0000000000873777

AUTHOR

Ruth Alonso

showing 2 related works from this author

Vitamin A deficiency alters the structure and collagen IV composition of rat renal basement membranes.

2005

Retinoids can modulate the expression of extracellular matrix (ECM) proteins with variable results depending on other contributing factors. Because changes in these proteins may alter the composition and impair the function of specialized ECM structures such as basement membranes (BMs), we studied the effects of vitamin A deficiency on renal BMs during the growing period. Newborn male rats were fed a vitamin A-deficient (VAD) diet for 50 d. The ultrastructure of renal BMs was analyzed by electron microscopy. Total collagen IV, the different alpha(IV) chains, matrix degrading metalloproteinases (MMP), and tissue inhibitors of metalloproteinases (TIMP) were quantified by immunocytochemistry a…

VitaminCollagen Type IVmedicine.medical_specialtyMMP2Kidney GlomerulusMedicine (miscellaneous)BiologyMatrix metalloproteinaseMMP9KidneyBasement MembraneExtracellular matrixchemistry.chemical_compoundInternal medicinemedicineAnimalsRNA MessengerRats WistarTIMP1DNA PrimersBasement membraneKidneyNutrition and DieteticsBase SequenceReverse Transcriptase Polymerase Chain ReactionVitamin A DeficiencyMatrix MetalloproteinasesRatsmedicine.anatomical_structureEndocrinologychemistryFemaleThe Journal of nutrition
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Different adhesins for type IV collagen on Candida albicans: identification of a lectin-like adhesin recognizing the 7S(IV) domain

2001

Adherence of the opportunistic pathogen Candida albicans to basement membrane (BM) proteins is considered a crucial step in the development of candidiasis. In this study the interactions of C. albicans yeast cells with the three main domains of type IV collagen, a major BM glycoprotein, were analysed. C. albicans adhered to the three immobilized domains by different mechanisms. Adhesion to the N-terminal cross-linking domain (7S) required the presence of divalent cations, whereas interaction with the central collagenous domain (CC) was cation-independent. Recognition of the C-terminal non-collagenous domain (NC1) was partially cation-dependent. Binding inhibition assays with the correspondi…

Collagen Type IVGlycosylationImmunoblottingOligosaccharidesBiologyMicrobiologyBasement MembraneType IV collagenOligosaccharide bindingCationsLectinsCandida albicansCell AdhesionAnimalsCandida albicanschemistry.chemical_classificationExtracellular Matrix ProteinsLectinOligosaccharidebiology.organism_classificationCorpus albicansBacterial adhesinchemistryBiochemistrybiology.proteinCattleGlycoproteinMicrobiology
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