Search PubMed⌕ Search

Biomedical subjects

J Hoh

Publications and source records attributed to J Hoh.

4 recordsLinked to original sources
PubMed1991

Arecoline-associated changes in open-field behavior following swim stress in the rat. A possible relationship to water temperature.

The rat exhibits a reduction in movement in an open field following a 14-day course of forced swim stress at 12 degrees C. The decrease in movement is greater in rats receiving arecoline relative to those receiving saline prior to placement in the open field. The authors report that when water temperature is increased to 20 degrees, there is a categorical difference in the results. The saline control group exhibits a rise and the arecoline group no change in crossings.

Animals↗
PubMed1990

Chronic swim stress enhances the motoric inhibiting effects of a muscarinic agonist.

The authors previously demonstrated that chronic inescapable swim stress and footshock increase the capacity of a fixed dose of a muscarinic agonist to produce hypothermia in the rat. This project was designed to determine whether chronic inescapable swim stress in cold water would render a low dose of a muscarinic agonist, devoid of an effect on motor behavior in the naive rat (i.e., prior to subjection to the course of swim stress), an inhibitor of mobility. The study involved two groups of rats, an experimental group which received arecoline and a control group which received saline five minutes prior to being placed in an open field. Number of crossings, the dependent variable, was measured in both groups before and after a 14-day course of twice daily inescapable swim stress of 10 minutes duration at 12 degrees C. The arecoline-treated group, as hypothesized, exhibited a significantly greater reduction in number of crossings than the saline-treated groups following the course of swim stress.

Animals↗
PubMed1987

Sequence diversity of gap junction proteins.

This paper summarizes our understanding of the molecular organization of gap junction proteins. There appear to be overall similarities in the organization of heart and liver junctions in terms of general domains, even though the molecular sizes of the two proteins are quite different. Sequence data on the amino-terminal regions of these two proteins show 43% of the residues to be identical and 25% more to be homologous. The major intrinsic protein of lens (MIP), believed by many to be the lens-fibre junction protein, does not show such sequence homology with the known portions of junction proteins from either heart or liver. Yet the sequence of MIP, which is completely known, suggests a conformation for this molecule quite compatible with a junctional role. It thus appears that molecules potentially involved in junction formation will prove to form a rather diverse family, with special characteristics of organ-specific molecules that may well be related to their function.

Amino Acid Sequence↗