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Desmosine

Desmosine is a unique amino acid found in the elastin of connective tissues.
It plays a crucial role in the structural integrity and elasticity of these tissues, particularly in the lungs and arteries.
Researchers utilize various techniques, such as mass spectrometry, to quantify and study desmosine levels, which can provide insights into the pathogenesis of diseases like chronic obstructive pulmonary disease (COPD) and cardiovascular disorders.
PubCompare.ai's AI-driven platform offers a streamlined approach to locating the best protocols and products for desmosine research, empowering reproducible investigations and identifying the most reliable and effective methodologies.
Leveraging AI-powered analysis, scientists can efficiently compare data from literature, preprints, and patents, facilitating advancements in the understading of desmosine's role in health and disease.

Most cited protocols related to «Desmosine»

Several methodological comparisons have been made regarding quantitative radio graphic data generated by the OAI (Supplementary Table 2 online). The findings emphasize, for example, the need to take radio-anatomic alignment of OAI fixed-flexion radiographs into account when analyzing change in JSW, and the need for central radiographic readings. Regarding semiquantitative scoring of articular tissue pathology using MRI images, two existing systems—WORMS (whole organ MRI score) and BLOKS (Boston Leeds osteoarthritis knee score)—were applied to a sample of images of 113 knees with radiographic OA and at risk of progression, from the OAI cohort. Both methods were shown to be reliable cross-sectionally (Supplementary Table 2 online). Longitudinally, BLOKS was found to be superior to WORMS for assessment of change in the meniscus, and WORMS was superior to BLOKS for scoring bone-marrow lesions (BMLs), in terms of predicting cartilage loss.4 (link) A new hybrid method (MOAKS; MRI OA knee score) was hence proposed with the aim of combining the advantages of each scoring system.5 (link) In assessing which sequence is better to detect such changes, more and larger focal cartilage defects and BMLs were detected with the intermediate-weighted fat-suppressed spin echo sequence than with DESS6 ,7 (link) (Figure 2, Supplementary Table 2 online).
Semi-automated segmentation algorithms for quantitative measurement of cartilage, bone, meniscus, and thigh muscles (Figure 3) have been assessed. These studies have used different image analysis approaches and have reported, in part, the level of agreement with manual segmentation and/or the level of inter-observer reliability (Figure 1, Supplementary Table 2 online).
The sensitivity to change of cartilage thick ness over 1 year in the medial femorotibial compartment was found to be similar between sagittal DESS, coronal multiplanar reconstructed DESS, and coronal FLASH in 80 knees (Figure 2), with SRMs ranging from −0.34 to −0.38.8 (link) The three protocols were also highly intercorrelated cross-sectionally (coefficient of correlation [r] ≥0.94); analysis of every second 0.7 mm DESS image provided similar sensitivity to change as analysis of every image.8 (link) Change in the medial weight-bearing femur substantially exceeded that in the posterior aspect of the femoral condyle, suggesting that structural progression is faster in (commonly) weight-bearing regions of the joint.9 (link)Measuring between-group differences using cartilage subregions (Figure 4) or atlases of cartilage thickness within anatomically defined cartilage plates has also been explored by several groups, alongside assessing whether such methods improve sensitivity to change (Supplementary Table 3 online). These studies generally identified the central subregion of the weight-bearing medial femoral cartilage plate as the region of interest with the greatest rate of cartilage loss and sensitivity to change (Figure 4).
Publication 2012
Bone Marrow Bones Cartilage Condyle Desmosine Disease Progression ECHO protocol Enchondroma Femur Helminths Hybrids Hypersensitivity Joints Knee Meniscus Muscle Tissue NES protein, human Radiography Thigh Tissues
The neural network model chosen for this problem is based on the U-Net architecture, which has previously shown promising results in the tasks of segmentation, particularly for medical images (15 (link),22 –25 ), and has fewer trainable parameters than the other popular segmentation architecture, SegNet (26 ). The U-Net architecture can be viewed in Figure E1 (online). The network takes a full image section as input and then, through a series of trainable weights, creates the corresponding section segmentation mask (22 ).
Our U-Net model uses a weighted cross-entropy loss function between the true segmentation value and the output for our model. The weighted cross-entropy function was used to account for the class imbalance of the volume that cartilage and meniscus compartments make up compared with the entire MR imaging volume. Details on this equation can be viewed in Appendix E1 (online).
To build the U-Net models, data in subjects from both the T1ρ-weighted and the DESS sets were divided into training, validation, and time-point testing sets with a 70/20/10 split and were then broken down into their respective two-dimensional (2D) sections to be used as inputs for the two sequence models. The time-point testing set for both data sets consisted of only follow-up studies corresponding to baseline studies in the training and validation data sets. This time-point hold-out data set was used as validation for the precision of the automatic segmentation longitudinally. A full breakdown of the T1ρ-weighted and DESS training, validation, and time-point testing data according to diagnostic group (ACL, OA, control) can be viewed in Table 2. The full 3D segmentation map was then generated by stacking the predicted 2D sections for a subject and then taking the largest 3D-connected component for each compartment class.
All U-Net models were implemented in Native TensorFlow, version 1.0.1 (Google, Mountain View, Calif). Model selection was made by using the 1-standard-error rule on the validation data set (27 ) (B.N., with 3 years of experience). For full learning specifications and learning curves of the U-Net, see Table E1 and Figure E2 (both online).
Publication 2018
Cartilage Catabolism Desmosine Entropy Learning Curve Meniscus

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Publication 2016
Bones Cartilage Cartilages, Articular Condyle Desmosine ECHO protocol Femur Knee Knee Joint Radionuclide Imaging Radius Strains Tibia TRIO protein, human

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Publication 2012
Desmosine ECHO protocol Ethics Committees, Research Healthy Volunteers Index, Body Mass Injuries Knee Magnetic Resonance Imaging Males Patients Radionuclide Imaging TRIO protein, human Woman
A total of twenty subjects (n=10 with BMI of 18.5–24.9 kg/m2 and n=10 with BMI of 25–31 kg/m2) participated in this IRB approved study. No subjects had a history of knee injury or knee surgery. Subjects in each group were age- and sex- matched. Each subject was imaged twice in one day (at 8:00 AM and 4:00 PM) using a 3T MRI scanner (Trio Tim, Siemens Medical Solutions USA, Malvern, Pennsylvania) and an eight channel knee coil. Subjects were instructed to refrain from exercise or any strenuous activity prior to the morning scan. Subjects were scanned while lying supine, with the knee in a relaxed, slightly flexed position (26 (link)). A double-echo steady-state sequence (DESS, field of view: 15×15 cm, matrix: 512×512 pixels, slice thickness: 1 mm, flip angle: 25°, repetition time: 17 ms, echo time: 6 ms) was used to generate sagittal plane images of the knee (Figure 1) (23 (link), 26 (link)). Total scan time was approximately 9 min. Subjects were asked to perform their normal activities throughout the day. Subjects returned to the same facility at 4:00PM and were imaged immediately upon arrival using the same protocol. In addition, each participant wore a pedometer to provide a measure of the number of steps taken between MR imaging sessions.
The MR images were used to generate 3D models of each subject’s knee, including models of the femur, tibia, patella, and the corresponding articular surfaces (Figure 1) (23 (link)). In each image, the outer margins of the cortices and articular surfaces of cartilage were segmented using a solid modeling software (Rhinoceros, McNeel and Associates, Seattle, WA) (23 (link), 27 (link)). These curves were then used to generate 3D surface mesh models of each surface (Studio, Geomagic Inc., Research Triangle Park, NC) (Figure 1). AM and PM models of the femur, tibia, and patella were aligned using an iterative closest point technique so that thickness measurements and strain calculations could be made at the same locations in each model (23 (link)). A grid sampling system was used to characterize cartilage thickness in different regions of the joint (23 (link)). Specifically, cartilage thickness on the tibia was sampled over a grid of nine evenly spaced points spanning both the medial and lateral tibial plateaus, for a total of 18 points (Figure 1). Eleven points spanned the surface of the patella and six points were sampled on the subpatellar region of the femur. A total of 36 points were measured across the surfaces of the medial and lateral femoral condyles. Thickness was defined as the minimum distance from the articular surface to bone at each mesh point on the model (Figure 2). Thickness was averaged across each mesh point within a 2.5mm radius of the sampling point. In this fashion, diurnal strain was calculated using the ratio of the change in thickness (final thickness minus initial thickness) to the initial thickness at the same location (23 (link)). This methodology has been previously validated for measuring cartilage thickness in the tibiofemoral joint (28 (link)). A more recent study from our laboratory reported a coefficient of repeatability of 0.03mm; thus, we estimate the resolution of strain measurements to be less than 1% (23 (link)).
Publication 2013
Bones Cartilage Cartilages, Articular Condyle Cortex, Cerebral Desmosine ECHO protocol Femur Joints Knee Knee Injuries Knee Joint Operative Surgical Procedures Patella Radionuclide Imaging Radius Strains Tibia TRIO protein, human

Most recents protocols related to «Desmosine»

The second stage juveniles (J2s) of M. chitwoodi race 1 were hatched from eggs collected from Rutgers tomatoes grown in greenhouses at Washington State University. Meloidogyne fallax and M. minor J2s were provided by the Wageningen Nematode Collection (National Plant Protection Organization, the Netherlands) and stored in DESS at -20°C. Second stage juveniles were digested using the protocol described in Qiu et al. (2006) (link). In brief, J2s were picked under a dissecting scope and transferred to 15 µL droplets of Milli-Q water. The nematodes were crushed using a pipet tip; 10 µL of the crushed nematode was transferred to a 10 µL solution containing 2 µL AmpliTaq Gold 360 buffer, 2 uL of 600 µg/mL Proteinase K, and 6 µL Milli-Q water. The reaction mixes were incubated at -20°C for 20 minutes, heated for 1 hour at 65°C, and then 95°C for 10 min before cooling to room temperature. The nematode samples were spun at 12,000 rpm for 2 min before storing at -20°C until used in PCR. Five µL of these J2 samples were used as template for molecular beacon RT-PCR, and each sample was run in duplicate or triplicate. The 50 µL reaction mixes contained 1x AmpliTaq Gold 360 buffer, 3 mM MgCl2, 200 µM dNTPs, 200 nM F-HSP90 and R-HSP90 primers, 200 nM target beacon (C1-Hsp90-FAM-6, F1-Hsp90-HEX-5, or M2-Hsp90-Cyan-5) and 1.25 U of AmpliTaq Gold. The reaction conditions were the same as those used for the standard curves. All molecular beacon RT-PCR assays with these three species were repeated at least twice with similar results.
To ensure the specificity of this assay 40 ng of gDNA from M. incognita, M. javanica, M. arenaria, or M. hapla was used as template for molecular beacon RT-PCR assay using C1-Hsp90-FAM-6, F1-Hsp90-HEX-5, and M2-Hsp90-Cyan-5 beacons. Non-template controls containing only Milli- Q water were included as well as positive controls using 4 pg of plasmid HSP90 for M. chitwoodi,
M. fallax, or M. minor. The 50 µL reaction mixes contained 1x AmpliTaq Gold 360 buffer, 3 mM MgCl2, 200 µM dNTPs, 200 nM F-HSP90 and R-HSP90 primers, 200 nM target beacon (C1- Hsp90-FAM-6, F1-Hsp90-HEX-5, or M2-Hsp90-Cyan-5) and 1.25 U of AmpliTaq Gold. The reaction conditions were the same as those used for the standard curves. The molecular beacon RT-PCR assays with non-target species were repeated twice with similar results.
All PCR products in this paper were visualized as follows: 10 µL of each PCR product was loaded onto a 1.5% agarose gel and separated for 45 min at 100 V before visualizing with ethidium bromide under UV light. The Invitrogen 1-kb plus DNA ladder was used as reference for size.
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Publication 2023
Adjustment Disorders Biological Assay Buffers Desmosine Eggs Endopeptidase K Ethidium Bromide Gold HSP90 Heat-Shock Proteins Lycopersicon esculentum Magnesium Chloride Meloidogyne Nematoda Oligonucleotide Primers Plants Plants, Arenaria Plasmids Reverse Transcriptase Polymerase Chain Reaction Sepharose Ultraviolet Rays
To calculate the maximum concentration at which there was no cell death a MTS cell viability assay was performed. HUVECs were cultured according to supplier protocols, subcultured, and seeded in a 96 well‐plate at a density of 10 000 cells per well. After allowing for cell adhesion overnight, the cells were treated with serial dilutions of DESs dissolved in fresh HUVEC media. The plate was incubated for 4 hours before the media was aspirated and replaced with fresh media containing 20% MTS Reagent. After 1 hours the absorbance was measured at 490 nm (BioTek Synergy neo2).
To assess vascular permeability, transport across transwell cell culture experiments were used. First, sufficient 24 well‐plate transwell inserts were coated with 0.1% gelatin under sterile conditions and stored at 4 °C overnight. The excess gelatin was removed by inversion of transwell and washed with sterile PBS. HUVECs were cultured according to supplier protocols, subcultured, and seeded on the transwell inserts with 400 µL of 250 000 cells mL−1 media. The outer well was then filled with 600 µL of fresh media and allowed to grow for 48 hours before the experimental progression. After monolayers had formed, the media was removed from the top chamber and replaced with media containing 0.15% IL and 0.9 U mL−1 insulin, this was in preparation for the concentration and insulin to IL ratio to be used in the future in vivo studies. The plate was incubated in appropriate cell culture conditions and 300 µL samples were taken from the plate wells and replaced with fresh media every 10 minutes for 1 hour. The samples were then stored at 4 °C until they were diluted appropriately and quantified using ELISA.
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Publication 2023
Biological Assay Cell Adhesion Cell Culture Techniques Cell Death Cells Cell Survival Desmosine Disease Progression Enzyme-Linked Immunosorbent Assay Gelatins Insulin Inversion, Chromosome Sterility, Reproductive Technique, Dilution Vascular Permeability
To evaluate the physical stability of the formulations, the hydrodynamic size of insulin was measured using dynamic light scattering (DLS, Malvern Zetasizer Pro) in the presence of human collagen type I/III (Advanced BioMatrix, Carlsbad, CA). Insulin formulations with DESs, along with their respective clinical controls Humalog and saline, were added to a neutral‐pH solution of collagen at predetermined w/w ratios of collagen to insulin and size was measured at various timepoints.
Physical stability of the formulations in the presence of collagen was further assessed using fluorescence polarization (FP). In principle, a molecule of interest, in this case insulin around 5.8 kDa, will rotate faster in an unbound state than a bound state, in this case bound to collagen around 300 kDa, due to its Brownian rotation and its smaller molecular radius. When insulin is fluorescently labeled and excited with polarized light the perpendicular and parallel polarized light emission can be measured. Plate readers designed for FP can measure perpendicular and parallel polarized light to generate a polarization, with units mP, value which indicates the binding state of the fluorescently labeled protein. Bound insulin that is rotating more slowly will emit in the parallel direction and have a higher polarization value as the complex has not had sufficient time to rotate. Unbound insulin, or binding inhibition, is indicated by more perpendicular binding and lower polarization values.[43] Formulations were prepared with Cy 5.5‐labeled insulin. The formulations were mixed with a collagen solution at predetermined w/w ratio, and fluorescence polarization was detected using Molecular Devices Flexstation 3 plate reader.
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Publication 2023
Binding Proteins Collagen Collagen Type I Desmosine Enzyme Multiplied Immunoassay Technique Fluorescence Polarization Homo sapiens Humalog Hydrodynamics Insulin Light Medical Devices Physical Examination Psychological Inhibition Radius Saline Solution
tert-Butyl N-(4-hydroxybutyl)-N-methyl-carbamate (1.00 g, 4.91 mmol, 1 equiv) and Dess–Martin
periodinane (2.92 g, 6.88 mmol, 1.4 equiv) were dissolved in DCM (15
mL). The reaction mixture was stirred at rt for 2 h, then diluted
with EtOAc and filtered through a Celite. The filtrate was washed
with an aq. solution of Na2S2O3,
NaHCO3, dried over MgSO4, and concentrated under
reduced pressure to yield tert-butyl N-methyl-N-(4-oxobutyl)carbamate 76 as
a colorless oil. The product was used in the next step without further
purification. 76 (990 mg, 4.92 mmol, 1 equiv) and tert-butyl(triphenylphosphoranylidene)acetate (2.04 g, 5.41
mmol, 1.1 equiv) were dissolved in dry PhMe (16.4 mL). The reaction
mixture was heated to 120 °C and stirred for 16 h. The solvent
was removed under reduced pressure. Purification by NP column chromatography
(eluent: 15–40% EtOAc/cyclohexane) afforded 77 (1.02 g, 70% after 2 steps) as a yellow oil. 1H NMR (500
MHz, chloroform-d) δ 6.84 (dt, J = 15.6, 6.8 Hz, 1H), 5.75 (dt, J = 15.7, 1.6 Hz,
1H), 3.28–3.16 (m, 2H), 2.83 (s, 3H), 2.20–2.10 (m,
2H), 1.71–1.61 (m, 2H), 1.46 (d, J = 12.3
Hz, 18H). HPLC/MS: m/z 322.1992
[M + Na]+. Rt (2 min): 1.57
min.
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Publication 2023
1H NMR Acetate Bicarbonate, Sodium Carbamates Celite Chloroform Chromatography Cyclohexane Desmosine High-Performance Liquid Chromatographies N-methylcarbamate Pressure Sulfate, Magnesium TERT protein, human
Consecutive patients who underwent PCI at Chang Gung Memorial Hospital, LinKou, Taiwan, between January 2010 and December 2017 were screened retrospectively for eligibility. We identified cases from the medical records with at least one long coronary lesion treated with one or multiple overlapping second-generation DESs with a total stent length of ≥38 mm. We excluded patients presenting with ST-segment elevation myocardial infarction (STEMI) or cardiogenic shock. The included patients with dsDMax ≤ 2.0 mm based on the quantitative coronary analysis were categorized into the extremely small distal vessel (ESDV) group, and the remaining patients were assigned to the non-ESDV group (dsDMax > 2.0 mm). Patients with simultaneous long lesions of dsDMax ≤ 2.0 and dsDMax > 2.0 mm in different vessels were categorized into the ESDV group. The baseline characteristics, risk factors for atherosclerotic cardiovascular disease, comorbidities, and medications of the included patients were obtained from the electronic medical records.
The study was approved by the Institutional Review Board of Chang Gung Memorial Hospital. All the patients underwent standard medical management. The requirement for written consent from patients was waived owing to the retrospective nature of this study.
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Publication 2023
Blood Vessel Desmosine Eligibility Determination Ethics Committees, Research Heart Patients Pharmaceutical Preparations Shock, Cardiogenic Stents ST Segment Elevation Myocardial Infarction

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More about "Desmosine"

Desmosine is a unique amino acid found in the elastin of connective tissues, playing a crucial role in their structural integrity and elasticity, particularly in the lungs and arteries.
Researchers utilize various techniques, such as mass spectrometry, to quantify and study desmosine levels, which can provide insights into the pathogenesis of diseases like chronic obstructive pulmonary disease (COPD) and cardiovascular disorders.
PubCompar.ai's AI-driven platform offers a streamlined approach to locating the best protocols and products for desmosine research, empowering reproducible investigations and identifying the most reliable and effective methodologies.
Leveraging AI-powered analysis, scientists can efficiently compare data from literature, preprints, and patents, facilitating advancements in the understanding of desmosine's role in health and disease.
Desmosine is a unique biomarker that can be measured using techniques like mass spectrometry, such as with the MAGNETOM Trio or Eclipse Ni microscope.
Its levels are associated with conditions like COPD, which involves the breakdown of elastin in the lungs, as well as cardiovascular disorders involving the aorta and arteries.
Studying desmosine can provide insights into the pathogenesis of these diseases, and researchers may use tools like MATLAB, Simplicity 185, or NanoDrop ND-1000 to analyze desmosine data.
In addition to its role in health and disease, desmosine is also found in other connective tissues, such as those containing fibrinogen.
Researchers may investigate desmosine levels in the context of treatments like SeQuent Please or Orsiro, which can affect the extracellular matrix and elastin content.
By understanding desmosine's function and regulation, scientists can contribute to the development of new diagnostic and therapeutic approaches for conditions involving connective tissue impairment.