Glutamate decarboxylase activity in the rat posterior pituitary, pineal gland, dorsal root ganglion and superior cervical ganglion

1976 ◽  
Vol 27 (5) ◽  
pp. 1267-1269 ◽  
Author(s):  
I. Kanazawa ◽  
L. L. Iversen ◽  
J. S. Kelly
Keyword(s):  
Dorsal Root Ganglion ◽  
Pineal Gland ◽  
Superior Cervical Ganglion ◽  
Glutamate Decarboxylase ◽  
Dorsal Root ◽  
Decarboxylase Activity ◽  
Posterior Pituitary ◽  
Cervical Ganglion

scholarly journals Retrograde Tracing of Nerve Fibers to the Rat Middle Cerebral Artery with True Blue: Colocalization with Different Peptides

1989 ◽  
Vol 9 (2) ◽  
pp. 212-218 ◽  
Author(s):  
L. Edvinsson ◽  
H. Hara ◽  
R. Uddman
Keyword(s):  
Dorsal Root Ganglion ◽  
Middle Cerebral Artery ◽  
Nerve Cell ◽  
Trigeminal Ganglion ◽  
Cerebral Artery ◽  
Superior Cervical Ganglion ◽  
Dorsal Root ◽  
Nerve Fibers ◽  
Retrograde Tracing ◽  
Cervical Ganglion

The origin of nerve fibers to the rat middle cerebral artery was studied by retrograde tracing with the fluorescent tracer True Blue (TB) in combination with immunocytochemistry to known perivascular peptides. Application of TB to the middle cerebral artery labeled nerve cell bodies in the ipsilateral superior cervical ganglion, the otic ganglion, the sphenopalatine ganglion, the trigeminal ganglion, and the cervical dorsal root ganglion at level C2. A few labeled nerve cell bodies were seen in contralateral ganglia. Judging from the number and intensity of the labeling, the superior cervical ganglion and the trigeminal ganglion and dorsal root ganglion at level C2 contributed most to the innervation. A moderate number of nerve cell bodies were labeled in the sphenopalatine and otic ganglia. The TB-labeled nerve cell bodies were further examined for the presence of neuropeptides. For that purpose antibodies raised against neuropeptide Y (NPY), vasoactive intestinal polypeptide (VIP), substance P (SP) and calcitonin gene-related peptide (CGRP) were used. A considerable portion of the TB-labeled nerve cell bodies in the superior cervical ganglion contained NPY. About half of the labeled nerve cell bodies in the sphenopalatine and otic ganglia contained VIP. In the trigeminal ganglion and in the dorsal root ganglion at level C2, one-third of the TB-labeled nerve cell bodies were CGRP-immunoreactive, while only few nerve cell bodies contained SP. The study provides direct evidence for the origin of cerebrovascular peptidergic nerve fibers and demonstrates that not only ipsilateral but also contralateral ganglia contribute to the innervation of the cerebral circulation.

scholarly journals Expression of unique sets of GPI-linked proteins by different primary neurons in vitro.

1992 ◽  
Vol 117 (3) ◽  
pp. 617-627 ◽  
Author(s):  
C L Rosen ◽  
M P Lisanti ◽  
J L Salzer
Keyword(s):  
Membrane Proteins ◽  
Dorsal Root Ganglion ◽  
Relative Abundance ◽  
Superior Cervical Ganglion ◽  
Dorsal Root ◽  
Surface Proteins ◽  
Dorsal Root Ganglion Neurons ◽  
Primary Neurons ◽  
Cervical Ganglion ◽  
Ganglion Neurons

We have surveyed the proteins expressed at the surface of different primary neurons as a first step in elucidating how axons regulate their ensheathment by glial cells. We characterized the surface proteins of dorsal root ganglion neurons, superior cervical ganglion neurons, and cerebellar granule cells which are myelinated, ensheathed but unmyelinated, and unensheathed, respectively. We found that the most abundant proteins are common to all three types of neurons. Reproducible differences in the composition of the integral membrane proteins (enriched by partitioning into a Triton X-114 detergent phase) were detected. These differences were most striking when the expression of glycosylphosphatidyl-inositol (GPI)-anchored membrane proteins by these different neurons was compared. Variations in the relative abundance and degree of glycosylation of several well known GPI-anchored proteins, including Thy-1, F3/F11, and the 120-kD form of the neural cell adhesion molecule (N-CAM), and an abundant 60-kD GPI-linked protein were observed. In addition, we have identified several potentially novel GPI-anchored glycoproteins on each class of neurons. These include a protein that is present only on superior cervical ganglion neurons and is 90 kD; an abundant protein of 69 kD that is essentially restricted in its expression to dorsal root ganglion neurons; and proteins of 38 and 31 kD that are expressed only on granule cell neurons. Finally, the relative abundance of the three major isoforms of N-CAM was found to vary significantly between these different primary neurons. These results are the first demonstration that nerve fibers with diverse ensheathment fates differ significantly in the composition of their surface proteins and suggest an important role for GPI-anchored proteins in generating diversity of the neuronal cell surface.

scholarly journals Histochemical investigation of criteria for the distinction between monoamine oxidase A and B in various species.

1984 ◽  
Vol 32 (6) ◽  
pp. 667-673 ◽  
Author(s):  
E Uchida ◽  
G B Koelle
Keyword(s):  
Dorsal Root Ganglion ◽  
Monoamine Oxidase ◽  
Dorsal Root ◽  
Monoamine Oxidase A ◽  
Rat Tissues ◽  
Histochemical Investigation ◽  
Mao B ◽  
Total Inhibition ◽  
Mao A ◽  
Cervical Ganglion

The superior cervical ganglion (SCG), pineal body (PB), and liver (L) of the rat, rabbit and cat were stained for monoamine oxidase (MAO) A and B by the tetranitro blue tetrazolium (TNBT) and coupled peroxidase ( PerOx ) methods, using 5-hydroxytryptamine (5HT), tryptamine ( Tryp ), tyramine (Tyr), and benzylamine (Bz) as substrates, and clorgyline (Cl) and deprenyl (Dep), both at 10(-7) M, as selective inhibitors. The nodose ganglion (NG) and dorsal root ganglion (DRG) of the rabbit and cat were also studied. The results with rat tissues were consistent with published quantitative findings (SCG, MAO-A much greater than B; PB, MAO-A less than or equal to B; L, MAO-A = B). In the rabbit, the findings with the SCG were similar; the MAO activities of the PB were relatively resistant to both inhibitors; the MAO of the liver required 10(-4) M concentrations of both inhibitors to produce near total inhibition, suggesting that the liver contains an MAO distinct from MAO A and B. All cat tissues examined appeared to contain almost exclusively MAO-B. In this species 5HT, which is generally considered a selective substrate for MAO-A, was oxidized by MAO-B. The findings indicate that criteria for MAO-A, -B, and other subgroups must be defined for each species and tissue.

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