Lax eyelid syndrome (LES), obstructive sleep apnea (OSA), and ocular surface inflammation.

Purpose: Lax eyelid syndrome (LES) is defined as the association of distensible "floppy" eyelids and chronic papillary conjunctivitis. LES is also found in patients with obstructive sleep apnea (OSA) who have systemic elevation of inflammatory markers, including matrix metalloproteinases (MMP). Locally elevated MMP levels have also been demonstrated co-localized with elastin loss in eyelids of patients with LES, accounting for their "floppiness.

Metal-ion binding to parvalbumin. A 113Cd-n.m.r. study of the binding of different lanthanide ions.

113Cd-n.m.r.

Observation of the 43Ca NMR signals from Ca2+ ions bound to calmodulin, parvalbumin, and troponin C.

Through the combined use of isotopically enriched 43Ca2+, high magnetic field, Fourier transform techniques, and a high-performance probe, the 43Ca NMR signals from ions bound to three proteins have been observed. These proteins are calmodulin, parvalbumin, and troponin C. Both longitudinal (1/T1) and transverse (1/T2) relaxation rates were measured for protein-bound 43Ca2+, and the quadrupole coupling constant and correlation time were obtained from these data.

NMR studies on parvalbumin phylogeny and ionic interactions.

The inspection of several muscular parvalbumins from different species by two NMR methods (113Cd resonance and 1H relaxation measurements) allows two classes of parvalbumins to be distinguished according to their ion-binding properties. This result is in agreement with the phylogenetic classification of parvalbumins in two series, alpha and beta, which was established on the basis of the primary structures of these proteins. All parvalbumins are characterized by the presence of two primary cationic sites CD and EF, with structural features closely related to those already known on the basis of X-ray crystallographic studies of the beta parvalbumin pI 4.