Pseudotumor cerebri: a new door opens for treatment.

Pseudotumor cerebri remains a scarcely known pathology. We present the experience of a multidisciplinary working group which studied this disorder focusing on the venous alterations of the dural sinuses. Seventeen cases were studied, diagnosed, controlled and treated by our team.

Novel avian thymic parvalbumin displays high degree of sequence homology to oncomodulin.

CPV3 is a novel avian parvalbumin. It displays an isoelectric point of 4.6, intermediate between that of avian thymic hormone (pI = 4.

Evidence that deprotonation of serine-55 is responsible for the pH-dependence of the parvalbumin Eu3+ 7F0-->5D0 spectrum.

The Eu(III)7F0-->5D0 excitation spectra of the parvalbumins are highly pH-dependent. Below pH 6.0, they exhibit a sharp, partially resolved doublet centered near 5,795 A.

Interactions between residues in the oncomodulin CD domain influence Ca2+ ion-binding affinity.

Despite striking sequence homology with rat parvalbumin, oncomodulin exhibits much lower affinity for Ca2+ ion. We are attempting to identify the structural basis for this difference by systematically substituting the parvalbumin residue for the oncomodulin residue at points of nonidentity. In this paper, we examine two mutations in the helical segments flanking the CD ion-binding loop.

Identification of a novel parvalbumin in avian thymic tissue.

A novel calcium-binding protein has been isolated from chicken thymus tissue. Its molecular weight (approximately 11,500) and characteristic interactions with Tb3+ and Eu3+ identify the protein as a member of the parvalbumin family. Electrophoretically distinct from both chicken (muscle) parvalbumin and avian thymic hormone, it represents the third parvalbumin to be identified in avian tissues and the second to be identified in the avian thymus gland.