Entry of monocytes into the brain after injection of Corynebacterium parvum.

The receptiveness of the brain to monocyte infiltration was studied in rats that had been injected intracerebrally with Corynebacterium parvum. At 0-17 days after intracerebral injection and 18 h after intravenous injection of diI-labeled isogenous mononuclear cells, host rats were sacrificed and cells from the vicinity of the injection site and from the contralateral cerebral hemisphere were dissociated and analyzed by flow cytometry. In rats sacrificed 4-11 days postinjection of C.

Distribution and hormonal regulation of androgen receptor (AR) and AR messenger ribonucleic acid in the rat hippocampus.

The actions of androgens in both peripheral and central tissues are linked in part to their ability to specifically bind and activate androgen receptors (ARs). ARs have been well studied in the rat hypothalamus and peripheral reproductive tissues, where they are directly involved in endocrine feedback mechanisms and reproduction. Previous studies revealed relatively high levels of AR and AR messenger RNA (mRNA) in the rat hippocampus; however, the action of androgen in this brain region remains unclear.

Cell-specific expression of high levels of human S100 beta in transgenic mouse brain is dependent on gene dosage.

The beta-subunit of S100 protein (S100 beta) is highly conserved in the mammalian brain. The gene coding for human S100 beta has been mapped to chromosome 21. In order to study the consequences of overexpression of the S100 beta gene, transgenic mice were generated by microinjection of a 17.

Cloning and expression of the human S100 beta gene.

S100 protein is a low molecular weight, EF-hand, Ca2(+)-binding protein widely distributed and conserved in the central nervous system of vertebrates. The gene coding for the beta subunit of human S100 protein (S100 beta) has been recently mapped to chromosome 21. In order to study the expression of this gene in normal and abnormal brain development, we have isolated and characterized overlapping genomic clones spanning the region coding for human S100 beta and its flanking sequences.

S100 protein and Down syndrome.

S100 protein is a low molecular weight calcium-binding protein widely distributed in the central nervous system of vertebrates. Recent evidence suggests that S100 protein may play a role in the regulation of glial proliferation and neuronal differentiation. The gene for S100 protein has been mapped to the 21q22 region, a chromosomal locus whose duplication has been implicated in the generation of Down Syndrome (DS).

Refined sublocalization of the human gene encoding the beta subunit of the S100 protein (S100B) and confirmation of a subtle t(9;21) translocation using in situ hybridization.

The gene which encodes the beta subunit of the S100 protein was mapped to 21q22.2----q22.3 by in situ hybridization.

Gene encoding the beta subunit of S100 protein is on chromosome 21: implications for Down syndrome.

S100 protein is a calcium-binding protein found predominantly in the vertebrate nervous system. Genomic and complementary DNA probes were used in conjunction with a panel of rodent-human somatic cell hybrids to assign the gene for the beta subunit of S100 protein to the distal half of the long arm of human chromosome 21. This gene was identified as a candidate sequence which, when expressed in the trisomic state, may underlie the neurologic disturbances in Down syndrome.

Reduction in S100 protein beta subunit mRNA in C6 rat glioma cells following treatment with anti-microtubular drugs.

S100 protein is a calcium-binding protein found in vertebrate nervous tissue. Synthesis of S100 protein in the rat glioma cell line, C6, is inhibited by the addition of anti-microtubular drugs. We have cloned a cDNA for the beta subunit of S100 protein from rat brain in a lambda gt 11 expression vector and used this cDNA to measure the amounts of S100 beta subunit mRNA in C6 cells after treatment with anti-microtubular drugs.

A recommendation for visualizing disulfide bonding by one-dimensional sodium dodecyl sulfate--polyacrylamide gel electrophoresis.

A simple modification of the conventional one-dimensional sodium dodecyl sulfate--polyacrylamide gel electrophoresis technique has been used to visualize inter- and intramolecular disulfide bonding in proteins. The gradient of reducing agent established between adjacent slab gel tracks by electrophoresing identical protein samples next to one another, one containing and the other not containing 2-mercaptoethanol, has been used to visualize the change in mobility of disulfide bond-containing proteins throughout the transition from a reducing to a nonreducing environment. As illustrated by an analysis of immunoglobulin heavy and light chains, the method particularly facilitates the positive identification of proteins containing intrachain disulfide bonds.

Inter- and intramolecular disulfide bonding among lymphocyte plasma membrane proteins and glycoproteins.

The disulfide bonding characteristics of the pig lymph node plasma membrane (PM) proteins and glycoproteins have been examined by 1- and 2-dimensional sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Reaction of the purified PM vesicles with N-ethyl maleimide (NEM) prior to detergent solubilization was found to markedly reduce the extent of intermolecular disulfide bonding subsequently observed. Thus the blocking of free sulfhydryl groups with NEM prevented the detergent-induced disulfide bonding of numerous components, including PM-bound actin.

Structural studies of purified pig lymph node plasma membrane: association of cytoskeletal compounds with the plasma membrane and the effect of detergent solubilization.

The reproducibility of preparation, stability at 4 degrees C, and detergent solubilization characteristics of plasma membrane vesicles purified from domestic pig mesenteric lymph node tissue have been examined. It was found that 2% (w/v) Nonidet P-40 solubilized 50-60% and 2% (w/v) sodium deoxycholate solubilized 60-70% of the total membrane protein. As judged by 125I-labelled lentil lectin staining of the sodium dodecyl sulfate--polyacrylamide gel electrophoresis patterns, 2% (w/v) Nonidet p-40 solubilized approximately 73%, and 2% (w/v) sodium deoxycholate approximately 82% of the total glycoprotein.