Increased detection rate of glaucomatous visual field damage with locally condensed grids: a comparison between fundus-oriented perimetry and conventional visual field examination.

Objective: To compare detection rates of glaucomatous visual field defects (VFDs) between the conventional 6 degrees x 6 degrees stimulus grid and locally condensed target arrangements in morphologically suspicious regions.

Methods: A total of 66 eyes of 66 patients with glaucoma or patients suspected of having glaucoma (34 females and 32 males; age range, 14-85 years) were enrolled in this study. Individual, local target condensation was realized by fundus-oriented perimetry (FOP) using a campimeter and compared with the results of conventional automated perimetry (CAP), obtained with the Humphrey Field Analyzer (30-2 grid).

RGM is a repulsive guidance molecule for retinal axons.

Axons rely on guidance cues to reach remote targets during nervous system development. A well-studied model system for axon guidance is the retinotectal projection. The retina can be divided into halves; the nasal half, next to the nose, and the temporal half.

Evaluation of glaucomatous visual field loss with locally condensed grids using fundus-oriented perimetry (FOP).

Purpose: We compared detection rates of glaucomatous visual field defects (VFDs) between a conventional rectangular stimulus grid and locally condensed test point arrangements in morphologically suspicious regions.

Methods: Humphrey Field Analyzer model 630 (HFA I, program 30-2 with a rectangular 6 degrees x 6 degrees grid) was used as the conventional perimetric method. Individual local test-point condensation was realized by fundus-oriented perimetry (FOP) on the Tuebingen Computer Campimeter (TCC).

Nucleotide sequence and molecular variants of rat receptor-type protein tyrosine phosphatase-zeta/beta.

We have previously described the cloning of phosphacan, a chondroitin sulfate proteoglycan of nervous tissue which interacts with neurons, glia, neural cell adhesion molecules, and tenascin, and represents the extracellular domain of a receptor-type protein tyrosine phosphatase. We now report the complete cDNA and deduced amino acid sequences of the rat transmembrane phosphatase, and demonstrate that the phosphatase and the extracellular proteoglycan have different 3'-untranslated regions. Northern analysis showed three probable splice variants, comprising the extracellular proteoglycan (phosphacan) and long and short forms of the transmembrane phosphatase.

Interactions of the chondroitin sulfate proteoglycan phosphacan, the extracellular domain of a receptor-type protein tyrosine phosphatase, with neurons, glia, and neural cell adhesion molecules.

Phosphacan is a chondroitin sulfate proteoglycan produced by glial cells in the central nervous system, and represents the extracellular domain of a receptor-type protein tyrosine phosphatase (RPTP zeta/beta). We previously demonstrated that soluble phosphacan inhibited the aggregation of microbeads coated with N-CAM or Ng-CAM, and have now found that soluble 125I-phosphacan bound reversibly to these neural cell adhesion molecules, but not to a number of other cell surface and extracellular matrix proteins. The binding was saturable, and Scatchard plots indicated a single high affinity binding site with a Kd of approximately 0.