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Collagen Type III

Collagen Type III: A key structural component of the extracellular matrix found in various connective tissues, including skin, blood vessels, and organs.
This fibrillar collagen plays a crucial role in tissue development, repair, and homeostasis.
Discover innovative tools from PubCompare.ai that can help streamline your research on Collagen Type III, locate relevant protocols, and leverage AI-driven comparisons to identify the best approaches.
Enhance reproducibility and unlock new insights into this important biological molecule.

Most cited protocols related to «Collagen Type III»

1
Extracellular Matrix Formation in Cell Cultures
Cited 9 times
Both HCFs and HKCs were plated on transwell 6-well plates containing polycarbonate membrane inserts with 0.4 μm pores (Costar, Charlotte, NC, USA,) at a density of 106 cells/mL. The protocol followed was identical for both cell types. Cells were cultured in EMEM with 10% FBS and 0.5 mM 2-O-α-D-glucopyranosyl-L-ascorbic acid (VitC, Wako Chemicals USA, Inc.; Richmond, VA, USA). The cultures were allowed to grow for 4 weeks in the presence of 0.1ng/mL TGF-β1 (T1) or TGF-β3 (T3). Cultures without any growth factors served as Controls (C). Culture medium was changed every other day for the duration of the experiment. The morphology of the cultures was examined using transmission electron microscopy (TEM). In addition, indirect-immunofluorescence was used to identify specific markers of stromal components—Smooth muscle actin (SMA), type I collagen (Col I), type III collagen (Col III), type V collagen (Col V) and fibronectin (EDA-Fn).
Karamichos D., Zareian R., Guo X., Hutcheon A.E., Ruberti J.W, & Zieske J.D. (2012). Novel in Vitro Model for Keratoconus Disease. Journal of Functional Biomaterials, 3(4), 760-775.
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Publication 2012
Actins Ascorbic Acid Cells Collagen Type I Collagen Type III Collagen Type V Culture Media extra domain A fibronectin, human FN1 protein, human Growth Factor Indirect Immunofluorescence polycarbonate Smooth Muscles TGF-beta1 Tissue, Membrane Transmission Electron Microscopy
2
Immunofluorescence of Tissue Constructs
Cited 8 times
Constructs were collected and fixed in 4% paraformaldehyde. IF was performed as previously described (Zieske et al. 2001 (link)). Following fixation, the constructs were incubated at 4°C overnight with the primary antibody—anti-type III collagen (1:40: Southern Biotech; Birmingham, AL), or anti-SMA (1:50: Dako North America; Carpinteria, CA)—diluted in 1%BSA + 0.1%Triton-X. The constructs were then washed and incubated overnight at 4°C with the corresponding secondary antibody—donkey anti-goat IgG (1:200, type III collagen), or donkey anti-mouse IgG (1:200, SMA)—diluted in 1%BSA + 0.1%Triton-X. Phalloidin-rhodamine (Invitrogen; Carlsbad, CA), which binds to the f-actin in all cells, was also used. Constructs were counterstained with TOPRO-3 iodide (1:1000, Invitrogen), a marker of all cell nuclei. Negative controls, where the primary antibody was omitted, were run with all experiments. Constructs were washed, mounted with Vectashield Mounting Media (Vector Laboratories; Burlingame, CA), observed and photographed using a confocal TCS-SP2 Leica microscope (Leica Microsystems; Bannockburn, IL). In addition, construct thicknesses were also measured with the confocal microscope, beginning with the first cell visible at the top of the construct and the last cell visible at the bottom. Data was averaged and analyzed.
Karamichos D., Hutcheon A.E, & Zieske J.D. (2011). Transforming growth factor beta 3 regulates assembly of a non-fibrotic matrix in a 3D corneal model. Journal of tissue engineering and regenerative medicine, 5(8), e228-e238.
Publication 2011
anti-IgG Cell Nucleus Cells Cloning Vectors Collagen Type III Equus asinus F-Actin Germ Cells Goat Immunoglobulins Iodides Microscopy, Confocal Mus paraform Phalloidine Rhodamine
3
Immunohistochemistry Protocol for Tissue Analysis
Cited 4 times
Immunohistochemical staining was performed on paraffin‐embedded tissue, as described previously 36. Immunostaining for α‐SMA and CD3 was accomplished with the EnVision System (Dako, Glostrup, Denmark). Other markers were identified with the ABC system (Vector Laboratories). The sections were all visualized using 3,3′‐diaminobenzidine (Sigma–Aldrich). CD3‐, CD68‐ and EGFP‐positive cells and the positive areas for α‐SMA, collagen type I, and collagen type III staining were assessed as the average of five randomly selected fields (×200) for each rat with ImageJ software (NIH).
Yoshida K., Nakashima A., Doi S., Ueno T., Okubo T., Kawano K., Kanawa M., Kato Y., Higashi Y, & Masaki T. (2018). Serum‐Free Medium Enhances the Immunosuppressive and Antifibrotic Abilities of Mesenchymal Stem Cells Utilized in Experimental Renal Fibrosis. Stem Cells Translational Medicine, 7(12), 893-905.
Publication 2018
Cells Cloning Vectors Collagen Type I Collagen Type III Paraffin Embedding Tissues
4
Cardiac Remodeling Assessment Post-Myocardial Infarction
Cited 4 times
LV remodeling was assessed by morphometric analysis on mosaic images of Sirius red-stained heart cross-sections using Axiovision 4.6 software (Zeiss, Zaventem, Belgium). Infarct size (%) at day 7 and day 28 post-MI was calculated according to Takagawa et al.50 (link) by dividing the sum of midline infarct lengths from all sections by the sum of midline LV circumferences from all sections and multiplying by 100. Midline infarct length was defined as the midline length of infarct that included >50% of the whole thickness of the myocardial wall. Whole LV area (μm2), LV cavity area (μm2), LV remote muscle area (μm2; including the septum) and infarct area (μm2) were analyzed. Infarct wall thickness (μm) was measured at equidistant points over the infarct area perpendicular to the infarcted wall. The thinning index was determined as the ratio of the mean infarct wall thickness normalized to the mean septal wall thickness. Expansion index was calculated as ((mean septal thickness/mean infarct thickness) × (LV cavity area/whole LV area)).51 (link) All geometric measurements were computed in a blinded fashion from representative tissue sections of four separate regions and the average value was used to represent that animal for statistical purposes.
To assess the degree of fibrosis in the heart, the area of collagen deposition was traced on Sirius red-stained tissue sections using polarized light and spectral thresholding allowing evaluation of tightly packed (red-orange) type I collagen versus thin, loosely assembled (yellow-green) type III collagen on a Leica RBE microscope with KS300 software (Zeiss). The degree of intersitital fibrosis (%) and the degree of collagen deposition in the infarct area (%) is expressed as the total collagen-positive area normalized to the total LV remote area or infarct area, respectively. Any perivascular fibrosis was excluded from this analysis. Two mid-ventricular sections were studied per animal.
Cardiomyocyte hypertrophy was analyzed on laminin-stained sections by measuring the cardiomyocyte cross-sectional area (μm2) of at least 200 randomly selected cardiomyocytes in the non-infarcted LV myocardium. Two mid-ventricular cross-sections were analyzed per mouse. Cardiomyocyte density was determined on the same laminin-stained sections by counting the number of cross-sectioned round shaped cardiomyocytes per mm2 of cardiomyocyte-covered LV myocardium.
Van Craeyveld E., Jacobs F., Gordts S.C, & De Geest B. (2011). Low-density lipoprotein receptor gene transfer in hypercholesterolemic mice improves cardiac function after myocardial infarction. Gene Therapy, 19(8), 860-871.
Publication 2011
Animals Collagen Collagen Type I Collagen Type III Dental Caries Fibrosis Heart Heart Ventricle Hypertrophy Infarction Laminin Light Mice, Laboratory Microscopy Muscle Tissue Myocardium Myocytes, Cardiac Tissues Tissue Stains
5
Collagen Staining for Tissue Architecture
Cited 4 times
Tissue samples were embedded in paraffin, sectioned at 5 μm, and stained with hematoxylin for evaluation of tissue architecture. The slides were washed with tap water and stained a with 0.1% fast green FCF for 10 min, followed by washing with acetic acid and staining with picrosirius red F3BA for 1 h. The slides were then washed with acidified water, dehydrated, cleared, and mounted in resinous medium. Sirius red/fast green (SR/FG) stain was chosen for its ability to differentiate type I from type III collagen. Sirius red is a strong anionic dye that stains collagen by reacting, via its sulfonic acid groups, with basic groups present in the collagen molecule. The dye molecules attach to the collagen fibers in such a way that their long axes are parallel. This configuration between the dye and the collagen results in an enhanced birefringency [14 (link)]. When viewed under cross-polarized light, the collagen fibers appear distinctly different from one another, with the type I collagen fibers appearing bright yellow-red/orange, while the type III collagen fibers appear green-blue. Slides were examined using cross-polarized light microscopy with an Axioskop 40 microscope (Carl Zeiss, Thornwood, NY) equipped with a Zeiss Axiocam at 400× magnification. A total of ten high-resolution images were captured of each slide, taking care not to overlap the images, ensuring ample representation of the field. The images were stored as multidimensional ZVI files for analysis.
Brown S.R., Melman L., Jenkins E., Deeken C., Frisella M.M., Brunt L.M., Eagon J.C, & Matthews B.D. (2010). Collagen type I:III ratio of the gastroesophageal junction in patients with paraesophageal hernias. Surgical endoscopy, 25(5), 1390-1394.
Publication 2010
Acetic Acid Birefringence Collagen Collagen Type I Collagen Type III Epistropheus Fast Green Fast Green FCF Light Light Microscopy Paraffin Embedding Resins, Plant Stains Sulfonic Acids Tissues

Most recents protocols related to «Collagen Type III»

1
Histological Analysis of Burn Wound Healing
The injured area was evaluated macroscopically after the burn and throughout the experiment considering skin color, presence of blisters and superficial crust formation. The histological sections stained with H&E were scanned using a Leica® DM 2500 microscope coupled to a Leica® DFC 425 camera and the Leica® Application Suite LAS v3.7 program. The images were obtained from the cross sections of four sequential fields of each slide, with the 10X and 40X objectives under a light microscope. To quantify the number of inflammatory cells (neutrophils and macrophages) and fibroblasts (young and adult), the images were analyzed using the ImageJ software, which allowed elaborating a grid and the individual marking of the cell nuclei with the aid of the manual counting tool.
The slides stained with Picrosirius Red were evaluated by digital image analysis to calculate the area occupied by the deposition of collagen types I and III, and photographed with the 10X objective, with a polarized light microscope (Leica® DM 2000) coupled to the camera (Leica® DFC 425). The Image-Pro Plus 4.5 program was used to quantify the percentage of type I and III collagens. When analyzed in association with polarized light, presence of collagen considered the following specifications for identification of the collagen types: collagen type I - yellow-reddish color; and collagen type III - green-whitish color. All histomorphometric analyses were performed blindly.
Amorim F.C., Arisawa E.Â., Sant’anna L.B., Rodrigues A.B, & Costa D.R. (2023). Preclinical study of experimental burns treated with photobiomodulation and Human Amniotic Membrane, both isolated and associated. Revista Latino-Americana de Enfermagem, 31, e3726.
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Publication 2023
Adult Cell Nucleus Collagen Collagen Type I Collagen Type III Fibroblasts Inflammation Light Light Microscopy Macrophage Microscopy Microscopy, Polarization Neutrophil Skin Pigmentation
2
Evaluation of Collagen Type III Expression
Immunocytochemical staining was used to evaluate the expression of collagen type III after 24 h incubation with decoction at 50 µg/mL. Betulinic acid (2 µM) was used as a positive control. The study was performed exactly as described in our previous paper [7 (link)], except that a decoction was used instead of acetone and ethanol extracts. The intensity of immunohistochemical staining was evaluated as negative (−), weak (+), moderate (++), or strong (+++), as in the previous article [7 (link),26 (link)].
Hadzik J., Choromańska A., Karolewicz B., Matkowski A., Dominiak M., Złocińska A, & Nawrot-Hadzik I. (2023). Oral Wound Healing Potential of Polygoni Cuspidati Rhizoma et Radix Decoction—In Vitro Study. Pharmaceuticals, 16(2), 267.
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Publication 2023
Acetone Betulinic Acid Collagen Type III Debility Ethanol
3
Quantifying Collagen Content in Vascular Tissue
To compare the difference in vascular collagen content between groups, the tissue sections were stained with Sirius Red. Sections were deparaffinized and hydrated to distilled water. Then, sections were placed in Sirius Red solution for 8 min followed by dehydration and mounting. Sirius Red dye is strongly acidic and easy to combine with basic groups in collagen molecules. Collagen fibers were stained a red–orange color and observed by an image acquisition system (Aerio CS2, Leica, Germany). Image Pro Plus version 7.0 was used to calculate the percentage of collagen fibers in tunica media. Sirius Red bonds with collagen fibers, which makes collagen fibers produce obvious birefringence. Under the polarizing microscope (DM2700P, Leica, Germany; polarization angle is 90 degrees), through the characteristics of enhanced birefringence light, type I and III collagen fibers show different colors, and type I collagen fibers show red–orange red; type III collagen fibers are green.
Autofluorescence of elastic fibers in tissue sections stained H&E was recorded with excitation wavelength at 460 nm–550 nm (Olympus 1 × 2 UCB) [32 (link),82 (link)].
Liu Q., Dong S., Zhou X., Zhao Y., Dong B., Shen J., Yang K., Li L, & Zhu D. (2023). Effects of Long-Term Intervention with Losartan, Aspirin and Atorvastatin on Vascular Remodeling in Juvenile Spontaneously Hypertensive Rats. Molecules, 28(4), 1844.
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Publication 2023
Acids Birefringence Blood Vessel Collagen Collagen Type I Collagen Type III Dehydration Elastic Fibers Light Microscopy Tissues Tunica Media
4
Histological Evaluation of Bone Healing
The structural and cellular changes during the progression of healing were investigated using the following histological stains: (1) Trichrome Masson Goldner stain [90 (link),91 (link)] to obtain an overview of mineralized and nonmineralized bone matrix changes within the fractured callus. (2) Sirius red stain [65 (link)] to investigate the changes in type I collagen distribution with the progression of healing. The stain facilitates the visualization of type I and type III collagen under polarized light. However, this study mainly focused on investigating the organization of type 1 collagen using Sirius red stain and silver nitrate stain [52 (link),91 (link)] to examine the morphological changes of osteocytes over the course of healing.
Malhan D., Schmidt-Bleek K., Duda G.N, & El Khassawna T. (2023). Landscape of Well-Coordinated Fracture Healing in a Mouse Model Using Molecular and Cellular Analysis. International Journal of Molecular Sciences, 24(4), 3569.
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Publication 2023
Bone Matrix Callus Cells Collagen Type I Collagen Type III Disease Progression Light Osteocytes Silver Nitrate Staining Stains trichrome stain
5
Porcine Collagen Matrix Preparation
The membrane (Cellis Dental), produced by Cellis Dental (La Rochelle, France) was a non-pyrogenic collagen type I&III matrix obtained from porcine skin. It was supplied dry, sterilized, and did not contain any preservatives. In in vitro tests, the matrix was cut into squares of 5 mm × 5 mm under sterilized conditions.
Felice P., D’Amico E., Pierfelice T.V., Petrini M., Barausse C., Karaban M., Barone A, & Iezzi G. (2023). Osteoblasts and Fibroblasts Interaction with a Porcine Acellular Dermal Matrix Membrane. International Journal of Molecular Sciences, 24(4), 3649.
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Publication 2023
Collagen Type III Dental Health Services In Vitro Testing Pharmaceutical Preservatives Pigs Skin Tissue, Membrane

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Ab7778 by Abcam
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Anti collagen type 3 by Abcam
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Anti-collagen type III is a laboratory reagent used for the detection and quantification of collagen type III in biological samples. It functions as an analytical tool for researchers studying the structure and composition of extracellular matrix proteins.
10
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TRIzol is a monophasic solution of phenol and guanidine isothiocyanate that is used for the isolation of total RNA from various biological samples. It is a reagent designed to facilitate the disruption of cells and the subsequent isolation of RNA.

More about "Collagen Type III"

Collagen Type III is a critical structural component of the extracellular matrix (ECM), found in a variety of connective tissues like skin, blood vessels, and organs.
This fibrillar collagen plays a pivotal role in tissue development, repair, and homeostasis.
Collagen III, also known as type III collagen, is a member of the collagen family of proteins.
It is often co-expressed with Collagen Type I and is essential for the proper assembly and organization of the ECM.
Alterations in Collagen Type III expression or structure have been implicated in various disease states, including fibrotic disorders, cardiovascular conditions, and wound healing impairments.
Researchers studying Collagen Type III can leverage a range of analytical tools and reagents to investigate its expression, localization, and function.
TRIzol reagent, for example, is a common solution used for RNA extraction, which can be useful for quantifying Collagen Type III gene expression using techniques like TaqMan Gene Expression Assays.
Antibodies such as Ab7778 and Ab34710 can be employed for immunohistochemical or Western blot analysis to detect and visualize Collagen Type III protein in biological samples.
Additionally, Triton X-100 and PVDF membranes are often utilized in Western blotting protocols to study Collagen Type III and other ECM components.
The use of Anti-collagen type III antibodies, like Ab6310 and Ab6308, can further enable the identification and characterization of Collagen Type III in various experimental settings.
By harnessing the power of PubCompare.ai's innovative tools, researchers can streamline their investigations on Collagen Type III, locate relevant protocols from literature, preprints, and patents, and leverage AI-driven comparisons to identify the most effective approaches.
This can enhance reproducibility, accuracy, and unlock new insights into this crucial structural protein and its role in tissue biology and disease.