Ultracytochemical Localization of Thiamine Monophosphatase Activity in the Substantia Gelatinosa of the Rat Spinal Cord

Acid phosphatase activities in the transitional epithelium of canine urinary bladder.

“…With the method of Gomori using 9-glycerophosphate extra-lysosomal reacting patterns in addition to the lysosomal one have been reported only under somewhat unusual or pathological circumstances, such as hepatocellular carcinoma (4), virus-infected encephalitis (5), ascites hepatoma (15), kidney adenoma (17), axon terminals in the substantia gelatinosa of the mouse spinal cord (8) and the small intestine of the newborn rat (1) . At the biochemical level the acid phosphatase was proved merely in lysosomes and microsomes.…”

High voltage electron microscopical analysis of synaptic glomeruli in the rat substantia gelatinosa.

“…In 1979, Inomata and Ogawa (14) reported that intense thiamine monophosphatase (TMPase) activity is specifically localized on the plasma membrane of the synaptic glomeruli in the substantia gelatinosa of the spinal cord, at an especially dense sinusoid axon (DSA) terminal, where it is particularly concerned with the relay of thermal and noxious stimuli. TMPase activity was transported from the smalltype neuron in the dorsal root ganglion to the plasma membrane of the DSA terminal in the substantia gelatinosa passes through the dorsal root (14)(15)(16).…”

“…TMPase activity was transported from the smalltype neuron in the dorsal root ganglion to the plasma membrane of the DSA terminal in the substantia gelatinosa passes through the dorsal root (14)(15)(16).…”

Capsaicin-induced activation and chemical injury of nociceptive primary sensory neurons

“…The previously described non-lysosomal fluorideresistant acid phosphatase (FRAP) has the same localization pattern as TMPase. It is assumed that these are identical enzymes (Dodd et al, 1984;Inomata and Ogawa, 1979;Knyihár-Csillik et al, 1986) which present in 30-50% of spinal ganglion cells of rodents, in particular in small-to medium-sized neurons (Colmant, 1959;Silverman and Kruger, 1990). According to recent findings, TMPase is molecularly identical with the transmembrane isoform of prostatic acid phosphatase (PAP) (Taylor-Blake and Zylka, 2010;Zylka et al, 2008) which is regarded as a marker of non-peptidergic neurons.…”

“…TMP which is present in about 30-50% of the DRG neurons of rodents (in particular in small-diameter cells with unmyelinated axons), is known as a marker of small primary afferent neurons (Colmant, 1959;Inomata and Ogawa, 1979;Knyihár-Csillik et al, 1986). On the control side the enzyme activity was present in the substantia gelatinosa of the spinal dorsal horn.…”