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Procollagen

Q: What are the different types or variations of procollagen?

There are several types of procollagen, each corresponding to the different collagen types found in the body. The most common are type I procollagen, type II procollagen, and type III procollagen, which are the precursors to the most abundant collagen types in connective tissues such as bone, cartilage, and skin.

Most cited protocols related to «Procollagen»

Hepatic Fibrosis Induction and Assessment

Cited 15 times

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Publication 2011

3,3',5,5'-tetramethylbenzidine Acetic Acid Acids Aftercare Animals Biological Assay Buffers Carbon Tetrachloride CCL4 protein, human Centrifugation Collagen Dental Caries Edetic Acid Fibrosis Fibrosis, Liver Freezing Homo sapiens Horseradish Peroxidase Hydrolysis Hydroxyproline Institutional Animal Care and Use Committees Liver Mice, House Mice, Inbred C57BL N,N-dimethylcasein Nitrogen Oil, Mineral Pepsin A Peritoneum Peritonitis Procollagen Protease Inhibitors Protein Glutamine gamma Glutamyltransferase 2 Radiotherapy Dose Fractionations Rodent Serial Extraction Sodium Chloride Streptavidin Susceptibility, Disease Thioacetamide Tissue Adhesions Tissues Treatment Protocols Tromethamine Tube Feeding Tweens

Histological Analysis of ACI Cartilage Repair

Cited 10 times

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Publication 2009

Adult Antibodies Antigens Arthroscopy Autopsy Avidin Biopsy Biotin Bone Marrow Bones Cartilage Cartilages, Articular Cells Cell Shape Clone Cells Cloning Vectors Collagen Collagen Type I Collagen Type II Condyle Eosin Femur Femur Heads Fibrocartilage Fibrosis Formalin Freezing Frozen Sections Glycosaminoglycans Grafts Homozygote Hyaline Cartilage Hyalin Substance Hyaluronidase Hybridomas Immunoglobulins Immunohistochemistry Joints Joints, Ankle Knee Light Methanol Mus Needles Nitrogen Operative Surgical Procedures Oryctolagus cuniculus Paraffin Paraffin Embedding Patella Pathologic Neovascularization Patients Peroxidase Peroxides Phosphates Physiologic Calcification Procollagen PRSS2 protein, human Rabbits Saline Solution Serum Sodium Acetate Sodium Chloride Tissues Tolonium Chloride Tritium Trypsin Wound Healing

Characterization of Type II Procollagen, BMP-2, and IGF-1 in Chondrocytes

Cited 7 times

Three antibodies were used for immunohistochemistry of type II procollagen, and another two were used to detect BMP-2 and IGF-1 by ELISA and Western blots. Rabbit antisera against recombinant human type IIA-GST (IIA) only recognizes the exon 2 domain of type II procollagen (Oganesian et al., 1997 (link)). Rabbit antisera IIC reacts with bovine COOH-propeptide of type II collagen (provided by Dr. A. Robin Poole) and rat antisera against bovine type II collagen, IIF (provided by Dr. M. Cremer), recognizes the triple-helical domain of type II collagen. Preimmune sera from the rabbit producing anti–type IIA procollagen antibodies and nonimmune rat serum (Jackson ImmunoResearch Laboratories, Inc.) were used as controls. Anti–human integrin β1 mAb (GIBCO BRL) was used to demarcate the periphery of chondrocytes.
TGF-β1 antibodies were obtained from Santa Cruz Biotechnology. They are specific for active TGF-β1. IGF-1 antiserum was from Austral Biologicals. The BMP-2/4 mAb (AbH3b2/17) was kindly provided by Dr. Elizabeth Morris (Genetics Institute, Cambridge, MA). This reagent, AbH3b2/17, was made by standard mAb procedures using full length recombinant human BMP-2 as the immunogen. It reacts with both BMP-2 and BMP-4. Details of antibody specificity have been described in Yoshikawa et al. (1994) (link) and Bostrom et al. (1995) (link).

Zhu Y., Oganesian A., Keene D.R, & Sandell L.J. (1999). Type IIA Procollagen Containing the Cysteine-rich Amino Propeptide Is Deposited in the Extracellular Matrix of Prechondrogenic Tissue and Binds to TGF-β1 and BMP-2. The Journal of Cell Biology, 144(5), 1069-1080.

Publication 1999

Anti-Antibodies Antibodies Antibody Specificity Antigens Biological Factors BMP4 protein, human Bos taurus chondrocalcin Chondrocyte Collagen Type II Enzyme-Linked Immunosorbent Assay Exons Helix (Snails) Homo sapiens IGF1 protein, human Immune Sera Immunohistochemistry Integrins Procollagen Procollagen Type II Rabbits recombinant human bone morphogenetic protein-2 Robins Serum TGF-beta1 Western Blot

Probing Chondrocyte Development Genes

Cited 7 times

Probes included human CDMP1 cDNA (an ApaI fragment, residue 470– 1155) (Chang et al., 1994 (link)) and mouse α2(XI) collagen cDNA (pRAC2-28) (Tsumaki and Kimura, 1995 (link)). Mouse Ihh (Hh-14.1) and Shh (Hh-16.1) cDNA probes were provided by A. McMahon (Echelard et al., 1993 (link)). Mouse Pax1 cDNA (a HincII-SacI fragment) was obtained from H. Koseki and R. Balling (Deutsch et al., 1988 (link)). Mouse PTHrP cDNA (a AvrII/ SmaI fragment) and PTH/PTHrP receptor cDNA (a Sau3A/PvuII fragment) were obtained from A. Broadus (Mangin et al., 1990 (link)). Mouse α1(X) collagen cDNA (pRK26) was provided by K.S.E. Cheah (Kong et al., 1993 (link)). Mouse type IIA procollagen cDNA (exon 2) was from L.J. Sandell (Metsaranta et al., 1991 (link)).

Tsumaki N., Tanaka K., Arikawa-Hirasawa E., Nakase T., Kimura T., Thomas J.T., Ochi T., Luyten F.P, & Yamada Y. (1999). Role of CDMP-1 in Skeletal Morphogenesis: Promotion of Mesenchymal Cell Recruitment and Chondrocyte Differentiation. The Journal of Cell Biology, 144(1), 161-173.

Publication 1999

Collagen DNA, Complementary Exons GDF5 protein, human HMN (Hereditary Motor Neuropathy) Proximal Type I Homo sapiens methyl 4-azidophenylacetimidate Mus Parathyroid Hormone Receptor Procollagen PTHLH protein, human

Synovial Fluid Biomarker Profiling

Cited 5 times

Synovial fluid was analyzed with commercially available enzyme-linked immunosorbent assays (ELISA), high-performance liquid chromatography (bilirubin/biliverdin), or chemical assay (sulfated glycosaminoglycan [sGAG]). Table 1 lists all the assayed biomarkers, the processes they reflect, and the assay coefficients of variation. Due to volume limitations, assays were run in singlicate. Random samples were selected for duplicates, and any samples that were above the level of quantification or outside the standard curve were repeated at higher dilutions. Intra-assay coefficients of variation, as determined by standards and samples run in duplicates, were \12% for all assays. The multiplex Proinflammatory Panel 1 (Meso Scale Discovery) was used to measure concentrations of IL-1β, IL-2, IL-6, IL-8, TNFα, IFN-γ, IL-10, IL-12p70, IL-13, and IL-4. Human MMP 3-Plex Kit (Meso Scale Discovery) was used for MMP-1, MMP-3, and MMP-9. Commercially available individual assay kits were obtained for the following: IL-1ra (R&D Systems), IL-1α (Meso Scale Discovery), N-terminal telopeptide (NTX; Ostex International), C-terminal crosslinked telopeptide type II collagen (CTXII; Immunodiagnostic Systems), cartilage oligomeric matrix protein (COMP; Biovendor), sGAG (Kamiva), and procollagen II C-peptide (Ibex). An in house developed assay was used to measure bilirubin/biliverdin concentrations.

Amano K., Huebner J.L., Stabler T.V., Tanaka M., McCulloch C.E., Lobach I., Lane N.E., Kraus V.B., Benjamin C, & Li X. (2018). Synovial Fluid Profile at the Time of Anterior Cruciate Ligament Reconstruction and Its Association With Cartilage Matrix Composition 3 Years After Surgery. The American journal of sports medicine, 46(4), 890-899.

Publication 2018

Bilirubin Biliverdine Biological Assay Biological Markers C-Peptide Cartilage Oligomeric Matrix Protein Collagen Type II COMP protocol Enzyme-Linked Immunosorbent Assay High-Performance Liquid Chromatographies Homo sapiens IL1RN protein, human IL10 protein, human Immunodiagnosis Interferon Type II Interleukin-1 beta Interleukin-12 Interleukin-13 Interstitial Collagenase Matrix Metalloproteinase 3 MMP9 protein, human polysulfated glycosaminoglycan Procollagen Synovial Fluid Technique, Dilution Tumor Necrosis Factor-alpha

Most recents protocols related to «Procollagen»

Hypoxia and Adoptive Cell Therapy in Lung Fibrosis

NSG male and female mice (The Jackson Laboratory), average 10 weeks of age, were administered low-dose intratracheal bleomycin (1.25 U/kg) (9 (link)). Two weeks following a nonfibrogenic dose of bleomycin i.t., GPR81 shRNA or scrambled shRNA IPF MPCs were suspended in PBS (1 × 10⁶ cells/100 μL) and injected via tail vein. Following cell administration, the mice were maintained under normoxic (21% O₂) or hypoxic conditions (10%O₂; BioSpherix hypoxia chamber) for the duration of the experiment. Mice were euthanized 4 weeks after adoptive transfer of human cells, and the lungs were harvested. Collagen content was quantified in the left lung tissue by Sircol assay and served as the primary endpoint. Histological (H&E and trichrome staining) and IHC analysis was performed on paraffin-embedded and frozen right lung tissue. The presence of lung fibrotic lesions by histological analysis served as the secondary endpoint. Cells positive for human procollagen (anti–human procollagen type I antibody, 1:500; catalog MAB1912; EMD Millipore) were identified as human. IHC using the human procollagen antibody and GPR81 antibody was performed to assess the distribution of GPR81-expressing cells with human procollagen I expressing cells. The antibody used does not cross-react with mouse collagen.

Yang L., Gilbertsen A., Xia H., Benyumov A., Smith K., Herrera J., Racila E., Bitterman P.B, & Henke C.A. (2023). Hypoxia enhances IPF mesenchymal progenitor cell fibrogenicity via the lactate/GPR81/HIF1α pathway. JCI Insight, 8(4), e163820.

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Publication 2023

Adoptive Cell Transfer Antibodies, Anti-Idiotypic Biological Assay Bleomycin Cells Collagen Disease Progression Females Fibrosis Freezing Heterografts Homo sapiens Hypoxia Immunoglobulins Lung Males Mesenchymal Stem Cells Mus Paraffin Embedding Procollagen Procollagen Type I Pulmonary Fibrosis Short Hairpin RNA Tail Tissues Veins

Comprehensive Liver Biopsy and Biomarker Evaluation

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Publication 2023

ADIPOQ protein, human austin Biological Markers Biopsy BLOOD Blood Platelets Blood Proteins Caspase Cytokeratin 18 D-Alanine Transaminase Enzyme-Linked Immunosorbent Assay Fibrosis Hyaluronic acid Immunoassay Inflammation KRT18 protein, human Liver Metalloproteinase-1 Tissue Inhibitor Nonalcoholic Steatohepatitis Pathologists Patients Plasma Platelet Counts, Blood Precursor, Complement C3 Procollagen procollagen Type III-N-terminal peptide Proteins Serum Steatohepatitis Triglycerides

Quantifying Procollagen I Secretion

Fibroblasts were grown to confluence in 10‐cm tissue culture plates. Subsequently, the cell layers were washed with PBS. Then, each plate was filled with 7 mL of fresh DMEM medium containing 40 µg/mL of l‐ascorbic acid phosphate magnesium salt n‐hydrate. Fibroblasts from each patient were cultured with or without 10 ng/mL of TGFβ1. At defined time points, 50‐µL samples were withdrawn from the media. Subsequently, the samples were processed for polyacrylamide electrophoresis. Procollagen I present in cell culture media was detected by QWB with the anti‐pro‐α1(I) chain primary antibody, as described.²⁰ Signal intensities of protein bands corresponding to intact and partially processed procollagen α1(I) chain were measured. Subsequently, results were normalized to the 1‐h data point. Normalized data were plotted against time and fitted to the linear model (GraphPad Prism, version 6.07; GraphPad Software Inc.). The slopes of the fitted curves represented an hourly rate of secretion of procollagen I. The significance of differences between the (+)TGFβ1 and the (−)TGFβ1 groups was analyzed using GraphPad Prism, version 6.07. We expressed the procollagen secretion rates in arbitrary units (au)/h.

Hendy B.A., Fertala J., Nicholson T., Abboud J.A., Namdari S, & Fertala A. (2023). Profibrotic behavior of fibroblasts derived from patients that develop posttraumatic shoulder stiffness. Health Science Reports, 6(2), e1100.

Publication 2023

Cell Culture Techniques Cells Culture Media Electrophoresis Fibroblasts Immunoglobulins Magnesium Ascorbate Patients Phosphates polyacrylamide prisma Procollagen Proteins TGF-beta1 Tissues

Estimating Sample Size for Frozen Shoulder Study

To determine the number of patients required for our study, we employed a sample size estimation test used in the previous prevalence studies.²², ²³ On the basis of the literature, we expected to find postoperative frozen‐shoulder cases in 15% of patients.⁴, ⁵ Consequently, for the expected prevalence of 15%, the required sample size was 29 for the margin of error or absolute precision of ±13% in estimating the prevalence with 95% confidence. With this sample size, the anticipated 95% CI was (2%, 28%).
Analysis of differences in the expression of protein markers in fibroblasts isolated from NS and ST patients was performed using two‐sided one‐way ANOVA (IBM SPSS Statistic for Windows, version 27, IBM Corp.). The significance of differences between the kinetics of procollagen secretion, represented by the slopes of the fitted curves, was analyzed using GraphPad Prism, version 6.07 (GraphPad Software Inc.).
To evaluate differences in the collagen disc contractures, we applied repeated measures ANOVA, with a Greenhouse‐Geisser correction, to evaluate the discs' surface changes across various time points (IBM SPSS Statistic for Windows, version 27, IBM Corp.).
Our statistical analyses' results were presented in the form of graphs, tables, and descriptive statistics. In all assays, statistical significance was defined as p ≤ 0.05.

Publication 2023

Biological Assay Collagen Contracture Fibroblasts Kinetics neuro-oncological ventral antigen 2, human Patients prisma Procollagen Proteins secretion Shoulder, Frozen

Quantitative Analysis of Fibrotic Scar Markers

At the end of the culture, cell layers were washed with cold PBS. Next, the cell lysates were prepared from each cell culture dish. The protein concentration in the lysates was determined using the Bradford assay (Bio‐Rad Laboratories). Subsequently, 10‐µg protein samples were loaded onto polyacrylamide gels. Following electrophoretic separation, the proteins of interest were assayed using quantitative Western blot (QWB) assays using an infrared detection system (LI‐COR Biotechnology).
We rationally selected protein markers associated with the formation of collagen‐rich fibrotic scars. In particular, we were interested in the production of connective tissue growth factor (CTGF), whose expression is stimulated by TGFβ1‐dependent pathways.¹⁶, ¹⁷ TGFβ1 is the master regulator of fibrotic scar formation in many tissues, including those forming joints.¹⁰, ¹⁸, ¹⁹ In addition to being a strong stimulator of cell proliferation, TGFβ1 activates the biosynthesis of crucial extracellular matrix (ECM) components, including procollagen I and fibronectin. TGFβ1 acts by inducing CTGF, which is upregulated in many fibrotic disorders. Consequently, CTGF acts as the mediator of TGFβ1 activities.¹⁷To study the differentiation of fibroblasts into profibrotic myofibroblasts, we assayed the expression of α smooth muscle actin (αSMA). Additionally, we examined differences in the expression of crucial structural proteins that form the scar tissue, including collagen I and fibronectin. Finally, we analyzed the production of prolyl 4‐hydroxylase (P4H) and heat shock protein 47 (HSP47), essential proteins needed for the proper folding, stability, and secretion of procollagen I.
We measured glyceraldehyde 3‐phosphate dehydrogenase (GAPDH) in each sample as an internal reference. Using secondary antibodies conjugated with different infrared dyes allowed us to detect a target protein and GAPDH simultaneously. Table 2 presents the antibodies we employed in our assays.

Publication 2023

Actins Anabolism Antibodies Biological Assay Cell Culture Techniques Cell Proliferation Cells Cicatrix Cold Temperature Collagen Collagen Type I CTGF protein, human Dyes Electrophoresis Extracellular Matrix Fibroblasts Fibronectins Fibrosis Glyceraldehyde-3-Phosphate Dehydrogenases Heat-Shock Protein 47 Hyperostosis, Diffuse Idiopathic Skeletal Joints Myofibroblasts polyacrylamide gels Procollagen Procollagen-Proline Dioxygenase Proteins secretion SERPINA3 protein, human Smooth Muscles TGF-beta1 Tissues Western Blot

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Human pro collagen 1 alpha 1 duoset elisa by R&D Systems

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The Human Pro-Collagen I alpha 1 DuoSet ELISA is a quantitative sandwich enzyme-linked immunosorbent assay (ELISA) designed for the measurement of human pro-collagen I alpha 1 levels in cell culture supernates, serum, and plasma.

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What is procollagen and what is its importance in research?

Procollagen is the precursor molecule to collagen, the primary structural protein found throughout the body's connective tissues. It is synthesized by fibroblasts and other collagen-producing cells, and undergoes post-translational modifications before being secreted as mature collagen. Studying procollagen is crucial for understanding collagen-related disorders and developing therapies to address conditions affecting connective tissue integrity and function.

What are the different types or variations of procollagen?

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What are some common challenges in working with procollagen, and how can PubCompare.ai assist?

One common challenge in procollagen research is ensuring reproducibility and consistency across experiments. PubCompare.ai can help address this by allowing you to compare a wide range of procollagen research protocols from literature, preprints, and patents. This empowers you to identify the most effective and reliable methods, reducing the risk of variability in your results. The platform's AI-driven analysis can also help you troubleshoot any issues that may arise during your procollagen experiments.

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More about "Procollagen"

Procollagen is the precursor molecule to collagen, the primary structural protein found in the extracellular matrix of connective tissues throughout the body.
It is synthesized within fibroblasts and other collagen-producing cells, and undergoes a series of post-translational modifications and processing steps before being secreted as mature collagen.
Procollagen plays a crucial role in the maintenance and repair of tissues such as bone, cartilage, skin, and tendons.
The study of procollagen is vital for understanding the pathogenesis of collagen-related disorders, such as Ehlers-Danlos syndrome, osteogenesis imperfecta, and Marfan syndrome.
These conditions affect the integrity and function of connective tissues, leading to various clinical manifestations.
Researchers often utilize techniques like ELISA (e.g., Human Pro-Collagen I alpha 1 DuoSet ELISA), RT-PCR (e.g., RevertAid First Strand cDNA Synthesis Kit), and Western blotting to analyze procollagen expression and processing.
Optimizing procollagen research protocols can enhance productivity and reproducibility, leading to more robust findings and accelerated progress in the field.
Researchers may employ reagents like TRIzol and RNeasy Mini Kit to extract and purify RNA for gene expression analysis, and trypsin-EDTA to dissociate cells for culture experiments.
Additionally, the use of internal control genes, such as β-actin, can help normalize gene expression data and improve the reliability of procollagen-related studies.
By leveraging the insights gained from existing procollagen research and utilizing the right tools and techniques, scientists can advance our understanding of collagen-related disorders and develop more effective therapies to address conditions affecting connective tissue integrity and function.
PubCompare.ai's AI-driven research protocol comparison can be a valuable resource in this endeavor, helping researchers identify the most reproducible and effective methods for their procollagen studies.