Role of protein kinase C in intestinal ischemic preconditioning.

Introduction: Tissue protection by ischemic preconditioning (IPC) has been previously characterized in organs such as the heart and involves at least in part PKC activation. It is not yet clear whether such preconditioning against ischemia/reperfusion (I/R) injury operates in the intestine, and, if so, whether IPC involves protein kinase C (PKC).

Materials And Methods: IPC of the small intestine in male Sprague Dawley rats was induced by 10-min superior mesenteric artery (SMA) clamp followed by 120-min reperfusion.

K+ channel inhibition accelerates intestinal epithelial cell wound healing.

Restitution is the process by which superficial interruptions in the gastrointestinal mucosa are repaired by the flattening and spreading of epithelial cells surrounding the damage. During this process, mucosal epithelial cells undergo extensive reshaping and cytoskeletal remodeling. K(+) channels, located primarily on the basolateral surface of gut epithelial cells, are central to both actin polymerization, via their control of membrane potential, and cell volume regulation.

Bryostatin-1 enhances barrier function in T84 epithelia through PKC-dependent regulation of tight junction proteins.

Protein kinase C (PKC) is known to regulate epithelial barrier function. However, the effect of specific PKC isozymes, and their mechanism of action, are largely unknown. We determined that the nonphorbol ester PKC agonist bryostatin-1 increased transepithelial electrical resistance (TER), a marker of barrier function, in confluent T84 epithelia.

Electrogenic ion transport in mammalian colon involves an ammonia-sensitive apical membrane K+ conductance.

It is remarkable that high ammonia concentrations can be present within the colonic lumen without compromising normal epithelial function. We investigated the impact of luminal ammonia on Cl- secretion in native tissue. Stripped human colonic mucosa and unstripped rat distal colon were used.

Bryostatin-1 attenuates TNF-induced epithelial barrier dysfunction: role of novel PKC isozymes.

Tumor necrosis factor (TNF) increases epithelial permeability in many model systems. Protein kinase C (PKC) isozymes regulate epithelial barrier function and alter ligand-receptor interactions. We sought to define the impact of PKC on TNF-induced barrier dysfunction in T84 intestinal epithelia.

Opposing effects of PKCalpha and PKCepsilon on basolateral membrane dynamics in intestinal epithelia.

PKC is a critical effector of plasma membrane dynamics, yet the mechanism and isoform-specific role of PKC are poorly understood. We recently showed that the phorbol ester PMA (100 nM) induces prompt activation of the novel isoform PKCepsilon followed by late activation of the conventional isoform PKCalpha in T84 intestinal epithelia. PMA also elicited biphasic effects on endocytosis, characterized by an initial stimulatory phase followed by an inhibitory phase.