Analysis of parvalbumin and calbindin D28k-immunoreactive neurons in dorsal root ganglia of rat in relation to their cytochrome oxidase and carbonic anhydrase content.

Abstract:

:Histochemical and immunohistochemical techniques were used to determine relationships between the parvalbumin or calbindin D28k content and the cytochrome oxidase or carbonic anhydrase activity of neurons in lumbar dorsal root ganglia in rat. Subpopulations of dorsal root ganglion neurons that displayed parvalbumin- or calbindin D28k-immunoreactivity were classified as containing either light, moderate or dense histochemical reaction product for cytochrome oxidase and either a positive or negative reaction for carbonic anhydrase. It was found that approximately 90% of all parvalbumin and calbindin D28k-immunoreactive cells exhibited dense staining for cytochrome oxidase and that 87% of parvalbumin- and 76% of calbindin D28k-immunoreactive cells were positive for carbonic anhydrase. Conversely, 85% of all cells with a dense cytochrome oxidase reaction contained parvalbumin and calbindin D28k. Although not quantified, it appeared that many, but not all, carbonic anhydrase-positive cells contained parvalbumin or calbindin D28k. These results indicate the existence of a subpopulation of primary sensory neurons that contains parvalbumin and calbindin D28k and that expresses high levels of cytochrome oxidase and carbonic anhydrase activity. It is suggested that primary afferent neurons with this cytochemical profile transmit a sensory modality that requires them to discharge rapidly and/or frequently. The existence of a subpopulation of carbonic anhydrase-positive cells that lack immunoreactivity for parvalbumin or calbindin D28k suggests that the role of carbonic anhydrase in some sensory neurons is unrelated to functions requiring these calcium binding proteins.

journal_name

Neuroscience

journal_title

Neuroscience

authors

Carr PA,Yamamoto T,Karmy G,Baimbridge KG,Nagy JI

doi

10.1016/0306-4522(89)90216-9

subject

Has Abstract

pub_date

1989-01-01 00:00:00

pages

363-71

issue

2

eissn

0306-4522

issn

1873-7544

pii

0306-4522(89)90216-9

journal_volume

33

pub_type

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