Novel role of Egr-1 in nicotine-related neointimal formation.

Aims: The aim of this study was to investigate the mechanisms by which nicotine increases vascular smooth muscle cell (VSMC) proliferation and post-injury neointimal formation.

Methods And Results: Vascular injury was inflicted in the right iliac artery of nicotine-treated and control rats. Nicotine increased post-injury VSMC proliferation (Ki67(+) cells) and neointimal formation (neointima/media ratio, 0.

Aging increases p16 INK4a expression in vascular smooth-muscle cells.

Alteration of VSMC (vascular smooth-muscle cell) physiology is associated with the development of atherosclerosis and restenosis. We hypothesize that aging up-regulates the expression of p16 INK4a in VSMCs, which may increase the susceptibility of blood vessels to vascular occlusive diseases. Aortic VSMCs were obtained from young and aged mice.

The origin of post-injury neointimal cells in the rat balloon injury model.

Aims: The origin of post-injury neointimal cells is still a matter of debate. This study aims to determine the anatomic source of neointimal cells in one of the most important animal models for the study of vascular stenosis in response to injury, the rat balloon injury model.

Methods And Results: Chimeric rats were generated by rescuing lethally irradiated animals with green fluorescent protein (GFP)(+) bone marrow (BM) cells from transgenic rats.

An internal ribosome entry site mediates the initiation of soluble guanylyl cyclase beta2 mRNA translation.

The soluble guanylyl cyclases (sGC), the receptor for nitric oxide, are heterodimers consisting of an alpha- and beta-subunit. This study aimed to investigate the translational mechanism of the sGC beta2-subunit. Two mRNA species for sGC beta2 were isolated from human kidney.

Voltage-dependent calcium channels in young and old human red cells.

Presence of subtypes of voltage-dependent Ca channels was investigated in young and old human red cells, employing immunological and flux-kinetics methods. Western blots showed specific reaction toward polyclonal rabbit antibodies raised against a highly conserved residue of alpha1 subunit of high-voltage activated Ca channels (pan alpha1) and against conserved residues of alpha1C and alpha1E subunits. No specific reaction was detected with antibodies against conserved residues of alpha1A, alpha1B, or alpha1D subunits.

Structural determinants for phosphatidic acid regulation of phospholipase C-beta1.

Signaling from G protein-coupled receptors to phospholipase C-beta (PLC-beta) is regulated by coordinate interactions among multiple intracellular signaling molecules. Phosphatidic acid (PA), a signaling phospholipid, binds to and stimulates PLC-beta(1) through a mechanism that requires the PLC-beta(1) C-terminal domain. PA also modulates Galpha(q) stimulation of PLC-beta(1).