Biomedical subjects

J Rothlein

Publications and source records attributed to J Rothlein.

3 recordsLinked to original sources

PubMed2001

Work characteristics and pesticide exposures among migrant agricultural families: a community-based research approach.

There are few data on pesticide exposures of migrant Latino farmworker children, and access to this vulnerable population is often difficult. In this paper we describe a community-based approach to implement culturally appropriate research methods with a migrant Latino farmworker community in Oregon. Assessments were conducted in 96 farmworker homes and 24 grower homes in two agricultural communities in Oregon. Measurements included surveys of pesticide use and work protection practices and analyses of home-dust samples for pesticide residues of major organophosphates used in area crops. Results indicate that migrant farmworker housing is diverse, and the amounts and types of pesticide residues found in homes differ. Azinphos-methyl (AZM) was the pesticide residue found most often in both farmworker and grower homes. The median level of AZM in farmworker homes was 1.45 ppm compared to 1.64 ppm in the entry area of grower homes. The median level of AZM in the play areas of grower homes was 0.71 ppm. The levels of AZM in migrant farmworker homes were most associated with the distance from fields and the number of agricultural workers in the home. Although the levels of AZM in growers and farmworker homes were comparable in certain areas, potential for disproportionate exposures occur in areas of the homes where children are most likely to play. The relationship between home resident density, levels of pesticide residues, and play behaviors of children merit further attention.

Adult↗

PubMed1986

Characterization of synapsin I binding to small synaptic vesicles.

The binding of synapsin I, a synaptic vesicle-associated phosphoprotein, to small synaptic vesicles has been examined. For this study, synapsin I was purified under nondenaturing conditions from rat brain, using the zwitterionic detergent 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate (CHAPS), and characterized. Small synaptic vesicles were purified from rat neocortex by controlled pore glass chromatography as the last purification step, and binding was characterized at an ionic strength equivalent to 40 mM NaCl. After removal of endogenous synapsin I, exogenous dephospho-synapsin I bound with high affinity (Kd, 10 +/- 6 nM) to synaptic vesicles. The binding saturated at 76 +/- 40 micrograms synapsin I/mg of vesicle protein, which corresponded to the amount found endogenously in purified vesicles. Synapsin I binding exhibited a broad pH optimum around pH 7. Other basic proteins, specifically myelin basic protein and histone H2b, did not compete with synapsin I for binding to vesicles. Other membranes purified from rat brain and membranes derived from human erythrocytes did not show the high affinity binding site for synapsin I found in vesicles. The binding of three different forms of phosphosynapsin I to vesicles was investigated. Synapsin I, phosphorylated at sites 2 and 3 by purified calcium/calmodulin-dependent protein kinase II, bound with a 5-fold lower affinity to the vesicles than did dephospho-synapsin I. In contrast, synapsin I, phosphorylated at site 1 by purified catalytic subunit of cAMP-dependent protein kinase, bound with an affinity close to that of dephospho-synapsin I. Synapsin I phosphorylated on all three sites bound to the vesicles with an affinity comparable to that of synapsin I phosphorylated on sites 2 and 3. Under conditions of higher ionic strength (150 mM NaCl equivalent), synapsin I bound with a 5-fold lower affinity to vesicles, and no effect of phosphorylation on binding was observed under these conditions.

Animals↗

PubMed1984

Facilitation of Ca2+-channel currents in bovine adrenal chromaffin cells.

Ca2+-channel currents in primary cultures of bovine adrenal chromaffin cells were studied using the whole-cell patch-clamp method. Parameters of a double-pulse protocol were systematically varied to characterize facilitation by a prepulse (P1) of Ca2+-channel current during a test pulse (P2). The pulses were usually separated by 30 msec, an interval sufficient for decay of any measurable P1 tail currents. The Ca2+-channel current amplitude during P2 increased when P1 voltage was more positive than 0 mV. The effect became progressively greater with more positive P1 voltage. With a 60-msec P1 to +80 mV, the current amplitude typically increased by 25%-35% during a 60-msec P2. Comparison of facilitated and control inward Ca2+-channel current I(V) curves showed that facilitation was also strongly dependent on P2 test voltage. Facilitation of Ca2+-channel currents is a voltage-dependent phenomenon and is not dependent on Ca2+ entry. When short repetitive voltage-clamp pulses were applied, the Ca2+-channel current amplitude increased with each pulse. This suggests that Ca2+-channel facilitation could enhance release of catecholamines from chromaffin cells during a train of action potentials.

Adrenal Medulla↗