ELISA) and analyzed using micro-Raman spectroscopy. The significance of differences in periodontal parameters between the groups was determined using Kruskal-Wallis and Mann-Whitney U tests. The percent loss of dry mass over exposure time and the rate of release of ICTP and CTX from all groups were compared using the paired t-test to examine the effects of exposure time.

    RESULTS: Clinical and radiographic periodontal parameters were significantly higher in the NW group than the control group (P collagen breakdown in the connective tissue of subjects in the NW group as a result of naswar usage.

    Matched MeSH terms: Collagen/metabolism*; Collagen Type I/metabolism*
  8. Hukmi, N.M.M., Sarbon, N.M.
    MyJurnal
    The aims of this study are to isolate and characterize acid soluble collagen (ASC) and pepsin soluble collagen (PSC) extracted from silver catfish (Pangasius sp.) skin. Isolated ASC and PSC collagen were characterized in terms of chemical composition (moisture, protein, fat and ash content), protein concentration, functional group, solubility, and morphological properties as compared to commercial collagen. Yields of ASC and PSC were 4.27% and 2.27%, respectively. The chemical compositions of raw skin were 34.64%, 2.81%, 3.68%, and 0.31%, while the chemical compositions of ASC and PSC were 94.21%, 3.48%, 0.81%, 59.15%, and 88.25%, 3.46%, 0.92%, and 29.24%, for moisture, protein, fat, and ash, respectively. ASC and PSC had protein concentrations of 2.27 mg/mL and 2.70 mg/mL, respectively. Functional group analysis revealed that both isolated collagens exhibited Amide A, II and III as a fingerprint for collagen structure. The highest solubility was found at pH 4 for ASC, pH 1 for PSC, and pH 5 for commercial collagen. The morphology of the isolated collagens was porous and they contained fibril. In conclusion, the characteristics of the isolated ASC and PSC from silver catfish (Pangasius sp.) skin indicate that value-added collagen can be produced from the alternative source of freshwater fish.
    Matched MeSH terms: Collagen
  9. Kim TW, Kim CW, Kwon SG, Hwang JH, Park DH, Kang DG, et al.
    Sains Malaysiana, 2016;45:1097-1103.
    In order to examine differences of meat quality traits depending on pH values post-mortem, the pH range was classified
    according to initial pH (pH45min) and ultimate pH (pH24hr) post-mortem. The differences of meat quality traits depending
    on sex were not changed by a number of amount, except for backfat thickness and fat content. The value of pH45min was
    positively correlated with pHdif, whereas pH24hr was negatively associated with lightness (CIE L*) and protein content. At
    pH45min post-slaughter, collagen content, fat content, shear force, water holding capacity and yellowness (CIE b*) showed
    lower values at the higher pH range of pH>6.7 than those of other ranges, but CIE L* and redness (CIE a*) presented
    the lowest value at the intermediate pH range of pH6.3~6.7. Conversely, at pH24hr post-slaughter, fat and moisture
    contents maintained the highest average values at the higher pH range of pH>6.1, but protein content showed higher
    value at the lower pH range of pH<5.7. Higher pH24hr appeared significantly lower shear force, but higher water holding
    capacity. CIE L*, a*, and b* values showed significantly higher values at the lowest region of pH24hr. Since meat quality
    characteristics seemed to be favored by consumers in rather than at the range of pH5.7~6.1, which showed significant
    differences of meat color, appearance, and meat juiciness, it is suggested that production of pork meat to appropriate
    pH value is performed by pig breeders and control measures taken during pre- and post-slaughters.
    Matched MeSH terms: Collagen
  10. Ab Aziz NA, Salim N, Zarei M, Saari N, Yusoff FM
    Prep Biochem Biotechnol, 2021;51(1):44-53.
    PMID: 32701046 DOI: 10.1080/10826068.2020.1789991
    The study was conducted to determine anti-tyrosinase and antioxidant activities of the extracted collagen hydrolysate (CH) derived from Malaysian jellyfish, Rhopilema hispidum. Collagen was extracted using 1:1 (w:v) 0.1 M NaOH solution at temperature 25 °C for 48 hr followed by treatment of 1:2 (w:v) distilled water for another 24 hr and freeze-dried. The extracted collagen was hydrolyzed using papain at optimum temperature, pH and enzyme/substrate ratio [E/S] of 60 °C, 7.0 and 1:50, respectively. CH was found to exhibit tyrosinase inhibitory activity, DPPH radical scavenging and metal ion-chelating assays up to 64, 28, and 83%, respectively, after 8 hr of hydrolysis process. The molecular weight of CH was found <10 kDa consisting of mainly Gly (19.219%), Glu (10.428%), and Arg (8.848%). The UV-visible spectrum analysis showed a major and minor peak at 218 and 276 nm, accordingly. The FTIR spectroscopy confirmed the amide groups in CH. The SEM images demonstrated spongy and porous structure of CH. In the cytotoxicity study, CH has no cytotoxicity against mouse embryonic 3T3 fibroblast cell line with IC50 value >500 µg/ml. Results revealed that the CH generated from this study has a potential to be developed as active ingredient in cosmeceutical application.
    Matched MeSH terms: Collagen/isolation & purification*; Collagen/pharmacology*; Collagen/chemistry
  11. Naomi R, Ardhani R, Hafiyyah OA, Fauzi MB
    Polymers (Basel), 2020 Sep 13;12(9).
    PMID: 32933133 DOI: 10.3390/polym12092081
    Collagen (Col) is a naturally available material and is widely used in the tissue engineering and medical field owing to its high biocompatibility and malleability. Promising results on the use of Col were observed in the periodontal application and many attempts have been carried out to inculcate Col for gingival recession (GR). Col is found to be an excellent provisional bioscaffold for the current treatment in GR. Therefore, the aim of this paper is to scrutinize an overview of the reported Col effect focusing on in vitro, in vivo, and clinical trials in GR application. A comprehensive literature search was performed using EBSCOhost, Science Direct, Springer Link, and Medline & Ovid databases to identify the potential articles on particular topics. The search query was accomplished based on the Boolean operators involving keywords such as (1) collagen OR scaffold OR hybrid scaffold OR biomaterial AND (2) gingiva recession OR tissue regeneration OR dental tissue OR healing mechanism OR gingiva. Only articles published from 2015 onwards were selected for further analysis. This review includes the physicochemical properties of Col scaffold and the outcome for GR. The comprehensive literature search retrieved a total of 3077 articles using the appropriate keywords. However, on the basis of the inclusion and exclusion criteria, only 15 articles were chosen for further review. The results from these articles indicated that Col promoted gingival tissue regeneration for GR healing. Therefore, this systematic review recapitulated that Col enhances regeneration of gingival tissue either through a slow or rapid process with no sign of cytotoxicity or adverse effect.
    Matched MeSH terms: Collagen
  12. Aziz J, Shezali H, Radzi Z, Yahya NA, Abu Kassim NH, Czernuszka J, et al.
    Skin Pharmacol Physiol, 2016;29(4):190-203.
    PMID: 27434176 DOI: 10.1159/000447017
    Collagen and elastin networks make up the majority of the extracellular matrix in many organs, such as the skin. The mechanisms which are involved in the maintenance of homeostatic equilibrium of these networks are numerous, involving the regulation of genetic expression, growth factor secretion, signalling pathways, secondary messaging systems, and ion channel activity. However, many factors are capable of disrupting these pathways, which leads to an imbalance of homeostatic equilibrium. Ultimately, this leads to changes in the physical nature of skin, both functionally and cosmetically. Although various factors have been identified, including carcinogenesis, ultraviolet exposure, and mechanical stretching of skin, it was discovered that many of them affect similar components of regulatory pathways, such as fibroblasts, lysyl oxidase, and fibronectin. Additionally, it was discovered that the various regulatory pathways intersect with each other at various stages instead of working independently of each other. This review paper proposes a model which elucidates how these molecular pathways intersect with one another, and how various internal and external factors can disrupt these pathways, ultimately leading to a disruption in collagen and elastin networks.
    Matched MeSH terms: Collagen/metabolism*; Collagen/radiation effects; Collagen/ultrastructure*
  13. Aina, M.A., Amin, I., Raja Mohd Hafidz, R.N., Yaakob, C.M.
    MyJurnal
    The peptide composition of gelatin is known to vary very common that the electrophoretic pattern of gelatin from one source differs from another source even for the same raw material. Therefore, the present study aimed to use proteomics field to identify gelatin polypeptides biomarker for depending on the condition under which collagen is hydrolyzed. Hence, it is porcine skins. The polypeptides obtained for porcine skin gelatins can be used as reference in future to detect the origins of gelatin added in the processed food. We compared porcine skin gelatin samples obtained from three producers. Total average numbers of polypeptides of porcine skin gelatins from company A, B and C were 303 ± 2.8, 285.5 ± 3.5 and 270.5 ± 4.9 spots respectively. 10 biomarkers were identified and presented in all different companies. We also did a mixture of porcine and bovine skin gelatin to detect the presence of these 10 biomarkers. The level of adulteration that could be detected was as low as 1.0% w/w
    Matched MeSH terms: Collagen
  14. Deen I, Selopal GS, Wang ZM, Rosei F
    J Colloid Interface Sci, 2022 Feb;607(Pt 1):869-880.
    PMID: 34536940 DOI: 10.1016/j.jcis.2021.08.199
    Coatings with bioactive properties play a key role in the success of orthopaedic implants. Recent studies focused on composite coatings incorporating biocompatible elements that can increase the nucleation of hydroxyapatite (HA), the mineral component of bone, and have promising bioactive and biodegradable properties. Here we report a method of fabricating composite collagen, chitosan and copper-doped phosphate glass (PG) coatings for biomedical applications using electrophoretic deposition (EPD). The use of collagen and chitosan (CTS) allows for the co-deposition of PG particles at standard ambient temperature and pressure (1 kPa, 25 °C), and the addition of collagen led to the steric stabilization of PG in solution. The coating composition was varied by altering the collagen/CTS concentrations in the solutions, as well as depositing PG with 0, 5 and 10 mol% CuO dopant. A monolayer of collagen/CTS containing PG was obtained on stainless steel cathodes, showing that deposition of PG in conjunction with a polymer is feasible. The mass of the monolayer varied depending on the polymer (collagen, CTS and collagen/CTS) and combination of polymer + PG (collagen-PG, CTS-PG and collagen/CTS-PG), while the presence of copper led to agglomerates during deposition at higher concentrations. The deposition yield was studied at different time points and showed a profile typical of constant voltage deposition. Increasing the concentration of collagen in the PG solution allows for a higher deposition yield, while pure collagen solutions resulted in hydrogen gas evolution at the cathode. The ability to deposit polymer-PG coatings that can mimic native bone tissue allows for the potential to fabricate orthopaedic implants with tailored biological properties with lower risk of rejection from the host and exhibit increased bioactivity.
    Matched MeSH terms: Collagen
  15. Das Gupta E
    Malays Fam Physician, 2009;4(2-3):48-50.
    PMID: 25606162 MyJurnal
    No screening test is ideal for detecting rheumatic diseases; diagnosis depends on appropriate history and thorough physical examination. Sometimes, laboratory investigations may be useful in confirming or ruling out rheumatic disease after a clinical diagnosis is considered. Once a rheumatic disease has been diagnosed, certain laboratory tests can help in assessing prognosis or determining the extent of the disease. Laboratory tests may also help the physician monitor certain rheumatic diseases, guide treatment or assess potential drug toxicity.
    Matched MeSH terms: Collagen Diseases
  16. Vithana EN, Aung T, Khor CC, Cornes BK, Tay WT, Sim X, et al.
    Hum Mol Genet, 2011 Feb 15;20(4):649-58.
    PMID: 21098505 DOI: 10.1093/hmg/ddq511
    Central corneal thickness (CCT) is a risk factor of glaucoma, the most common cause of irreversible blindness worldwide. The identification of genetic determinants affecting CCT in the normal population will provide insights into the mechanisms underlying the association between CCT and glaucoma, as well as the pathogenesis of glaucoma itself. We conducted two genome-wide association studies for CCT in 5080 individuals drawn from two ethnic populations in Singapore (2538 Indian and 2542 Malays) and identified novel genetic loci significantly associated with CCT (COL8A2 rs96067, p(meta) = 5.40 × 10⁻¹³, interval of RXRA-COL5A1 rs1536478, p(meta) = 3.05 × 10⁻⁹). We confirmed the involvement of a previously reported gene for CCT and brittle cornea syndrome (ZNF469) [rs9938149 (p(meta) = 1.63 × 10⁻¹⁶) and rs12447690 (p(meta) = 1.92 × 10⁻¹⁴)]. Evidence of association exceeding the formal threshold for genome-wide significance was observed at rs7044529, an SNP located within COL5A1 when data from this study (n = 5080, P = 0.0012) were considered together with all published data (reflecting an additional 7349 individuals, p(Fisher) = 1.5 × 10⁻⁹). These findings implicate the involvement of collagen genes influencing CCT and thus, possibly the pathogenesis of glaucoma.
    Matched MeSH terms: Collagen/genetics*; Collagen Type VIII/genetics
  17. Sergeeva IA, Klinov DV, Schäffer TE, Dubrovin EV
    Int J Biol Macromol, 2023 Jul 01;242(Pt 2):124835.
    PMID: 37201883 DOI: 10.1016/j.ijbiomac.2023.124835
    Though the capability of chromium treatment to improve the stability and mechanical properties of collagen fibrils is well-known, the influence of different chromium salts on collagen molecules (tropocollagen) is not well characterized. In this study, the effect of Cr3+ treatment on the conformation and hydrodynamic properties of collagen was studied using atomic force microscopy (AFM) and dynamic light scattering (DLS). Statistical analysis of contours of adsorbed tropocollagen molecules using the two-dimensional worm-like chain model revealed a reduction of the persistence length (i.e., the increase of flexibility) from ≈72 nm in water to ≈56-57 nm in chromium (III) salt solutions. DLS studies demonstrated an increase of the hydrodynamic radius from ≈140 nm in water to ≈190 nm in chromium (III) salt solutions, which is associated with protein aggregation. The kinetics of collagen aggregation was shown to be ionic strength dependent. Collagen molecules treated with three different chromium (III) salts demonstrated similar properties such as flexibility, aggregation kinetics, and susceptibility to enzymatic cleavage. The observed effects are explained by a model that considers the formation of chromium-associated intra- and intermolecular crosslinks. The obtained results provide novel insights into the effect of chromium salts on the conformation and properties of tropocollagen molecules.
    Matched MeSH terms: Collagen; Tropocollagen*
  18. Zhao Y, Lu K, Piao X, Song Y, Wang L, Zhou R, et al.
    Food Chem, 2023 May 01;407:135157.
    PMID: 36529012 DOI: 10.1016/j.foodchem.2022.135157
    Surimi products have unsatisfactory gel properties. Hence, this study evaluates the effect of collagen-adding on surimi gel properties and provides the first observation results regarding collagen type influence. With higher water solubility and more charged amino acids than type II, collagen type I intertwines with surimi myofibrillar proteins better to induce higher exposure of protein functional domains, more sufficient conformational changes of myosin and greater formation of chemical forces among proteins. These enhancements accelerate the gelation rate, leading to a well-stabilized surimi gel. The collagen I-containing surimi gels show more compact structures with uniformly distributed smaller pores than those containing collagen II, thereby providing the final products with higher water holding capacity and better textural profiles. As such, the surimi gel fortification performance of collagen I and the well-elucidated collagen-myofibrillar protein interaction mechanism will guide the further exploitation of collagen as an effective additive in the food industry.
    Matched MeSH terms: Collagen
  19. Aziz J, Ahmad MF, Rahman MT, Yahya NA, Czernuszka J, Radzi Z
    Int J Biol Macromol, 2018 Feb;107(Pt A):1030-1038.
    PMID: 28939521 DOI: 10.1016/j.ijbiomac.2017.09.066
    Successful use of tissue expanders depends on the quality of expanded tissue. This study evaluates the impact of anisotropic self-inflating tissue expander (SITE) on the biomechanics of skin. Two different SITE were implanted subcutaneously on sheep scalps; SITE that requires 30days for maximum expansion (Group A; n=5), and SITE that requires 21days for maximum expansion (Group B; n=5). Control animals (n=5) were maintained without SITE implantation. Young's Modulus, D-periodicity, overlap and gap region length, diameter, and height difference between overlap and gap regions on collagen fibrils were analyzed using atomic force microscopy. Histology showed no significant differences in dermal thickness between control and expanded skin of groups A and B. Furthermore, most parameters of expanded skin were similar to controls (p>0.05). However, the height difference between overlap and gap regions was significantly smaller in group B compared to both control and group A (p<0.01). Strong correlation was observed between Young's Modulus of overlap and gap regions of the control and group A, but not group B. Results suggest that a relatively slower SITE can be useful in reconstructive surgery to maintain the biomechanical properties of expanded skin.
    Matched MeSH terms: Collagen/ultrastructure; Collagen/chemistry*
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