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Expression and distribution of tartrate-resistant purple acid phosphatase in the rat nervous system.
- Source :
-
The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society [J Histochem Cytochem] 2001 Mar; Vol. 49 (3), pp. 379-96. - Publication Year :
- 2001
-
Abstract
- Tartrate-resistant purple acid phosphatase (TRAP) of osteoclasts and certain cells of the monocyte-macrophage lineage belongs to the family of purple acid phosphatases (PAPs). We provide here evidence for TRAP/PAP expression in the central and peripheral nervous systems in the rat. TRAP/PAP protein was partially purified and characterized from the trigeminal ganglion, brain, and spinal cord. The TRAP activity (U/mg tissue) in these tissues was about 10-20 times lower than in bone. Reducing agents, e.g. ascorbate and ferric iron, increased the TRAP activity from the neural tissues (nTRAP) and addition of oxidizing agents completely inactivated both bone and nTRAP. The IC(50) for three known oxyanion inhibitors of TRAP/PAP was similar for bone and nTRAP with the same rank order of potency (molybdate > tungstate > phosphate). This indicates that the redox-sensitive binuclear iron center characteristic of mammalian PAPs is present also in nTRAP. Western blots of partially purified nTRAP revealed a band with the expected size of 35 kD. The expression of TRAP in the trigeminal ganglion, brain, and spinal cord was confirmed at the mRNA level by RT-PCR. In situ hybridization histochemistry demonstrated TRAP mRNA expression in small ganglion cells of the trigeminal ganglion, in alpha-motor neurons of the ventral spinal cord, and in Purkinje cells of the cerebellum. TRAP-like immunoreactivity was encountered in the cytoplasm of neuronal cell bodies in specific areas of both the central and the peripheral nervous system. Together, the data demonstrate that active TRAP/PAP is expressed in certain parts of the rat nervous system.
- Subjects :
- Acid Phosphatase isolation & purification
Animals
Brain anatomy & histology
Glycoproteins isolation & purification
Immunoblotting
Immunohistochemistry
In Situ Hybridization
RNA, Messenger metabolism
Rats
Rats, Sprague-Dawley
Reverse Transcriptase Polymerase Chain Reaction
Acid Phosphatase metabolism
Brain enzymology
Glycoproteins metabolism
Spinal Cord enzymology
Trigeminal Ganglion enzymology
Subjects
Details
- Language :
- English
- ISSN :
- 0022-1554
- Volume :
- 49
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society
- Publication Type :
- Academic Journal
- Accession number :
- 11181741
- Full Text :
- https://doi.org/10.1177/002215540104900312