0000000000236408

AUTHOR

Sarah Klapproth

showing 2 related works from this author

The fibronectin synergy site re-enforces cell adhesion and mediates a crosstalk between integrin classes

2017

Fibronectin (FN), a major extracellular matrix component, enables integrin-mediated cell adhesion via binding of α5β1, αIIbβ3 and αv-class integrins to an RGD-motif. An additional linkage for α5 and αIIb is the synergy site located in close proximity to the RGD motif. We report that mice with a dysfunctional FN-synergy motif (Fn1syn/syn) suffer from surprisingly mild platelet adhesion and bleeding defects due to delayed thrombus formation after vessel injury. Additional loss of β3 integrins dramatically aggravates the bleedings and severely compromises smooth muscle cell coverage of the vasculature leading to embryonic lethality. Cell-based studies revealed that the synergy site is dispensa…

0301 basic medicineMouseQH301-705.5extracellular matrixScienceExtracellular matrix componentIntegrinHemorrhageGeneral Biochemistry Genetics and Molecular BiologyExtracellular matrixMice03 medical and health sciencesfibronectinAnimalsBiology (General)Cell adhesionRGD motifMice KnockoutGeneral Immunology and MicrobiologybiologyCell adhesion moleculeChemistryGeneral NeuroscienceQRThrombosiscell adhesionCell BiologyGeneral MedicineFibronectinsCell biologyFibronectinCrosstalk (biology)030104 developmental biologymechanosignalingImmunologyintegrinsbiology.proteinMedicineResearch ArticleeLife
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Author response: The fibronectin synergy site re-enforces cell adhesion and mediates a crosstalk between integrin classes

2016

FibronectinCrosstalk (biology)biologyChemistryIntegrinbiology.proteinCell adhesionCell biology
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