Knowledge of risk factors for greater procedural pain intensity identified in this study may help clinicians select interventions that are needed to minimize procedural pain. Clinical trial registered with www.clinicaltrials.gov (NCT 01070082).
Missing data are common and generate interpretation biases. They should be reported routinely and taken into account when modelling data from clinical studies.
Regulation of integrin affinity and clustering plays a key role in the control of cell adhesion and migration. The protein ICAP-1␣ (integrin cytoplasmic domain-associated protein-1␣) binds to the cytoplasmic domain of the  1A integrin and controls cell spreading on fibronectin. Here, we demonstrate that, despite its ability to interact with  1A integrin, ICAP-1␣ is not recruited in focal adhesions, whereas it is colocalized with the integrin at the ruffling edges of the cells. ICAP-1␣ induced a rapid disruption of focal adhesions, which may result from the ability of ICAP-1␣ to inhibit the association of  1A integrin with talin, which is crucial for the assembly of these structures. ICAP-1␣-mediated dispersion of  1A integrins is not observed with  1D integrins that do not bind ICAP. This strongly suggests that ICAP-1␣ action depends on a direct interaction between ICAP-1␣ and the cytoplasmic domain of the  1 chains. Altogether, these results suggest that ICAP-1␣ plays a key role in cell adhesion by acting as a negative regulator of  1 integrin avidity.
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