Search results for "Type I collagen"

showing 10 items of 28 documents

Visualizing In Vitro Type I Collagen Fibrillogenesis by Transmission Electron Microscopy

2017

Techniques and protocols for the in vitro formation of collagen type I fibrils and the extensive biochemical variation of the fibrillogenesis conditions are presented. In all cases, the incubation and fibrillogenesis product can be readily monitored by transmission electron microscopic study of negatively stained specimens. Representative TEM data is presented and discussed within the context of the products of the fibrillogenesis protocols, from which the extensive biochemical and structural possibilities of this integrated approach can be appreciated.

0301 basic medicineChemistryfood and beveragesFibrillogenesisContext (language use)02 engineering and technology021001 nanoscience & nanotechnologyFibrilNegative stainIn vitrolaw.invention03 medical and health sciences030104 developmental biologyTransmission electron microscopylawBiophysicsElectron microscope0210 nano-technologyType I collagen
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The Commensal Microbiota Enhances ADP-Triggered Integrin αIIbβ3 Activation and von Willebrand Factor-Mediated Platelet Deposition to Type I Collagen

2020

The commensal microbiota is a recognized enhancer of arterial thrombus growth. While several studies have demonstrated the prothrombotic role of the gut microbiota, the molecular mechanisms promoting arterial thrombus growth are still under debate. Here, we demonstrate that germ-free (GF) mice, which from birth lack colonization with a gut microbiota, show diminished static deposition of washed platelets to type I collagen compared with their conventionally raised (CONV-R) counterparts. Flow cytometry experiments revealed that platelets from GF mice show diminished activation of the integrin αIIbβ3 (glycoprotein IIbIIIa) when activated by the platelet agonist adenosine diphosphate (ADP). Fu…

0301 basic medicineMaleGene Expression030204 cardiovascular system & hematologyvon Willebrand factorlcsh:Chemistrychemistry.chemical_compoundMice0302 clinical medicinePlateletToll-like receptor-2lcsh:QH301-705.5SpectroscopyMice KnockoutbiologyChemistryBrief ReportαIIbβ3General MedicineArteriesComputer Science ApplicationsCell biologyAdenosine DiphosphatePlatelet Glycoprotein GPIb-IX Complexgerm-freeplateletsFemaleType I collagenBlood PlateletsIntegrinPrimary Cell CulturePlatelet Glycoprotein GPIIb-IIIa ComplexCatalysisCollagen Type IInorganic Chemistry03 medical and health sciencesVon Willebrand factormedicineCell AdhesionmicrobiotaAnimalsGerm-Free LifeHumansPhysical and Theoretical ChemistryThrombusSymbiosisMolecular Biologyα<sub>IIb</sub>β<sub>3</sub>Innate immune systemOrganic ChemistryThrombosismedicine.diseaseImmunity InnateToll-Like Receptor 2Gastrointestinal MicrobiomeMice Inbred C57BLAdenosine diphosphateTLR2030104 developmental biologylcsh:Biology (General)lcsh:QD1-999biology.proteinInternational Journal of Molecular Sciences
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Fracture Mechanics of Collagen Fibrils: Influence of Natural Cross-Links

2013

AbstractTendons are important load-bearing structures, which are frequently injured in both sports and work. Type I collagen fibrils are the primary components of tendons and carry most of the mechanical loads experienced by the tissue, however, knowledge of how load is transmitted between and within fibrils is limited. The presence of covalent enzymatic cross-links between collagen molecules is an important factor that has been shown to influence mechanical behavior of the tendons. To improve our understanding of how molecular bonds translate into tendon mechanics, we used an atomic force microscopy technique to measure the mechanical behavior of individual collagen fibrils loaded to failu…

AdultMaleTailMechanical PhenomenaBiophysicsModulusFibrilta3111Collagen fibrilPatellar LigamentTensile StrengthUltimate tensile strengthmedicineAnimalsHumansMolecular Machines Motors and Nanoscale Biophysicsta315Mechanical PhenomenaChemistryFracture mechanicsta3141AnatomyHydrogen-Ion ConcentrationMiddle Agedmusculoskeletal systemTendonBiomechanical PhenomenaRatsmedicine.anatomical_structureSolubilityBiophysicsCollagenType I collagenBiophysical Journal
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Combined evaluation of resting IGF-I, N-terminal propeptide of type III procollagen (PIIINP) and C-terminal cross-linked telopeptide of type I collag…

2004

To verify whether combined measurements of GH-dependent parameters might be useful in detecting exogenous recombinant GH (rGH) administration in male athletes from different disciplines.Sixty-six athletes (control group) were sampled for the evaluation of resting IGF-I, N-terminal propeptide of type III procollagen (PIIINP) and telopeptide type I collagen (ICTP). Cut-off values (mean + 2 SD) for IGF-I, PIIINP and ICTP were calculated and arbitrary scores (1.5, 2.0) were assigned to abnormal parameters. By using the sum of individual parameter scores, positive (or = 3) or negative (3) scores were obtained. In addition, a subgroup of six athletes was treated for 3 weeks with rGH (0.09 IU/kg b…

AdultMalemedicine.medical_specialtyAdolescentEndocrinology Diabetes and MetabolismRhgh treatmentSensitivity and SpecificityCollagen Type IEndocrinologyN-terminal telopeptidePreliminary reportInternal medicinemedicineHumansInsulin-Like Growth Factor IDoping in Sportsbiologybusiness.industryAthletesN terminal propeptidebiology.organism_classificationPeptide FragmentsType III ProcollagenProcollagen peptidaseEndocrinologyCase-Control StudiesGrowth HormonebusinessPeptidesType I collagenBiomarkersProcollagenSportsClinical endocrinology
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Biochemical bone markers compared with bone density measurement by dual energy X-ray absorptiometry

1995

In contrast to medical imaging, the biochemical markers allow a more frequent determination and are not as invasive as histomorphometric methods. We investigated biochemical markers of type I collagen compared with bone density measurements in 85 females between 41 and 89 years of age (median: 57 years). The bone density measurements were performed by dual energy X-ray absorptiometry (DXA) on the lumbar spine (L1-4). The bone density measurements were stated as a percentage of the norm. All patients were divided into three groups: I =80%; II = 80-130%; III =120%. Based on this classification the median concentration of the I-carboxyterminal propeptide of type I collagen in serum (S-PICP) as…

AdultPathologymedicine.medical_specialtyAnabolismBone densityEndocrinology Diabetes and MetabolismBone and BonesCollagen Type IBone remodelingAbsorptiometry PhotonEndocrinologyN-terminal telopeptideBone DensityInternal medicinemedicineHumansOrthopedics and Sports MedicineDual-energy X-ray absorptiometryAgedAged 80 and overbiologymedicine.diagnostic_testChemistryLiterMiddle AgedPeptide FragmentsEndocrinologyOsteocalcinbiology.proteinRegression AnalysisFemaleCollagenPeptidesBiomarkersProcollagenType I collagenCalcified Tissue International
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Serum and urine markers of type I collagen metabolism in elderly women with high and low bone mineral density.

1996

The serum markers of bone formation (carboxy-terminal propeptide of type I collagen, PICP) and resorption (pyridinoline cross-links containing telopeptide of type I collagen, ICTP), as well as urinary resorption markers, pyridinoline (Pyr) and deoxypyridinoline (Dpyr), were studied in 78-year-old women with high (n = 18) and low (n = 17) bone mineral density (BMD) measured from the calcaneus and tibia. The low-BMD group had higher values for PICP (P = 0 center dot 025), Pyr (P = 0 center dot 001) and Dpyr (P < 0 center dot 001) than the high-BMD group. No inverse relationship between these markers and BMD was, however, observed within the study groups. ICTP, Pyr and Dpyr correlated with eac…

Bone mineralmedicine.medical_specialtyDeoxypyridinolineAgingPyridinolineBone densityClinical BiochemistryGeneral Medicinemusculoskeletal systemBiochemistryResorptionBone remodelingchemistry.chemical_compoundEndocrinologychemistryN-terminal telopeptideBone DensityInternal medicinemedicineHumansFemaleCollagenType I collagenAgedEuropean journal of clinical investigation
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Silica as a morphogenetically active inorganic polymer.

2013

At present the scaffolds used for bioprinting of cells do not elicit morphogenetic responses in the cells. In the present study we approached a solution by studying the effect of an inorganic silica supplement added to an Na-alginate matrix. Bone- and osteoblast-like SaOS-2 cells were embedded into this organic polymeric matrix which was additionally enriched with 400 μM prehydrolyzed TEOS [tetra-ethoxy-silane], a source of ortho-silicate. In this silica-based matrix the cells synthesized hydroxyapatite crystallites after exposure to a mineralization activation cocktail composed of β-glycerophosphate, ascorbic acid and dexamethasone. The degree of hydroxyapatite synthesis, determined by sta…

Bone sialoprotein0303 health sciencesbiologyChemistryBiomedical Engineering02 engineering and technology021001 nanoscience & nanotechnologyAscorbic acidMineralization (biology)03 medical and health sciencesstomatognathic systemBiochemistrybiology.proteinOsteocalcinAlkaline phosphataseGeneral Materials ScienceOsteopontinOsteonectin0210 nano-technologyType I collagen030304 developmental biologyBiomaterials science
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PLLA scaffolds produced by thermally induced phase separation (TIPS) allow human chondrocyte growth and extracellular matrix formation dependent on p…

2016

Damage of hyaline cartilage species such as nasoseptal or joint cartilage requires proper reconstruction, which remains challenging due to the low intrinsic repair capacity of this tissue. Implantation of autologous chondrocytes in combination with a biomimetic biomaterial represents a promising strategy to support cartilage repair. The aim of this work was to assess the viability, attachment, morphology, extracellular matrix (ECM) production of human articular and nasoseptal chondrocytes cultured in vitro in porous poly(L-lactic) (PLLA) scaffolds of two selected pore sizes (100 and 200 μm). The PLLA scaffolds with 100 and 200 μm pore sizes were prepared via ternary thermally induced ph…

Cartilage ArticularMaterials sciencePolyesters0206 medical engineeringType II collagenBioengineeringCondensed Matter Physic02 engineering and technologyChondrocyteBiomaterialsExtracellular matrixChondrocytesTissue engineeringmedicineHumansMechanics of MaterialCells CulturedAggrecanType II collagenSettore ING-IND/24 - Principi Di Ingegneria ChimicaTissue EngineeringTissue ScaffoldsHyaline cartilageMechanical EngineeringCartilageSettore ING-IND/34 - Bioingegneria IndustrialeAnatomy021001 nanoscience & nanotechnology020601 biomedical engineeringExtracellular MatrixArticular chondrocyteCartilagemedicine.anatomical_structureMechanics of MaterialsBiophysicsPoly(L)lactic acidMaterials Science (all)0210 nano-technologyPorosityNasoseptal chondrocyteType I collagenMaterials Science and Engineering: C
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Influence of Extracellular Matrix on the Lipogenesis of Cultured White Fat Cells.

1998

Collagenase digests from subcutaneous fat tissue of new born rats were cultured on different types of collagen gel containing 50% type I collagen, on fibronectin (Fn) or on laminin (Lm). On day 6, 17% of cells on a plastic substratum differentiated and had multilocular or unilocular cytoplasmic lipid droplets (CLDs). Cells on each type of collagen and on Lm had more CLDs than those on a plastic substratum. The extent of lipogenesis showed the following decreasing order: cells on Lm (80%), on type IV+I collagen (70%), on type I collagen (52%), on type III+I collagen (36%), on type II+I collagen (32%). On day 14, most cells on Lm became unilocular fat cells. Cells on Fn showed delipidation an…

HistologybiologyPhysiologyCell BiologyFat cell differentiationBiochemistryMolecular biologyPathology and Forensic MedicineFibronectinExtracellular matrixCollagen type I alpha 1Type IV collagenBiochemistryLamininbiology.proteinCollagenasemedicineType I collagenmedicine.drugACTA HISTOCHEMICA ET CYTOCHEMICA
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Integrin alpha(2)I domain recognizes type I and type IV collagens by different mechanisms.

2000

The collagens are recognized by the alphaI domains of the collagen receptor integrins. A common structural feature in the collagen-binding alphaI domains is the presence of an extra helix, named helix alphaC. However, its participation in collagen binding has not been shown. Here, we have deleted the helix alphaC in the alpha(2)I domain and tested the function of the resultant recombinant protein (DeltaalphaCalpha(2)I) by using a real-time biosensor. The DeltaalphaCalpha(2)I domain had reduced affinity for type I collagen (430 +/- 90 nM) when compared with wild-type alpha(2)I domain (90 +/- 30 nM), indicating both the importance of helix alphaC in type I collagen binding and that the collag…

IntegrinsIntegrinIntegrin alpha2CHO CellsBiochemistryCollagen receptorType IV collagenIntegrin alpha2Antigens CDCricetinaeAnimalsBinding siteMolecular BiologyBinding SitesbiologyChemistryChinese hamster ovary cellCell BiologyMolecular biologyRecombinant ProteinsCollagen type I alpha 1biology.proteinMutagenesis Site-DirectedCollagenType I collagenProtein BindingThe Journal of biological chemistry
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