PURPOSE: Fibrillar collagens like type I collagen, are the major constituent of the extracellular matrix and structural protein of bone. Also, it can be a scaffold for osteoblast migration. The purpose of this study is to estimate the effects of absorbable atelo-collagen sponge(Teruplug(R), Terumo biomaterials Co., Tokyo, Japan) insertion in tooth extraction sites on periodontal healing of the second molar, healing of the fractured mandibular bone and new bone formation of third molar socket after the extraction of the impacted third molar with mandibular angle fracture. METHODS: In our study of six cases of mandibular angle fractures, all of them underwent the extraction of the third molar tooth & absorbable atelo-collagen sponge insertion in tooth extraction site. Three of them had a intraoral infection & oral opening to fracture site, two of the six had dental caries, and only one had reduction problem due to third molar position. Six consecutive patients with non-comminuted fractures of the mandibular angle were treated by open reduction and internal fixation using one non-compression miniplates and screws placed through a transoral incision. RESULTS: All of the patients have showed good postoperative functions and have not experienced complications requiring second surgical intervention. There was well healing of the mandibular bone and the most new bone formation of third molar socket after the extraction of the impacted third molar with mandibular angle fracture. CONCLUSION: The results of this study suggest that absorbable atelo-collagen sponge is relatively favorable bone void filler with prevention of tissue collapse, food packing, and enhance periodontal healing. Thus, the use of atelo-collagen sponge and one noncompression miniplate seems to be relatively easy, safe, and effective for the treatment of fractures of the mandibular angle and third molar extraction.
Biocompatible Materials ; Collagen ; Collagen Type I ; Dental Caries ; Extracellular Matrix ; Fibrillar Collagens ; Humans ; Mandible ; Molar ; Molar, Third ; Osteoblasts ; Osteogenesis ; Porifera ; Tokyo ; Tooth ; Tooth Extraction

Solar ultraviolet (UV) irradiation leads to distinct changes in the skin connective tissues by degradation of collagen, which is a major structural component in the extracellular matrix. UV irradiation induces the production of matrix metalloproteinases (MMP) capable of attacking native fibrillar collagen and responsible for inhibiting the construction of collagenous extracellular matrix. In this study, we attempted to investigate the protective actions of Rubus coreanus ethanol extract (RCE) on the MMP production and the consequent procollagen/collagen degradation in UV-B-irradiated human dermal fibroblasts. The analytical data showed that Rubus coreanus ethanol extract was mostly comprised of cyanidin 3-rutinoside. Pre-treatment of fibroblasts with this extract inhibited UV-B-induced production of MMP-1, MMP-8 and MMP-13 in dose-dependent manners. In addition, Western blot analysis and immunocytochemical staining assay revealed that RCE markedly augmented the cellular levels of procollagen/collagen declined in UV-B-exposed dermal fibroblasts. These results demonstrate that RCE blocks UV-B-induced increase of the collagen degradation by inhibiting MMP production. Thus, RCE may act as an agent inhibiting excessive dermal collagen degradation leading to the skin photoaging.
Blotting, Western ; Collagen* ; Connective Tissue ; Ethanol* ; Extracellular Matrix* ; Fibrillar Collagens ; Fibroblasts* ; Humans* ; Matrix Metalloproteinases ; Skin

PURPOSE: To investigate of the histological characteristics of the lattice degeneration of the human peripheral retina. METHODS: The histological characteristics of the lattice degeneration of the retina was checked by flat preparation and serial section of the lattice lesion in three eyes was investigated by transmission electron microscopy. RESULTS: Flat preparation showed lattice lesion with a hole at the lateral margin with overlying sclerotic vessel and pigment clumping within the lesion. The ultrastructural initial findings showed that the collagen filament in the vitreous cavity was continuous with Muller fiber of the retina with the defect of the inner retina. The full-thikness defect of the sensory retina leaded to the retinal hole. The vascular wall was replaced and occluded by fine fibrillar collagen. The glial cell proliferated into the neural tissue of the sensory retina. These glial cells may secrete long spacing collagen (LSC) and curvilinear material shown at the area of the sensory retinal defect and near the vitreoretinal interface. CONCLUSIONS: These results suggest that the thinning of the retina occurs from the inner retina leading to retinal hole as the lattice degeneration progresses. LSC and curvilinear material are suggestive of derivatives derived from the extracellular material secreted from the glial cell.
Collagen ; Fibrillar Collagens ; Humans ; Microscopy, Electron ; Microscopy, Electron, Transmission ; Neuroglia ; Retina* ; Retinal Perforations ; Retinaldehyde*

Many researches have been reported that collagen as cellular stroma, matrix of grafting materials, mediator of agents for the purpose of promoting healing process in vivo, but the responses in vivo were seen various. The goal of this experiment is to assess the effect of collagen on bony healing, through histological evaluation of implanted collagen on the calvarial defect in rats. 2-month-old Sprague-Dawley, 24 rats were used and 12 rats assigned to each group of control and test. Defect of 5mm in diameter was made on the calvarial bone with trephine bur. Following thorough saline rinse, defect of control group was left in empty and that of experimental group was filled with fibrillar collagen(COLLATAPE(R), COLLA-TEC. INC. U.S.A.) soaked in saline. 3 rats in each group were sacrificed at 3, 7, 14, 21 days after operation respectively, and the tissue blocks were prepared for light microscope with H-E for evaluation of overall healing, with TRAP(tartrate resistant acid phosphatase) for evaluation of osteoclastic activity and with immunohistochemical staining for macrophages. The results were as follows: 1. In the control group, inflammatory responses were disappeared at day 14, but, in the experimental group inflammatory infiltrates were reduced at day 21. Thus, the experimental group showed more severe soft tissue inflammation than control group. 2. Both control and experimental group showed slight appositional growth at day 7 and gradual bony growth to 21th day. But, complete bony healing of the defect was not shown. There was no significant difference in bony healing between control and experimental group 3. Specific response of macrophages for implanted collagen was observed at day 14 in the experimental group. In conclusion, although fibrillar collagen caused inflammation of soft tissue during initial healing period, inflammatory responses by fibrillar collagen didn't inhibit bony regeneration and implanted collagen was biodegradaded by macrophages. Thus, we expect that fibrillar collagen can be used for useful mediator of graft materials or growth factors.
Animals ; Collagen ; Fibrillar Collagens* ; Humans ; Infant ; Inflammation ; Intercellular Signaling Peptides and Proteins ; Macrophages ; Osteoclasts ; Rats* ; Rats, Sprague-Dawley ; Regeneration ; Transplants

We observed the structure and form of adult annulus fibrosus of lumbar intervertebral disc at the fibrous layer level. The annulus fibrosus of lumbar interverbral disc was delaminated by using microsurgical technique. 8 testing points were taken in each layer and the angles between their fibers going and horizontal plane were measured. The results showed that the fiber going angle at each measurement point continually increased with the increase of fibrous layer from outside to inside along the radial direction in horizontal plane. The least fiber going angle was 25 degrees - 30 degrees. The fiber going angle at the same layer gradually increased from front to back. The fiber going angle was 70 degrees - 90 degrees at the middle of the back of annulus fibrosus of lumbar interverbral disc. The fiber going was consistent with the posterior longitudinal ligament going. Through the normalized equation and normalized line, the fiber going angle at any point in any layer could be obtained conveniently. We also observed that the annuli fibrosus were interlaced in the front, left and right of annulus fibrosus of lumbar intervertebral disc. And there were more interlaced areas in local sides of lumbar intervertebral disc, but there was no interlaced areas between layers near the middle of posterior annulus fibrosus. So we came to the conclusion: Annulus fibrosus of lumbar intervertebral disc has a special micro-structure in adaptation with its function.
Adult ; Compressive Strength ; Fibrillar Collagens ; physiology ; Humans ; Intervertebral Disc ; anatomy & histology ; physiology ; Lumbar Vertebrae ; anatomy & histology ; Male ; Middle Aged

Minor fibrillar collagen types V and XI, are those less abundant than the fibrillar collagen types I, II and III. The alpha chains share a high degree of similarity with respect to protein sequence in all domains except the variable region. Genomic variation and, in some cases, extensive alternative splicing contribute to the unique sequence characteristics of the variable region. While unique expression patterns in tissues exist, the functions and biological relevance of the variable regions have not been elucidated. In this review, we summarize the existing knowledge about expression patterns and biological functions of the collagen types V and XI alpha chains. Analysis of biochemical similarities among the peptides encoded by each exon of the variable region suggests the potential for a shared function. The alternative splicing, conservation of biochemical characteristics in light of low sequence conservation, and evidence for intrinsic disorder, suggest modulation of binding events between the surface of collagen fibrils and surrounding extracellular molecules as a shared function.
Alternative Splicing ; genetics ; Animals ; Fibrillar Collagens ; chemistry ; genetics ; metabolism ; Humans ; Sulfates ; chemistry ; metabolism ; Surface Properties ; Tyrosine ; analogs & derivatives ; chemistry ; metabolism

BACKGROUND: This study tried to compare the morphological changes of collagen fibrils between disused and denervated old rat Achilles tendons with those of young rats through quantitative analyses of collagen fibril diameters by transmission electron microscopy (TEM). METHODS: Old (18 months old) and young (6 months old) male Sprague-Dawley rats were divided into 3 groups (n=8 in each group): a control group, a complete denervation group for 4 weeks after the transection of the right sciatic nerve, and a disuse group with hindlimb unweighing by tail suspension. Each explanted Achilles tendon was used for TEM observation. Under TEM, quantitative analyses of collagen fibril diameters were performed. RESULTS: All groups comprising old rats had smaller mean diameters and showed more left-shifted distribution of collagen fibril diameters than young rats. In particular, the disuse group of old rats showed a more prominent mean fibril diameter decrease than young rats. CONCLUSION: Disuse might cause a more prominent decrease of collagen fibril size in the old than the young.
Achilles Tendon ; Aged ; Animals ; Collagen ; Denervation ; Fibrillar Collagens ; Hindlimb ; Hindlimb Suspension ; Humans ; Male ; Microscopy, Electron, Transmission ; Rats ; Rats, Sprague-Dawley ; Sciatic Nerve

Local or distant flap surgery has been applied in the soft tissue defect area where bone and tendon are exposed, but there are many pitfalls in these surgeries including limitation of donor site selection, as well as functional and aesthetic dissatisfaction of the donor and recipient site. So these problems have facilitated the development and study of skin substitute (artificial dermis). The history of artificial skin began in the 1980s with the invention of Stage I membrane by Yannas and Burke. Since then it has been developed and applied to chinical cases of extensive burn injury and soft tissue defect. In 1989, and artificial dermis (Terudermis) composed of fibrillar collagen and heat denaturated atelocollagen was developed by Konish. It has the advantage of allowing early-incorporation of cellular and vascular components into its collagen sponge, as well as dehydrothermal cross-linking, which is very weak. This study included 18 consecutive cases which underwent application of artificial dermis on bone and tendon from January 1997 to November 1998. The exposed areas were the result of trauma in 10 cases, postoperative complications in 2 cases, and other causes in 6 cases. The follow-up period ranged from 3 months to 18 months, averaging 11 months. A week after wound debridement and Terudermis application, neovascularization had begun and granulation tissue appeared aften 2-3 weeks. Then the split or full -thickness skin graft was secondarily applied resulting in the production of sufficient skin. In conclusion, Terudermis application to an area of exposed bone and tendon is a very useful method, especially when primary local or distant flap surgery cannot be used. This method is very simple, convenient and reliable.
Burns ; Collagen ; Debridement ; Dermis ; Fibrillar Collagens ; Follow-Up Studies ; Granulation Tissue ; Hot Temperature ; Humans ; Inventions ; Membranes ; Porifera ; Postoperative Complications ; Skin ; Skin, Artificial ; Tendons* ; Tissue Donors ; Transplants ; Wounds and Injuries

Formation of dermal collagen fiber is a complicated and sequential process with the progressive assembly of collagen. Collagen monomers form stepped and orderly protofibrils through longitudinal displacement. Subsequently, protofibrils or protofibrils and collagen are bonded by covalent bonds to form orderly lamellar structure of collagen fibers. Then collagen fibers are tightly wound into coarse collagen fiber bundles by covalent crosslinking. Decorin is a multifunctional small leucine-rich proteoglycan. It can prevent the aggregation of protofibrils by binding to the specific site of collagen with its core protein, and adjusting the spacing between the protofibrils with its glycosaminoglycan chain. Thus, by effecting the formation of collagen fibers with regulation of collagen assembly, decorin may help prevent scar formation and even promote regeneration.
Collagen ; Decorin ; metabolism ; Extracellular Matrix ; Extracellular Matrix Proteins ; metabolism ; pharmacology ; Fibrillar Collagens ; metabolism ; ultrastructure ; Fibrin ; metabolism ; Humans ; Microfibrils ; metabolism ; Proteoglycans ; metabolism ; pharmacology

Objective: To investigate the expression and function of collagen type ⅩⅦ α1 (COL17α1) in aging mouse skin and its effect on the stemness and proliferation of human epidermal stem cells (ESCs), and to explore the mechanism of related microRNA (miR) in intervening the expression of COL17α1 of human ESC. Methods: The method of experimental research was used. Twelve 2-month-old (young) and twelve 24-month-old (aged) male C57BL/6J mice were selected, and full-thickness skin samples from their upper back were taken for follow-up detection. After hematoxylin-eosin staining of the full-thickness skin samples of young mice and aged mice, the structure of the epidermis was observed and the thickness of the epidermis was measured; the morphology of epidermal basement membrane and hemidesmosomes were observed by transmission electron microscopy, and the hemidesmosomes were counted; the mRNA and protein expressions of COL17α1 were detected by real-time fluorescent quantitative reverse transcription polymerase chain reaction (RT-PCR) and Western blotting respectively, and the protein expression and distribution of COL17α1 was observed and detected by immunofluorescence method. The fresh foreskin tissue discarded after surgery was obtained from 3 healthy men aged 20-30 years who underwent circumcision at the Fourth Medical Center of PLA General Hospital, ESCs were extracted and well-grown cells were wsed for follow-up experiments. According to the random number table (the same grouping method below), ESCs were divided into blank control group, transfection reagent control group, empty vector plasmid group, and COL17α1 knockdown plasmid group with corresponding treatment. After 48 hours of culture, the mRNA expression of COL17α1 was detected by real-time fluorescent quantitative RT-PCR, the protein expressions of COL17α1 and cytokeratin 14 (CK14) were detected by Western blotting, and the cell proliferation level was detected by cell counting kit 8. miRs that might act on the 3' non-coding region of <i>COL17α1i> mRNA were screened through DIANA, miRTarBase, miRNAMap, TargetScan, and microRNA databases. The ESCs were divided into negative control group transfected with miR mimic negative control and each miR mimic group transfected with each of the previously screened miR mimics. Forty-eight hours after transfection, the protein expression of COL17α1 was detected by Western blotting. Based on the sequencing data set GSE114006 in Gene Expression Omnibus (GEO), the GEO2R tool was used to statistically analyze the expression of the previously screened miRs that could cause the reduction of COL17α1 protein expression in the skin of 30 young (18-25 years old) and 30 elderly (>70 years old) human skins. The full-thickness skin samples of young mice and aged mice were taken, and the expressions of increased miRs in the aforementioned aged human skin were detected by real-time fluorescent quantitative RT-PCR. Two batches of human ESCs were taken, the first batch was divided into COL17α1 wild type+miR-203b-3p negative control group and COL17α1 wild type+miR-203b-3p mimic group, and the second batch was divided into COL17α1 mutant+miR-203b-3p negative control group and COL17α1 mutant+miR-203b-3p mimic group. Each group of ESC was transfected with corresponding sequences respectively. Forty-eight hours later, the luciferase reporter gene detection kit was used to detect the gene expression level of COL17α1. The number of samples in the tissue experiment was 6, and the number of samples in the cell experiment was 3. Data were statistically analyzed with independent sample <i>ti> test, one-way analysis of variance, least significant difference test or Dunnett's test, Mann-Whitney <i>Ui> test or Kruskal-Wallis <i>Hi> test. Results: Compared with those of young mice, the boundary between the epidermis and the dermis of the aged mice skin was blurred and the cell layers were less, and the thickness of epidermis was significantly thinner (<i>Zi>=-2.88, <i>Pi><0.01); the morphology of basement membrane was discontinuous, with less unevenly distributed hemidesmosomes at the epidermis-dermis junction, and the number of hemidesmosomes was significantly reduced (<i>Zi>=-2.91, <i>Pi><0.01); the mRNA and protein expression levels of COL17α1 in the skin of aged mice were significantly decreased (with <i>ti> values of 10.61 and 6.85, respectively, <i>Pi><0.01). Compared with those of young mice, the protein expression of COL17α1 in the basal layer of epidermis and the bulb of hair follicle in the skin of aged mice was significantly decreased (<i>Zi>=-2.24, <i>Pi><0.05). After 48 hours of culture, the protein expression levels of COL17α1 in ESCs of blank control group, transfection reagent control group, empty vector plasmid group, and COL17α1 knockdown plasmid group were 1.00±0.27, 1.12±0.21, 1.13±0.23, and 0.42±0.18, respectively. Compared with those of blank control group, the mRNA and protein expression levels of COL17α1, the protein expression level of CK14, and the proliferation level of ESCs in transfection reagent control group and empty vector plasmid group did not change significantly (<i>Pi>>0.05), while these indexes in COL17α1 knockdown plasmid group were significantly decreased (<i>Pi><0.05 or <i>Pi><0.01). miR-203a-3p, miR-203b-3p, miR-512-5p, miR-124-3p, miR-28-5p, miR-590-3p, and miR-329-5p might bind to the 3' non-coding region of <i>COL17α1i> mRNA. Forty-eight hours after transfection, compared with 1.000±0.224 in negative control group, the protein expression level of COL17α1 in ESCs of miR-329-5p mimic group, miR-203b-3p mimic group, and miR-203a-3p mimic group decreased significantly (0.516±0.188, 0.170±0.025, and 0.235±0.025, with <i>ti> values of 3.17, 5.43, and 5.07, respectively, <i>Pi><0.05 or <i>Pi><0.01). Only the expression level of miR-203b-3p in the skin of the elderly was significantly higher than that of the young (<i>ti>=3.27, <i>Pi><0.01). The expression level of miR-203b-3p in the skin of aged mice was significantly higher than that of young mice (<i>Zi>=-2.88, <i>Pi><0.01). Forty-eight hours after transfection, the gene expression level of COL17α1 in ESCs of COL17α1 wild type+miR-203b-3p mimic group was significantly lower than that of COL17α1 wild type+miR-203b-3p negative control group (<i>ti>=7.66, <i>Pi><0.01). The gene expression level of COL17α1 in ESCs of COL17α1 mutant+miR-203b-3p mimic group was similar to that of COL17α1 mutant+miR-203b-3p negative control group (<i>Pi>>0.05). Conclusions: The mRNA and protein expression levels of COL17α1 decrease with age increasing in mice, which may lead to the detachment of mouse ESC from the epidermal basement membrane. Decreased expression of COL17α1 can inhibit the expression of CK14 and ESC proliferation, which may be responsible for the thinning of the epidermis and slower wound healing in aged human skin. The increased expression of miR-203b-3p in aged mouse skin can target and bind to the 3' non-coding region of <i>COL17α1i> mRNA, hindering the post-transcriptional translation process, thus resulting in decreased COL17α1 protein expression.
Adolescent ; Adult ; Aged ; Animals ; Autoantigens ; Humans ; Keratin-14 ; Male ; Mice ; Mice, Inbred C57BL ; MicroRNAs/genetics* ; Non-Fibrillar Collagens/pharmacology* ; Polyesters ; RNA, Messenger ; Skin Aging ; Stem Cells ; Young Adult