ABSTRACT
The localization of the calcium-binding proteins (CaBPs) calbindin-D28K (CB) and parvalbumin (PV) in avian rapidly-adapting Herbst and Grandry sensory corpuscles was studied with the use of immunocytochemistry and monoclonal antibodies. Strongest immunostaining was detected in cells of the capsule in both receptor types. Staining was more pronounced in the vicinity of endoplasmic reticulum and mitochondria in the perinuclear regions, whereas staining was distinct in pinocytotic vesicles in peripheral cytoplasmic lamellae. Fibroblasts and macrophages in the subcapsular space of Herbst receptors also showed strong immunostaining in organelles in perinuclear regions. Modified Schwann cells in both receptor types revealed moderately-expressed immunostaining, which was more pronounced in perinuclear regions. The various parts of the receptor nerve fibers showed weak to strong staining. The physiological roles of the investigated CaBPs may be associated with cytoplasmic calcium ion (Ca++) storage, which is necessary for either active metabolism in the immunostained structures and/or their transfer to sensory axonal regions where Ca++ channels are present.
