Search results for "Calponin"

showing 4 items of 4 documents

Arrangement of myofibroblastic and smooth muscle-like cells in superficial peritoneal endometriosis and a possible role of transforming growth factor…

2018

Purpose: Superficial peritoneal endometriotic (pEM) lesions are composed of endometrial glands and stroma, in addition to a third component—myofibroblasts and smooth muscles (SM)-like cells. The latter develops secondary to a metaplasia. In this study, we characterised the third component cells in pEM according to differentiation markers in different micro-compartments. Furthermore, a possible effect of TGFβ1 on myofibroblastic metaplasia in endometriotic epithelial cells was studied. Methods: Seventy-six premenopausal patients were included. Peritoneal biopsies were excised from EM patients (n = 23), unaffected peritoneum (peritoneum from EM patients but without EM components, n = 5/23) an…

0301 basic medicineAdultPathologymedicine.medical_specialtyCalponinEndometriosisPeritoneal DiseasesTransforming Growth Factor beta103 medical and health sciences0302 clinical medicineStromaPeritoneumMetaplasiamedicineHumansEndometriosiMyofibroblastsMyofibroblastMetaplasia030219 obstetrics & reproductive medicinebiologybusiness.industryPeritoneal endometriosiPeritoneal fluidTGFβ1Obstetrics and GynecologyCell DifferentiationMuscle SmoothGeneral MedicineTransforming growth factor beta030104 developmental biologymedicine.anatomical_structurePeritoneal Diseasebiology.proteinSmooth muscle-like cellDesminFemalemedicine.symptomPeritoneumbusinessMyofibroblastMyofibroblastic metaplasiaHumanArchives of gynecology and obstetrics
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Structure of the human filamin A actin-binding domain.

2009

Filamin A (FLNa) is a large dimeric protein that binds to actin filaments via its actin-binding domain (ABD). The crystal structure of this domain was solved at 3.2 A resolution. The domain adopts a closed conformation typical of other ABDs, but also forms a dimer both in crystallization conditions and in solution. The structure shows the localization of the residues mutated in patients with periventricular nodular heterotopia or otopalatodigital syndrome. Structural analysis predicts that mutations in both types of disorder may affect actin binding.

Models Molecularanimal structuresDimerFilaminsmacromolecular substancesFilaminCalponin homology domainCrystallography X-Raychemistry.chemical_compoundContractile ProteinsStructural BiologyFLNAHumansProtein Interaction Domains and MotifsActin-binding proteinProtein Structure QuaternaryActinbiologyMicrofilament ProteinsGeneral MedicineActinschemistryStructural Homology ProteinDomain (ring theory)Mutationbiology.proteinBiophysicsBinding domainProtein BindingActa crystallographica. Section D, Biological crystallography
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Primary cutaneous biphasic sarcomatoid basal cell carcinoma with myoepithelial carcinoma differentiation: A new variant

2019

Isolated cases of basal cell carcinoma (BCC) with partial myoepithelial component have been described. However, myoepithelial differentiation has not been described in sarcomatoid basal cell carcinomas, which usually show features resembling osteosarcoma, chondrosarcoma, or leiomyosarcoma. We report a case of an 87-year-old man with a forehead lesion that histologically showed a minor component of conventional nodular BCC in transition with a major biphasic sarcomatoid growth composed of invasive spindle-cell and epithelial-like components, the latter with a reticular pattern and scattered ductal structures. Both components showed cytological atypia and high mitotic rate (26/10HPF), with at…

Pathologymedicine.medical_specialtyHistologyintegumentary systembiologyGlial fibrillary acidic proteinCalponinMyoepithelial cellDermatologymedicine.diseasePathology and Forensic Medicine030207 dermatology & venereal diseases03 medical and health sciences0302 clinical medicine030220 oncology & carcinogenesisbiology.proteinmedicineAtypiaOsteosarcomaBasal cell carcinomaChondrosarcomaImmunostainingJournal of Cutaneous Pathology
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Novel structural insights into F-actin-binding and novel functions of calponin homology domains.

2008

Tandem calponin homology (CH) domains are well-known actin filaments (F-actin) binding motifs. There has been a continuous debate about the details of CH domain-actin interaction, mainly because atomic level structures of F-actin are not available. A recent electron microscopy study has considerably advanced our structural understanding of CH domain:F-actin complex. On the contrary, it has recently also been shown that CH domains can bind other macromolecular systems: two CH domains from separate polypeptides Ncd80, Nuf2 can form a microtubule-binding site, as well as tandem CH domains in the EB1 dimer, while the single C-terminal CH domain of alpha-parvin has been observed to bind to a alp…

biologyTandemChemistryDimerCalponinCalcium-Binding ProteinsMicrofilament ProteinsF-actin bindingmacromolecular substancesMicrotubulesActinschemistry.chemical_compoundCrystallographyActin CytoskeletonMicroscopy ElectronStructural BiologyStructural Homology Proteinbiology.proteinProtein Interaction Domains and MotifsPaxillinMolecular BiologyActinPaxillinMacromoleculeProtein Binding
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