Horseradish peroxidase: a tool for study of the neuroendocrine cell and other peptide-secreting cells

The versatility of horseradish peroxidase is its usefulness both as an antigenic marker and as a probe molecule. We have demonstrated in the neuroendocrine cell that an HRP-bound antibody offers a high order of resolution for determining in which cellular compartment an antigen is located and where it is not. When native peroxidase is applied as an intracellular probe, it labels organelles associated with endocytosis in retrograde axonal transport and with the lysosomal system in both retrograde and orthograde axonal transport. The investigation that remains is the application of lectin-bound HRP to determine the pathways of membrane flow at the time when the neuroendocrine cell is stimulated to synthesize, transport, and secrete its peptide. For example, we are interested to know (1) whether internalized axon terminal membrane tagged with wheat germ agglutinin-HRP is channeled to all Golgi saccules engaged in the production of secretory granules in salt stimulated supraoptic neurons; and (2) if internalized cell membrane of the supraoptic cell body is tagged with wheat germ agglutinin-HRP and channeled to GERL, will this membrane be transferred from GERL to secretory granules, lysosomes in the cell body and axon, the axonal endoplasmic reticulum, and to autophagic/crinophagic vacuoles in axon terminals of salt-stressed supraoptic neurons? These additional studies should provide a more comprehensive, morphological picture of membrane flow in a neuroendocrine cell that is responding to the metabolic demands placed upon it.