Cyr61, a product of a growth factor-inducible immediate-early gene, promotes cell proliferation, migration, and adhesion.

cyr61 was first identified as a growth factor-inducible immediate-early gene in mouse fibroblasts. The encoded Cyr61 protein is a secreted, cystein-rich heparin-binding protein that associates with the cell surface and the extracellular matrix, and in these aspects it resembles the Wnt-1 protein and a number of known growth factors. During embryogenesis, cyr61 is expressed most notably in mesenchymal cells that are differentiating into chondrocytes and in the vessel walls of the developing circulatory system.

Adenosine output from dog gracilis muscle during systemic hypercapnia and/or amiloride-SITS infusion.

The influence of acidosis on adenosine output from the isolated constant-flow-perfused gracilis muscle was studied in anesthetized dogs. Depression of intracellular pH (pHi) by supplementation of the inspired air with 10% CO2-90% O2 increased arterial PCO2 from 34.2 +/- 1.

Potentiation of thyrotropin-releasing hormone-stimulated prolactin mRNA levels in GH3 cells by acetylcholine.

We have examined the effect of acetylcholine (ACh) pretreatment on the thyrotropin-releasing hormone (TRH) induced prolactin gene expression in GH3 cells, a rat pituitary tumor cell line. Prolonged exposure (greater than 6 h) to ACh enhanced the TRH-induced prolactin mRNA accumulation in a time- and concentration-dependent manner while ACh by itself did not affect the basal prolactin mRNA levels appreciably. Maximal augmentation of the TRH-induced prolactin mRNA accumulation was obtained when cells were pretreated with 10(-5) M ACh for 24 h.

An EXAFS, and preliminary X-ray crystallographic, investigation of an iron-containing product from the lichen Cladonia deformis.

An iron-containing product in the acetone extract from the lichen Cladonia deformis has been investigated using chemical, spectroscopic and X-ray crystallographic methods. Visible-near UV, EPR and IR spectra indicate that the iron is present as high-spin Fe(III) and coordinates in an oxygen-containing environment arising from graciliformin (or graciliformin-like) ligands. This has been confirmed by an XAS (X-ray absorption) study using synchrotron radiation.