We report the purification from pig brain of a factor supporting the survival of, and fibre outgrowth from, cultured embryonic chick sensory neurons. The purified factor migrates as one single band, mol. wt. 12 300, on gel electrophoresis in the presence of sodium dodecylsulphate (SDS) and is a basic molecule (pI greater than or equal to 10.1). Approximately 1 microgram factor was isolated from 1.5 kg brain. The final degree of purification was estimated to be 1.4 X 10(6)-fold, and the specific activity 0.4 ng/ml/unit, which is similar to that of nerve growth factor (NGF) using the same assay system. This factor is the first neurotrophic factor to be purified since NGF, from which it is clearly distinguished because it has different antigenic and functional properties.

Purification of a new neurotrophic factor from mammalian brain.

The distribution of type II Ca2+/calmodulin-dependent protein kinase has been mapped in rat brain by immunochemical and immunohistochemical methods using an antibody against its alpha-subunit. The concentration of the kinase, measured by radioimmunoassay, varies markedly in different brain regions. It is most highly concentrated in the telencephalon where it comprises approximately 2% of the total hippocampal protein, 1.3% of cortical protein, and 0.7% of striatal protein. It is less concentrated in lower brain structures, ranging from about 0.3% of hypothalamic protein to 0.1% of protein in the pons/medulla. The gradient of staining intensity observed in brain sections by immunohistochemistry corroborates this distribution. Neurons and neuropil of the hippocampus are densely stained, whereas little staining is observed in lower brain regions such as the superior colliculus. Within the diencephalon and midbrain, dense staining is observed only in thalamic nuclei and the substantia nigra. The skewed distribution of alpha-subunit appears to be due in part to the occurrence in the cerebellum and pons/medulla of forms of the kinase with a high ratio of beta- to alpha-subunits. However, most of the variation is due to the extremely high concentration of the kinase in particular neurons, especially those of the hippocampus, cortex and striatum. The unusually high expression of the kinase in these neurons is likely to confer upon them specialized responses to calcium ion that are different from those of neurons in lower brain regions.

https://www.jneurosci.org/content/jneuro/5/12/3270.full.pdf

Regional distribution of type II Ca2+/calmodulin-dependent protein kinase in rat brain

Schwann cells have a unique role in regulating the growth of axons during regeneration and presumably during development. Here we show that Schwann cells are the best substrate yet identified for promoting process growth in vitro by peripheral motor neurons. To determine the molecular interactions responsible for Schwann cell regulation of axon growth, we have examined the effects of specific antibodies on process growth in vitro, and have identified three glycoproteins that play major roles. These are the Ca2+-independent cell adhesion molecule (CAM), L1/Ng-CAM; the Ca2+-dependent CAM, N-cadherin; and members of the integrin extracellular matrix receptor superfamily. Two other CAMs present on neurons and/or Schwann cells-N-CAM and myelin-associated glycoprotein-do not appear to be important in regulating process growth. Our results imply that neuronal growth cones use integrin-class extracellular matrix receptors and at least two CAMs--N-cadherin and L1/Ng-CAM-for growth on Schwann cells in vitro and establish each of these glycoproteins as a strong candidate for regulating axon growth and guidance in vivo.

/pdf/identification-of-the-major-proteins-that-promote-neuronal-3zsiwrcehf.pdf

Identification of the major proteins that promote neuronal process outgrowth on Schwann cells in vitro.

https://www.cell.com/neuron/pdf/S0896-6273(00)80155-5.pdf

GGF/Neuregulin Is a Neuronal Signal That Promotes the Proliferation and Survival and Inhibits the Differentiation of Oligodendrocyte Progenitors

How are the numbers of different cell types matched together during tissue development? The nervous system has provided an excellent model system for understanding this question as it contains two main classes of cell types, neurons and glia. Presynaptic neurons are believed to be precisely matched

https://rupress.org/jcb/article-pdf/147/6/1123/1288739/9909103.pdf

Axonal control of oligodendrocyte development.

Purification and preliminary characterization of a glial growth factor from the bovine pituitary.

This is the first report of a quantitative radioimmunoassay for P0. The assay uses antigen-coated plastic microwells, with antibody binding detected by 125I-labeled protein A. Either peripheral myelin proteins or purified P0 may be used as the antigen. Optimal extraction of tissue samples for P0 immunoassay requires careful attention to the sodium dodecyl sulfate-to-protein ratio. Sodium dodecyl sulfate interference with antibody binding can be minimized by adding an excess of nonionic detergent and carrier protein to the incubation buffer. This method allows the detection of 0.8 ng of P0 (20 ng/ml). Results from this assay showed little or no im-munoreactivity in extracts of brain, central myelin, liver, purified myelin basic proteins, cultured, purified second ary Schwann cells, or membrane preparations from these cells. P0 was clearly detectable in Schwann cell cultures from 3- to 4-day-old rats at 12–18 h after dissociation (4% of the level in adult sciatic nerve) and in extracts of one-day-old rat sciatic nerve (2% of the level in adult nerve). Myelin basic protein radioimmunoassays showed that the ratio of P0 to myelin basic protein is essentially constant in extracts of sciatic nerve from one-day-old, four-day-old and young adult rats. Another result was that P0 levels are reduced in the trembler mouse sciatic nerve.

Development and applications of a solid-phase radioimmunoassay for the PO protein of peripheral myelin.

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Purification and preliminary characterization of a glial growth factor from the bovine pituitary.

Development and applications of a solid-phase radioimmunoassay for the PO protein of peripheral myelin.