scholarly journals Specific immunohistochemical localization of osteonectin and collagen types I and III in fetal and adult porcine dental tissues.

1985 ◽  
Vol 33 (6) ◽  
pp. 531-540 ◽  
Author(s):  
P S Tung ◽  
C Domenicucci ◽  
S Wasi ◽  
J Sodek
Keyword(s):  
Periodontal Ligament ◽  
Type I Collagen ◽  
Alveolar Bone ◽  
Type Iii Collagen ◽  
Similar Distribution ◽  
Type I ◽  
Collagen Types ◽  
Type Iii ◽  
Dental Tissues ◽  
Strong Staining

Affinity-purified antibodies have been used in combination with the peroxidase-antiperoxidase technique to study the distribution of osteonectin and collagen types I and III in porcine dental tissues. Tissue sections (2 mm thick), including unerupted (fetal) or erupted (adult) teeth, were fixed in periodate-lysine-paraformaldehyde, demineralized in 12% w/v ethylenediaminetetraacetic acid, and after embedding, 6 micron sections were prepared for immunolocalization. Strong staining for osteonectin was observed in dentine of unerupted teeth and in the associated alveolar bone. Light to moderate staining was observed in the dental pulp, stratum intermedium, stellate reticulum, and the reticular elements in the endosteal spaces. In erupted teeth, osteonectin staining in dentine was concentrated around dentinal tubules and the associated alveolar bone stained with variable intensity. Cementum was poorly stained. However, the periodontal ligament and reticular material in the endosteal spaces showed moderate to strong staining. Weaker staining was apparent in the pulp and lamina propria of the gingiva. In comparison, type I collagen showed a similar distribution to osteonectin in both fetal and adult tissues, whereas type III collagen was generally restricted to the periodontal ligament, reticular elements of the endosteal spaces, and Sharpey's fibers in bone and cementum. Both odontoblast and ameloblast layers in fetal tissues stained for osteonectin and type III collagen.

scholarly journals Specific immunohistochemical localization of type III collagen in porcine periodontal tissues using the peroxidase-antiperoxidase method.

1980 ◽  
Vol 28 (11) ◽  
pp. 1215-1223 ◽  
Author(s):  
H M Wang ◽  
V Nanda ◽  
L G Rao ◽  
A H Melcher ◽  
J N Heersche ◽  
...  
Keyword(s):  
Bone Tissue ◽  
Type I Collagen ◽  
Alveolar Bone ◽  
Immunohistochemical Localization ◽  
Type Iii Collagen ◽  
Type I ◽  
Connective Tissues ◽  
Type Iii ◽  
Dental Tissues ◽  
Periodontal Tissues

Specific antibodies to porcine gingival type III collagen were raised in sheep. After purification on collagen affinity columns the antibodies were used for immunohistochemical localization of type III collagen in porcine periodontal and dental tissues employing the peroxidase-antiperoxidase (PAP) procedure. The extent of staining of the periodontal tissues was found to approximate the amount of type III collagen measured biochemically. A fairly uniform distribution of type III collagen was observed in the periodontal ligament and gingiva with more intense staining often being associated with blood vessels. A regular pattern of weakly staining fibers could be demonstrated throughout the cementum and in parts of the alveolar bone tissue. In addition, occasional sites in the cementum having a different morphological appearance from the rest of the cementum exhibited bundles of positively stained fibers. Although the bone tissue was essentially unstained, fibers in the endosteal spaces stained strongly. Sharpey's fibers passing from the soft connective tissues into alveolar bone and cementum also stained strongly. Three distinct arrangements of collagen fibers stained by the type III collagen antibodies could be identified: first, a reticular pattern, which was seen at the junction of the gingival epithelium and connective tissue, and in the endosteal spaces and dental pulp; second, a more diffuse pattern of fibers intermingled with type I collagen in the soft connective tissues; and third, a coating of some Sharpey's fibers, having a core believed to be type I collagen, and of fibers in the cementum inclusions.

scholarly journals Connective tissue of rat lung. II: Ultrastructural localization of collagen types III, IV, and VI.

1988 ◽  
Vol 36 (9) ◽  
pp. 1167-1173 ◽  
Author(s):  
P S Amenta ◽  
J Gil ◽  
A Martinez-Hernandez
Keyword(s):  
Type I Collagen ◽  
Ultrastructural Localization ◽  
Basement Membranes ◽  
Type Iii Collagen ◽  
Similar Distribution ◽  
Type I ◽  
Rat Lung ◽  
Collagen Types ◽  
Type Iii ◽  
Type Iv

We localized collagen types III, IV, and VI in normal rat lung by light and electron immunohistochemistry. Type IV collagen was present in every basement membrane examined and was absent from all other structures. Although types III and VI had a similar distribution, being present in the interstitium of major airways, blood vessels, and alveolar septa, as in other organs, they had different morphologies. Type III collagen formed beaded fibers, 15-20 nm in diameter, whereas type VI collagen formed fine filaments, 5-10 nm in diameter. Both collagen types were found exclusively in the interstitium, often associated with thick (30-35 nm) cross-banded type I collagen fibers. Occasionally, type III fibers and type VI filaments could be found bridging from the interstitium to the adventitial aspect of some basement membranes. Furthermore, the association of collagen type VI with types I and III and basement membranes suggests that type VI may contribute to integration of the various components of the pulmonary extracellular matrix into a functional unit.

scholarly journals Collagen heterogeneity and quantification in developing bovine nuchal ligament

1984 ◽  
Vol 220 (2) ◽  
pp. 385-394 ◽  
Author(s):  
C A Chambers ◽  
C A Shuttleworth ◽  
S Ayad ◽  
M E Grant
Keyword(s):  
Type I Collagen ◽  
Type Iii Collagen ◽  
Type I ◽  
Collagen Types ◽  
Constant Amount ◽  
Foetal Development ◽  
Type Iii ◽  
Major Species ◽  
Cnbr Cleavage ◽  
Nuchal Ligament

The collagenous components were investigated in peptic digests of developing bovine nuchal ligament. Types I and III collagen were the major species isolated, but the presence of types IV, V and VI was also shown. Changes in the pepsin-susceptibility of nuchal ligament during foetal development were observed. CNBr-cleavage peptide analysis indicated that type I collagen became cross-linked rapidly, as evidenced by the lack of alpha 1(I)CB6. At present it is not clear if this decrease in pepsin-susceptibility is due to cross-linking of collagen, to increased deposition of elastin, or to both. Quantification of collagen types I and III was shown to depend on the method used. When pepsin-solubilized material was examined an apparent increase in type III collagen with respect to foetal age was observed, whereas when CNBr digests of intact ligament were examined a relatively constant amount of type III collagen (approx. 24%) was found. The constant amount of type III collagen observed during foetal development changed at birth and increased in mature nuchal ligament to represent approx. 45% of the total collagen.

scholarly journals Platelet-aggregating activity of type I and type III collagens from human aorta and chicken skin

1976 ◽  
Vol 160 (3) ◽  
pp. 647-651 ◽  
Author(s):  
M J Barnes ◽  
J L Gordon ◽  
D E MacIntyre
Keyword(s):  
Type I Collagen ◽  
Human Aorta ◽  
Type Iii Collagen ◽  
Type I ◽  
Collagen Types ◽  
Type Iii ◽  
Disulphide Bonds ◽  
Chicken Skin ◽  
Human Collagen ◽  
Free Plasma

Human or chicken type III collagen dissolved in 0.1 M-acetic acid was much more potent than type I collagen at inducing platelet aggregation. After incubation in 0.38M-Na2HPO4 to promote fibrillogenesis, the platelet-aggregating activity of both collagen types increased, and type I was then virtually equiactive with type III. Preincubation in cell-free plasma increased the activity of chicken but not that of human collagen. The platelet-aggregating activity of type III collagen did not appear to depend on the integrity of the intrachain disulphide bonds.

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.

Has collagen a role in muscle pattern formation in the developing chick wing?

Development ◽  
1980 ◽  
Vol 60 (1) ◽  
pp. 245-254
Author(s):  
G. B. Shellswell ◽  
A. J. Bailey ◽  
V. C. Duance ◽  
D. J. Restall
Keyword(s):  
Type I Collagen ◽  
Immunofluorescence Microscopy ◽  
Microscopy Study ◽  
Type Iii Collagen ◽  
Type I ◽  
Embryonic Chick ◽  
Collagen Types ◽  
Developing Muscle ◽  
Ventral Muscle

We have used antibodies to three of the isomorphic forms of collagen, types I, III and V, in an immunofluorescence microscopy study of myogenesis in the embryonic chick wing, concentrating on the period between stages 27 and 30 (5 to 7·5 days incubation) which is when the dorsal and ventral muscle masses separate into discrete muscles. We have demonstrated the presence of all three collagen types at the ectoderm-mesenchyme junction from stage 27 onwards. Type I collagen and then type III collagen are found in progressively deeper layers of the dermis at the later stages. Both types I and V collagen are initially present in the cartilage elements, but type 1 collagen becomes restricted to the periphery of these structures at later stages. The developing muscle areas show a lack of staining at all stages and it is only at the latest stages that types I and III collagen first appear in the surrounding epimysium. We discuss possible mechanisms for the division of the muscle masses in the light of this information on the distribution of collagen types.

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.

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