Distribution of type I collagen in human kidney diseases in comparison with type III collagen

1990 ◽  
Vol 162 (2) ◽  
pp. 141-148 ◽  
Author(s):  
Kazuo Yoshioka ◽  
Machi Tohda ◽  
Tsukasa Takemura ◽  
Norihisa Akano ◽  
Kazunori Matsubara ◽  
...  
Keyword(s):  
Type I Collagen ◽  
Kidney Diseases ◽  
Human Kidney ◽  
Type Iii Collagen ◽  
Type I ◽  
Type Iii

Change in phenotype in long-term cultures of a clonal rat bone cell line: switch to the synthesis of α1 (I)-trimer collagen

1984 ◽  
Vol 62 (6) ◽  
pp. 462-469 ◽  
Author(s):  
Hardy Limeback ◽  
Kichibee Otsuka ◽  
Kam-Ling Yao ◽  
Jane E. Aubin ◽  
Jaro Sodek
Keyword(s):  
Collagen Synthesis ◽  
Type I Collagen ◽  
Bone Cell ◽  
Detectable Effect ◽  
Prostaglandin E ◽  
Intracellular Camp ◽  
Type Iii Collagen ◽  
Type I ◽  
Type Iii ◽  
Type V

A number of bone cell clones isolated from rat calvaria have been maintained in culture for more than 3 years. Several of these clones have undergone dramatic changes in phenotype. One of these clones, RGB 2.2, was observed originally to have a fibroblastic morphology in culture and to respond to parathyroid hormone (PTH), but not prostaglandin E2 (PGE2), with an increase in intracellular cAMP. Throughout several passages in early subcultures, these cells synthesized mostly type I collagen, with small amounts of type III and type V collagens. Whereas PTH had no detectable effect on collagen synthesis, PGE2 decreased the amount of total cell layer collagen, with the greatest effect on type III collagen, while increasing the proportion of type V collagen. Subsequent studies on these cells during 3 years in culture have indicated changes in their phenotype including a progressive change in morphology to a more cuboidal shape and a change in collagen synthesis, the cells producing large amounts of the "embryonic" collagen, α1(I) trimer. The reason(s) for the change in collagen expression is unknown, but may be the result of a change in which gene(s) is being expressed.

scholarly journals PERITONEAL ADHESIONS TYPE I, III AND TOTAL COLLAGEN ON POLYPROPYLENE AND COATED POLYPROPYLENE MESHES: EXPERIMENTAL STUDY IN RATS

2017 ◽  
Vol 30 (2) ◽  
pp. 77-82 ◽  
Author(s):  
Lucas Félix ROSSI ◽  
Manoel Roberto Maciel TRINDADE ◽  
Armando José D`ACAMPORA ◽  
Luise MEURER
Keyword(s):  
Type I Collagen ◽  
Cell Types ◽  
Type Iii Collagen ◽  
Type I ◽  
Abdominal Adhesions ◽  
Peritoneal Adhesions ◽  
Type Iii ◽  
Total Collagen

ABSTRACT Background: Hernia correction is a routinely performed treatment in surgical practice. The improvement of the operative technique and available materials certainly has been a great benefit to the quality of surgical results. The insertion of prostheses for hernia correction is well-founded in the literature, and has become the standard of treatment when this type of disease is discussed. Aim: To evaluate two available prostheses: the polypropylene and polypropylene coated ones in an experimental model. Methods: Seven prostheses of each kind were inserted into Wistar rats (Ratus norvegicus albinus) in the anterior abdominal wall of the animal in direct contact with the viscera. After 90 days follow-up were analyzed the intra-abdominal adhesions, and also performed immunohistochemical evaluation and videomorphometry of the total, type I and type III collagen. Histological analysis was also performed with hematoxylin-eosin to evaluate cell types present in each mesh. Results: At 90 days the adhesions were not different among the groups (p=0.335). Total collagen likewise was not statistically different (p=0.810). Statistically there was more type III collagen in the coated polypropylene group (p=0.039) while type I was not different among the prostheses (p=0.050). The lymphocytes were statistically more present in the polypropylene group (p=0.041). Conclusion: The coated prosthesis was not different from the polypropylene one regarding the adhesion. Total and type I collagen were not different among the groups, while type III collagen was more present on the coated mesh. There was a greater number of lymphocytes on the polypropylene mesh.

scholarly journals A matrix metalloproteinase-generated neoepitope of CRP can identify knee and multi-joint inflammation in osteoarthritis

2021 ◽  
Vol 23 (1) ◽  
Author(s):  
Louie C. Alexander ◽  
Grant McHorse ◽  
Janet L. Huebner ◽  
Anne-Christine Bay-Jensen ◽  
Morten A. Karsdal ◽  
...  
Keyword(s):  
Synovial Fluid ◽  
Matrix Metalloproteinase ◽  
Type I Collagen ◽  
Joint Inflammation ◽  
Cartilage Degradation ◽  
Womac Pain ◽  
Type Iii Collagen ◽  
Type I ◽  
Radiographic Imaging ◽  
Type Iii

Abstract Objective To compare C-reactive protein (CRP) and matrix metalloproteinase-generated neoepitope of CRP (CRPM) as biomarkers of inflammation and radiographic severity in patients with knee osteoarthritis. Methods Participants with symptomatic osteoarthritis (n=25) of at least one knee underwent knee radiographic imaging and radionuclide etarfolatide imaging to quantify inflammation of the knees and other appendicular joints. For purposes of statistical analysis, semi-quantitative etarfolatide and radiographic imaging scores were summed across the knees; etarfolatide scores were also summed across all joints to provide a multi-joint synovitis measure. Multiple inflammation and collagen-related biomarkers were measured by ELISA including CRP, CRPM, MMP-generated neoepitopes of type I collagen and type III collagen in serum (n=25), and CD163 in serum (n=25) and synovial fluid (n=18). Results BMI was associated with CRP (p=0.001), but not CRPM (p=0.753). Adjusting for BMI, CRP was associated with radiographic knee osteophyte score (p=0.002), while CRPM was associated with synovitis of the knee (p=0.017), synovitis of multiple joints (p=0.008), and macrophage marker CD163 in serum (p=0.009) and synovial fluid (p=0.03). CRP correlated with MMP-generated neoepitope of type I collagen in serum (p=0.045), and CRPM correlated with MMP-generated neoepitope of type III collagen in serum (p<0.0001). No biomarkers correlated with age, knee pain, or WOMAC pain. Conclusions To our knowledge, this is the first time that CRPM has been shown to be associated with knee and multi-joint inflammation based on objective imaging (etarfolatide) and biomarker (CD163) measures. These results demonstrate the capability of biomarker measurements to reflect complex biological processes and for neoepitope markers to more distinctly reflect acute processes than their precursor proteins. CRPM is a promising biomarker of local and systemic inflammation in knee OA that is associated with cartilage degradation and is independent of BMI. CRPM is a potential molecular biomarker alternative to etarfolatide imaging for quantitative assessment of joint inflammation.

Type VI collagen induces cardiac myofibroblast differentiation: implications for postinfarction remodeling

2006 ◽  
Vol 290 (1) ◽  
pp. H323-H330 ◽  
Author(s):  
Jennifer E. Naugle ◽  
Erik R. Olson ◽  
Xiaojin Zhang ◽  
Sharon E. Mase ◽  
Charles F. Pilati ◽  
...  
Keyword(s):  
Cardiac Fibrosis ◽  
Type I Collagen ◽  
In Vivo Model ◽  
Type Iii Collagen ◽  
Type I ◽  
Myofibroblast Differentiation ◽  
Type Vi Collagen ◽  
Collagen Substrate ◽  
Type Iii

Cardiac fibroblast (CF) proliferation and differentiation into hypersecretory myofibroblasts can lead to excessive extracellular matrix (ECM) production and cardiac fibrosis. In turn, the ECM produced can potentially activate CFs via distinct feedback mechanisms. To assess how specific ECM components influence CF activation, isolated CFs were plated on specific collagen substrates (type I, III, and VI collagens) before functional assays were carried out. The type VI collagen substrate potently induced myofibroblast differentiation but had little effect on CF proliferation. Conversely, the type I and III collagen substrates did not affect differentiation but caused significant induction of proliferation (type I, 240.7 ± 10.3%, and type III, 271.7 ± 21.8% of basal). Type I collagen activated ERK1/2, whereas type III collagen did not. Treatment of CFs with angiotensin II, a potent mitogen of CFs, enhanced the growth observed on types I and III collagen but not on the type VI collagen substrate. Using an in vivo model of myocardial infarction (MI), we measured changes in type VI collagen expression and myofibroblast differentiation after post-MI remodeling. Concurrent elevations in type VI collagen and myofibroblast content were evident in the infarcted myocardium 20-wk post-MI. Overall, types I and III collagen stimulate CF proliferation, whereas type VI collagen plays a potentially novel role in cardiac remodeling through facilitation of myofibroblast differentiation.

Effects of Fractional CO2 Laser Treatment on Subglottic Scar in a Rabbit Model

2020 ◽  
pp. 019459982097825
Author(s):  
Kastley Marvin ◽  
Isaac Schwartz ◽  
Edward Utz ◽  
Justin Wilson ◽  
Christopher Johnson ◽  
...  
Keyword(s):  
Laser Treatment ◽  
Type I Collagen ◽  
Medical Center ◽  
Academic Medical Center ◽  
Rabbit Model ◽  
Study Endpoint ◽  
Type Iii Collagen ◽  
Type I ◽  
Respiratory Complications ◽  
Type Iii

Objective The objective of this study was to investigate the effects of fractional CO2 laser on subglottic scar. Study Design Randomized controlled animal study. Setting Academic medical center. Methods Subglottic scar was induced in 12 New Zealand white rabbits via an endoscopic brush technique. This was followed by an open airway surgery that included vertical division of the cricoid and proximal trachea. Eight rabbits underwent fractional CO2 laser treatment of the scar via a Lumenis Ultrapulse Deep FX handpiece. Four rabbits underwent the open surgical approach without laser treatment. Bronchoscopy was performed at weeks 1, 2, 4, and 8. The animals were euthanized and laryngotracheal complexes harvested 12 weeks postsurgery. Immunohistochemistry was performed to determine the collagen composition of treated and untreated scars. Results All 12 subjects survived to the study endpoint with no significant respiratory complications, despite 10 of 12 developing some degree of lateral tracheal narrowing. The median ratio of type I collagen to type III collagen in the laser group (1.57) was significantly more favorable than that of the untreated group (2.84; P = .03). Conclusion Treatment with fractional CO2 laser appears to have similar effects on subglottic scars as with cutaneous scars, improving the ratio of type I to type III collagen. Additionally, we developed an open airway approach in the rabbit model to deliver fractional CO2 laser treatment to the subglottis without introducing respiratory complications or compromising survival.

scholarly journals Separation of the Binding Step from the Collagen Platelet Reaction

1977 ◽  
Author(s):  
P.L. Kronick ◽  
S.A. Jimenez
Keyword(s):  
Type I Collagen ◽  
Specific Activity ◽  
Adenine Nucleotides ◽  
High Specific Activity ◽  
Type Iii Collagen ◽  
Type I ◽  
Type Iii ◽  
Valid Comparison ◽  
Platelet Reaction

Determination of activity of most agents in stimulating platelets to aggregate or release adenine nucleotides is conveniently done by titrating the platelet reaction with the agent. Platelets have previously been titrated with different types of collagen (types I, II, and III) in this way to compare the activities of the collagens. It has been concluded that the order of activity is type III>I>II. Whether this order is due to differences in binding was not obvious from these experiments because the binding was not determined directly. We have developed a method of comparing activities by measuring the targeted dose for each point in the titration - the amount of collagen which actually binds to platelets. The collagens used in these experiments were prepared in vitro from embryonic chick tissue to give labelled products of extremely high specific activity without structural alteration. We find that type I collagen is at least 20 times as active as previously reported, and that the activity of Type III collagen is not significantly higher when the amounts bound are taken into account. The fraction of the labelled tendon collagen which was bound to platelets was identified as type I by its hydroxyproline/proline ratio. Direct measurement of the bound fraction in dose-response studies is required for valid comparison of collagen activities.

Influence of dermal equivalent maturation on the development of a cultured skin equivalent

1992 ◽  
Vol 70 (1) ◽  
pp. 34-42 ◽  
Author(s):  
Véronique Bouvard ◽  
Lucie Germain ◽  
Pierre Rompré ◽  
Brigitte Roy ◽  
François A. Auger
Keyword(s):  
Type I Collagen ◽  
Epidermal Cells ◽  
Skin Equivalent ◽  
Type Iii Collagen ◽  
Second Phase ◽  
Type I ◽  
Dermal Equivalent ◽  
Type Iii ◽  
Skin Equivalents ◽  
Dermal Equivalents

Histologic and immunofluorescence methods were used to analyse the presence of fibronectin, chondroitin-4-sulphate and chondroitin-6-sulphate, type III and IV collagens, laminin, and keratins to assess the maturation level of cultured dermal and skin equivalents. In a first phase, fibroblasts in monolayer culture were compared with dermal equivalents in which fibroblasts are embedded in a type I collagen gel. Different fluorescent patterns were observed depending on the culture system used. A sequential appearance of macromolecules was noticed in dermal equivalents. Fibronectin was first detected after 4 days of culture, whereas chondroitin-4-sulphate and chondroitin-6-sulphate and type III collagen were present after 7 days. In contrast, all three macromolecules were detected at 24 h of culture in fibroblastic monolayer cultures. In a second phase, the quality of our skin equivalents was evaluated according to the seeding time of epidermal cells upon dermal equivalents (1, 4, or 7 days). A satisfactory stratification was obtained when keratinocytes were seeded after 4 and 7 days of dermal equivalent culture. Laminin and fibronectin were detected at the dermo-epidermal junction, but type IV collagen was absent. Various keratins, as detected by the AE1, AE2, and AE3 antibodies, were present in the epidermal layer. Following keratinocyte confluence, a change in the organization pattern of type III collagen in the dermal fraction of the skin equivalent was also noticed. Our comparative results show that seeding of epidermal cells on a more mature dermal equivalent leads to improved differentiation status of the epidermal layer.Key words: collagen lattice, fibroblast, skin equivalent, dermal equivalent, maturation.

scholarly journals Antiaging Properties of Exosomes from Adipose-Derived Mesenchymal Stem Cells in Photoaged Rat Skin

2020 ◽  
Vol 2020 ◽  
pp. 1-13
Author(s):  
Jun-Xian Liang ◽  
Xuan Liao ◽  
Sheng-Hong Li ◽  
Xiao Jiang ◽  
Ze-Hua Li ◽  
...  
Keyword(s):  
Stem Cells ◽  
Mrna Expression ◽  
Real Time ◽  
Type I Collagen ◽  
Ultraviolet B ◽  
Type Iii Collagen ◽  
Type I ◽  
Type Iii ◽  
Photoaged Skin ◽  
Dermal Thickness

Adipose-derived stem cells (ADSCs) have been documented as possible candidates for skin rejuvenation. However, the effects of ADSC-derived exosomes on photoaged skin remain to be fully elucidated. This study was aimed at determining the antiaging effects of ADSC-derived exosomes on photoaged skin. Human ADSCs were isolated from the adipose tissue of healthy women and cultured in vitro. Then, exosomes were extracted from the cultured ADSCs, purified by ultracentrifugation, and verified by examination of cell morphology using transmission electron microscopy and the identification of specific biomarkers. Meanwhile, the optimal exosome concentration and treatment time were selected. The photoaged skin model was created by subjecting Sprague-Dawley rats to ultraviolet B radiation. Exosomes were injected into the photoaged skin in a single therapeutic dose. The thickness of the epidermis and dermis was observed by HE staining. The relative mRNA expression of type I collagen, type III collagen, and matrix metalloproteinases (MMP-1 and MMP-3) was determined by real-time PCR. In the rat model of photoaged skin, the injected exosomes markedly decreased the epidermal thickness and increased the dermal thickness of the photoaged skin 7 days after treatment. Moreover, the proportion of the stratum corneum of the epidermis was decreased. Furthermore, real-time RT-PCR showed that the mRNA expression of type I collagen was increased and that of type III collagen, MMP-1, and MMP-3 was decreased. Our results demonstrate that ADSC-derived exosome treatment could significantly improve skin photodamage and that ADSC-derived exosomes may be a potential agent for photoaged skin treatment.

Differential expression of type I and type III collagen genes during tooth development

Development ◽  
1991 ◽  
Vol 111 (3) ◽  
pp. 691-698
Author(s):  
M.B. Andujar ◽  
P. Couble ◽  
M.L. Couble ◽  
H. Magloire
Keyword(s):  
Gene Expression ◽  
Type I Collagen ◽  
Tooth Development ◽  
Expression Patterns ◽  
Type Iii Collagen ◽  
Type I ◽  
Collagen Gene ◽  
Type Iii ◽  
Collagen Gene Expression ◽  
Collagen Genes

Collagen gene expression during mouse molar tooth development was studied by quantitative in situ hybridization techniques. Different expression patterns of type I and type III collagen mRNAs were observed in the various mesenchymal tissues that constitute the tooth germ. High concentration for pro-alpha 1(I) and pro-alpha 2(I) collagen mRNAs were found within the osteoblasts. We found that the cellular content of type I collagen mRNAs in the odontoblasts varies throughout the tooth formation: whereas mRNA concentration for pro-alpha 1(I) collagen decreases and that of pro-alpha 2(I) increases, during postnatal development. Moreover, different amounts of pro-alpha 1(I) and pro-alpha 2(I) collagen mRNAs were observed in crown and root odontoblasts, respectively. Type III collagen mRNAs were detected in most of the mesenchymal cells, codistributed with type I collagen mRNAs, except in odontoblasts and osteoblasts. Finally, this study reports differential accumulation of collagen mRNAs during mouse tooth development and points out that type I collagen gene expression is regulated by distinct mechanisms during odontoblast differentiation process. These results support the independent expression of the collagen genes under developmental tissue-specific control.

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