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B J McLaughlin

Publications and source records attributed to B J McLaughlin.

At least 91 records · Page 5Linked to original sources
PubMed1980

A freeze-fracture study of synaptic junction development in the superficial layers of the chick optic tectum.

Synaptogenesis in the superficial layers of the rostral pole of the chick optic tectum has been studied using freeze-fracture techniques. The developmental sequence of intramembrane organization at synaptic junctions involves the accumulation and assembly of intramembrane particles into aggregates characteristic of the mature junctions. By embryonic day seven, areas of loosely-arranged clusters of medium-sized particles are observed on the cytoplasmic membrane leaflets (P-faces) of developing neurites. These clusters are characteristic of the intramembrane organization at presynaptic active zones. At later stages, small pits, characteristic of vesicle fusion sites, are observed interspersed among such P-face particle clusters. Complementary intramembrane specializations are also present on the external leaflets (E-faces) of presynaptic membranes at the active zones. Small solitary aggregates of large-sized particles on the E-faces of neurite plasma membranes are also seen at early embryonic stages. As development progresses, these aggregates increase in size and packing density and occupy large oval domains in postsynaptic membranes. These intramembrane specializations may represent the postsynaptic active zones of asymmetric synapses. Another type of intramembrane specialization, observed during the third week of incubation, is characterized by aggregates of small- and medium-sized particles on the P-face of postsynaptic membranes and is often seen directly apposed to the E-face of a presynaptic terminal. This type of intramembrane specialization may represent the postsynaptic active zone region at symmetrical synaptic contacts.

Aging↗
PubMed1980

The localization of lectin binding sites on photoreceptor outer segments and pigment epithelium of dystrophic retinas.

Carbohydrate-containing macromolecules on pigment epithelium (PE) and photoreceptor outer segment (OS) membranes of 14 to 16-day-old Royal College of Surgeons (RCS) rats and their genetic control (RCS-rdy+) have been localized with peroxidase-conjugated lectins from wheat germ agglutinin (WGA), Ricinus communis (RCA), Lens culinaris (LCA), and concanavalin A (Con A). All lectins stain the plasma membranes of photoreceptor inner segments and intact OSs of normal (RCS-rdy+) and dystrophic (RCS) retinas. In the normal retinas, all lectins stain also the plasma membranes of shed OSs, and WGA stains some intradisc membranes. In contrast, WGA, RCA, and Con A do not label the OS debris membranes in dystrophic retinas, but LCA labels some of them. In both normal and dystophic retinas, WGA uniformly labels both proximal and distal membrane surfaces of PE mcirovilli, whereas RCA labels primarily the distal regions. Con A labels both normal and dystrophic PE microvilli sparsely, and LCA stains the PE microvilli in RCS-rdy+ retinas more intensely than those in the RCS retinas. The major differences between the lectin labeling in normal and dystrophic retinas are the presence of LCA staining on OS debris and the absence of any other lectin staining on these membranes. Other differences are the sparse LCA staining on dystrophic PE microvillous membranes vs. the normal and the presence of WGA staining on OS intradisc membranes of normal retinas. These differences may reflect changes in the accessibility or composition of certain cell surface sugars on OS membranes and PE microvilli which may be related to the diminished rate of phagocytosis in RCS retinas.

Agglutinins↗
PubMed1977

Immunocytochemical localization of the sodium, potassium activated ATPase in knifefish brain.

Results presented in this paper demonstrate the feasibility of using immunocytochemical methods to localize the (Na+ + K+)-ATPase, and its subunits, in the C.N.S. We have shown that in the Black Ghost knifefish, Sternarchus albifrons, the enzyme is located on the plasma membrane of the somata and dendrites of neurons and on the somata and cellular processes of glia. In myelinated axons the enzyme is restricted in localization to those portions of the axolemma not covered by the myelin sheath. The capacity of cell plasma membranes to restrict mobility of functionally important proteins should be considered in models of membrane structure in which lateral mobility of membrane components is considered a major characteristic.

Adenosine Triphosphatases↗
PubMed1976

Cytochemical studies of lectin binding sites in smooth membrane cisternae of rat brain.

The cytochemical localization of concanavalin A (con A) binding sites has been studied in Purkinje cell axons and presynaptic terminals of rat cerebellum. Smooth membrane cisternae just beneath the axolemma contain con A binding sites on the side of the membrane facing the cisternal space. At certain regions, such as the node of Ranvier, these cisternae lie in virtual apposition to the axolemma. Such a specialized system of cisternae could serve as a channel through which some of the materials synthesized in the Purkinje somata are moved to the axon terminals. The close association of the cisternae and axolemma at certain regions could be a site at which some of the transported materials contribute to renewal of the axolemma. The con A binding sites on intracellular membranes of the Purkinje cell are removed by prior glycosidic and proteolytic enzyme digestions. The results suggest that at least some of the carbohydrates lining membrane cisternae are glycoprotein in nature.

Animals↗
PubMed1976

A fine structural and E-PTA study of photoreceptor synaptogenesis in the chick retina.

Photoreceptor synaptogenesis in the embryonic and hatchling chick retina was studied with conventional EM techniques and ethanolic phosphotungstic acid (E-PTA). The photoreceptors line up between 11 and 13 embryonic days with their undifferentiated synaptic bases facing the outer plexiform layer (OPL). E-PTA staining at 11 embryonic days does not reveal any para-membranous specializations of the receptors but numerous stained punctae adhaerentes are observed in the OPL. At 13 embryonic days neurites of presumed bipolar and horizontal neurons are aligned parallel to the bases of the receptors and cytoplasmic protrusions of the receptors project between some of these neurites to form dyad appositions. An osmiophilic undercoating, which is not E-PTA positive at this time, is present on the cytoplasmic face of the receptor membrane in these apposition regions. Between 13 and 15 embryonic days the filopodial protrusions of the receptors continue to elongate further and become aligned with neurites in dyad and triad appositions. The osmiophilic undercoating now extends along the entire inner surface of the receptor pedicle protrusions and becomes E-PTA positive. Between 15 and 17 embryonic days focal aggregations of osmiophilic and E-PTA stained material appear along the membranes of the protrusions and there is some E-PTA staining of the postsynaptic densities and intervening cleft material. Between 17 and 21 embryonic days mature ribbon synapses are observed on the surfaces of the conical-shaped, receptor pedicles where the ribbons and their synaptic vesicles are associated with the dense aggregations (arciform densities), seen earlier as isolated focal aggregations, and the receptor undercoating is restricted to non-synaptic regions. E-PTA staining shows that ribbons are positively stained around their borders only and that they are contiguous with the intensely stained arciform densities. The cleft material and postsynaptic densities of some synapses first stain as V-shaped junctions and later as Y-shaped junctions. These observations suggest that ribbon synaptic junction formation begins with an alignment of pre- and postsynaptic membranes and the presence of the receptor presynaptic membrane undercoating, followed by the appearance of the presynaptic arciform densities and some staining of the cleft material and postsynaptic densities. These events are followed by the appearance of synaptic ribbons which are associated with the presynaptic arciform densities and by a further differentiation of the cleft material and postsynaptic densities.

Animals↗
PubMed1975

Immunocytochemical localization of glutamate decarboxylase in rat spinal cord.

The GABA synthesizing enzyme, glutamate decarboxylase (GAD), has been localized by light and electron microscopy in the rat lumbosacral spinal cord using a peroxidase-labeling antibody technique. The light microscopic localization shows heavy, punctate reaction product for GAD in the dorsal horn laminae I-III. Moderately heavy reaction product is also seen in the deeper dorsal horn laminae IV-VI, the medial aspect of the intermediate gray (lamina VII) and the region around the central canal (lamina X). A moderately light concentration of GAD reaction product is observed in the ventral horn, and punctate deposits of reaction product also are seen on motoneuron cell bodies. The punctate distribution of reaction product for GAD in both ventral and dorsal horns, as visualized by light microscopy, corresponds to GAD-containing synaptic terminals seen by electron microscopy in comparable regions of the spinal gray. Many more GAD-positive terminals are observed in dorsal horn laminae I-III than in deeper laminae IV-VI. GAD-containing terminals in the dorsal horn are presynpatic to dendrites and cell bodies. Gad-containing terminals presynaptic to other axon terminals are observed also, and they are more numerous in laminae II and III. In the ventral horn motor nuclei, GAD-positive knobs are presynaptic to large and small dendrites and motoneuror cell bodies. In addition, small GAD-containing terminals also are presynaptic to larger axonal terminals which are in turn presynaptic to motoneuron somata. The observation of GAD-containing terminals presynaptic to dendrites and cell bodies in both dorsal and ventral horns is compatible with the evidence suggesting that GABA terminals may mediate postsynaptic inhibition of spinal interneurons and motoneurons. The additional finding of GAD-positive terminals presynaptic to other axonal terminals in the dorsal horn and motor nuclei is consistent with the growing evidence that GABA also may be the transmises mediating presynaptic inhibition via axo-axond synapses in the spinal cord.

Animals↗
PubMed1975

The fine structural localization of glutamate decarboxylase in developing axonal processes and presynaptic terminals of rodent cerebellum.

The immunocytochemical localization of L-glutamate decarboxylase (GAD), the enzyme which which forms gamma-aminobutyric acid (GABA), has been studied in developing rodent cerebellum. During the first 3-4 postnatal days, GAD is distributed along non-terminal portions of axonal processes in close association with small vesicles. Some of the axonal processes emanate from profiles which resemble growth cone varicosities, and are presumed to be foliopodia which extend distally from axonal growth regions. At the end of the first postnatal week the GAD-containing axonal processes are seen to form protosynaptic contacts, and GAD is localized around synaptic vesicles and at presynaptic junctional membranes. During the second and third postnatal weeks GAD gradually becomes localized to mature synaptic terminals in association with synaptic vesicle, mitochondrial, and presynaptic junctional membranes. The results suggest that GAD is present in growing neurites in close association with small vesicles prior to the time the neurites make protosynaptic contacts, and that differentiation of these contacts results in a sequestering of GAD into synaptic terminals.

Age Factors↗
PubMed1974

The visualization of concanavalin A binding sites in Purkinje cell somata and dendrites of rat cerebellum.

The localization of concanavalin A (Con A) binding sites in Purkinje cell somata and dendrites has been studied using a peroxidase labeling technique. In the somata, the nuclear, Golgi, and endoplasmic reticulum (ER) membranes are rich in Con A binding sites. The hypolemmal cisternae, which are continuous with the ER from the soma and throughout the dendritic tree of Purkinje cells, are also rich in Con A binding sites. Other cisternae seen in these dendrites do not bind detectable amounts of Con A. The results suggest that a cisternal system, rich in carbohydrate, may be continuous from the nuclear envelope to distal dendritic segments of Purkinje cells. Such a system could play a role in the movement of materials from Purkinje somata to dendrites.

Animals↗