2′,3′-Cyclic nucleotide 3′-phosphohydrolase in rat liver mitochondrial membranes

Dreiling, Charles E.; Schilling, Roger J.; Reitz, Ronald C.

doi:10.1016/0005-2736(81)90537-x

Cited by 26 publications

(13 citation statements)

References 25 publications

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“…Besides being a major protein in the central nervous system and highly expressed in oligodendrocytes and Schwann cells, CNP was also found outside myelin. Earlier, CNP activity was discovered in rat liver mitochondria (12) and later in mitochondria in cultured adrenal cells (27). Nevertheless, the CNP function in mitochondria has not yet been determined, and the influence of the CNP substrates on the mitochondrial function has not yet been investigated.…”

Section: Discussionmentioning

confidence: 99%

“…The paper reporting CNP activity in rat liver mitochondria appeared already 27 years ago, where the CNP activity was detected using 2Ј,3Ј-cNADP as substrate (12). However, so far, there are no data yet on the effect of CNP substrates on rat liver mitochondria functions.…”

Section: Effects Of 2ј3ј-camp On Mitochondrial Functions In Ratmentioning

confidence: 99%

“…CNP-like enzyme activity was found in nonmyelin membrane preparations derived from spleen, liver, thymus, adrenal glands, kidney, heart, and skeletal muscle. The levels of the enzymatic activity, however, are significantly lower than those in the central nervous system (12,15,40). CNP activity was revealed in rat liver mitochondria, specifically in the outer and inner mitochondrial membranes (12).…”

mentioning

confidence: 99%

“…The levels of the enzymatic activity, however, are significantly lower than those in the central nervous system (12,15,40). CNP activity was revealed in rat liver mitochondria, specifically in the outer and inner mitochondrial membranes (12). In cultured adrenal medullary chromaffin cells, which are not myelin associated, CNP was found to be located in mitochondria by means of immunofluorescence staining (27).…”

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confidence: 99%

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Ca²⁺-dependent permeability transition regulation in rat brain mitochondria by 2′,3′-cyclic nucleotides and 2′,3′-cyclic nucleotide 3′-phosphodiesterase

Azarashvili¹,

Krestinina²,

Galvita³

et al. 2009

American Journal of Physiology-Cell Physiology

109

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Azarashvili T, Krestinina O, Galvita A, Grachev D, Baburina Y, Stricker R, Evtodienko Y, Reiser G. Ca 2ϩ -dependent permeability transition regulation in rat brain mitochondria by 2Ј,3Ј-cyclic nucleotides and 2Ј,3Ј-cyclic nucleotide 3Ј-phosphodiesterase. Am J Physiol Cell Physiol 296: C1428 -C1439, 2009. First published April 8, 2009 doi:10.1152/ajpcell.00006.2009.-Recent evidence indicates that 2Ј,3Ј-cyclic nucleotide 3Ј-phosphodiesterase (CNP), a marker enzyme of myelin and oligodendrocytes, is also present in neural and nonneural mitochondria. However, its role in mitochondria is still completely unclear. We found CNP in rat brain mitochondria and studied the effects of CNP substrates, 2Ј,3Ј-cyclic nucleotides, on functional parameters of rat brain mitochondria. 2Ј,3Ј-cAMP and 2Ј,3Ј-cNADP stimulated Ca 2ϩ overload-induced Ca 2ϩ release from mitochondrial matrix. This Ca 2ϩ release under threshold Ca 2ϩ load correlated with membrane potential dissipation and mitochondrial swelling. The effects of 2Ј,3Ј-cyclic nucleotides were suppressed by cyclosporin A, a potent inhibitor of permeability transition (PT). PT development is a key stage in initiation of apoptotic mitochondriainduced cell death. 2Ј,3Ј-cAMP effects were observed on the functions of rat brain mitochondria only when PT was developed. This demonstrates involvement of 2Ј,3Ј-cAMP in PT regulation in rat brain mitochondria. We also discovered that, under PT development, the specific enzymatic activity of CNP was reduced. Thus we hypothesize that suppression of CNP activity under threshold Ca 2ϩ load leads to elevation of 2Ј,3Ј-cAMP levels that, in turn, promote PT development in rat brain mitochondria. Similar effects of 2Ј,3Ј-cyclic nucleotides were observed in rat liver mitochondria. Involvement of CNP in PT regulation was confirmed in experiments using mitochondria from CNP-knockdown oligodendrocytes (OLN93 cells). CNP reduction in these mitochondria correlated with lowering the threshold for Ca 2ϩ overload-induced Ca 2ϩ release. Thus our results reveal a new function for CNP and 2Ј,3Ј-cAMP in mitochondria, being a regulator/promotor of mitochondrial PT. oligodendrocyte mitochondria; 2Ј,3Ј-cyclic nucleotide 3Ј-phosphodiesterase; permeability transition; calcium transport THE ENZYME 2Ј,3Ј-CYCLIC NUCLEOTIDE 3Ј-phosphodiesterase (CNP, EC 3.1.4.37) accounts for ϳ2-5% of the total protein in the central nervous system myelin and 0.5-1% of peripheral nervous system myelin (36). CNP catalyzes the hydrolysis of 2Ј,3Ј-cyclic nucleotides to form the corresponding 2Ј-monophosphates (3). CNP was shown to be an integral protein of myelin of oligodendrocytes in the central nervous system and of peripheral myelin in Schwann cells (36,39). The majority of studies investigating the role of CNP were focused exclusively on the expression of CNP in oligodendrocytes and Schwann cells and the involvement of CNP in myelinogenesis. However, there is increasing evidence showing that this enzyme is present in a variety of other cell types. CNP-like enzyme activity was found ...

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Section: Discussionmentioning

confidence: 99%

Section: Effects Of 2ј3ј-camp On Mitochondrial Functions In Ratmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Ca²⁺-dependent permeability transition regulation in rat brain mitochondria by 2′,3′-cyclic nucleotides and 2′,3′-cyclic nucleotide 3′-phosphodiesterase

Azarashvili¹,

Krestinina²,

Galvita³

et al. 2009

American Journal of Physiology-Cell Physiology

109

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“…In addition to myelinating cells such as oligodendrocytes and Schwann cells, CNP is also expressed in various cell types such as chromaffin cell culNonspecific association of 2',3'-cyclic nucleotide 3'-phosphodiesterase with the rat forebrain postsynaptic density fraction tures (McFerran and Burgoyne, 1997), lymphocytes and retinal cells (Uyemura et al, 1972;Giulian and Moore, 1980;Weissbarth et al, 1981;Vogel and Thompson, 1988), liver cells (Dreiling et al, 1981), FRTL-5 thyroid cells (Laezza et al, 1997;Bifulco et al, 2002), and muscle cells (Weissbarth et al, 1981), indicating more general cellular functions. Recently, we found that CNP is expressed in Purkinje cells (PC's) and unidentified PSD95-positive cells but not in granule cells (GC's) in cerebellar cell cultures, indicating that both CNP is expressed in some subpopulations of cerebellar cells in addition to OL (Cho et al, 2003).…”

Section: Introductionmentioning

confidence: 99%

Nonspecific association of 2',3'-cyclic nucleotide 3'-phosphodiesterase with the rat forebrain postsynaptic density fraction

Cho

Jung²,

Shin³

et al. 2003

Exp Mol Med

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The 2',3'-cyclic nucleotide 3'-phosphodiesterase (CNP), a protein of unknow n function in vivo, is abundantly expressed in m yelinating glia in tw o isoform s, CNP1 and CNP2. In this study, im m unoblot analysis show ed that CNP1 is the m ajor isoform in adult forebrain, and that both isoform s are included in the postsynaptic density (PSD) fraction and tyrosine-phosphorylated at the basal level. H ow ever, subcellular distribution and detergent extraction data showed that CNP is nonspecifically associated w ith the PSD fraction. Im m unocytochem istry revealed that CNP is detected, in a weak but punctate pattern, in dissociated rat hippocam pal neurons of 3 days to 2 weeks in vitro. The CNP-positive punctae w ere distributed throughout som a and dendrites, and distinct from PSD95-positive ones. Im m unoblot analysis indicated that CNP is also expressed in neuronal stem cell lines, HiB5 and F11. Interestingly, in addition to the know n tw o isoform s, a new CNP isoform of M W 45 kDa was expressed in these cell lines and was the m ajor type of isoform in F11 cells. Taken together, our data suggest that CNP is expressed in the early stage of in vitro developm ent and nonspecifically included in the adult rat PSD fraction.

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Myelin

1984

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2′,3′-Cyclic nucleotide 3′-phosphohydrolase in rat liver mitochondrial membranes

Cited by 26 publications

References 25 publications

Ca²⁺-dependent permeability transition regulation in rat brain mitochondria by 2′,3′-cyclic nucleotides and 2′,3′-cyclic nucleotide 3′-phosphodiesterase

Ca²⁺-dependent permeability transition regulation in rat brain mitochondria by 2′,3′-cyclic nucleotides and 2′,3′-cyclic nucleotide 3′-phosphodiesterase

Nonspecific association of 2',3'-cyclic nucleotide 3'-phosphodiesterase with the rat forebrain postsynaptic density fraction

Myelin

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2′,3′-Cyclic nucleotide 3′-phosphohydrolase in rat liver mitochondrial membranes

Cited by 26 publications

References 25 publications

Ca2+-dependent permeability transition regulation in rat brain mitochondria by 2′,3′-cyclic nucleotides and 2′,3′-cyclic nucleotide 3′-phosphodiesterase

Ca2+-dependent permeability transition regulation in rat brain mitochondria by 2′,3′-cyclic nucleotides and 2′,3′-cyclic nucleotide 3′-phosphodiesterase

Nonspecific association of 2',3'-cyclic nucleotide 3'-phosphodiesterase with the rat forebrain postsynaptic density fraction

Myelin

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Ca²⁺-dependent permeability transition regulation in rat brain mitochondria by 2′,3′-cyclic nucleotides and 2′,3′-cyclic nucleotide 3′-phosphodiesterase

Ca²⁺-dependent permeability transition regulation in rat brain mitochondria by 2′,3′-cyclic nucleotides and 2′,3′-cyclic nucleotide 3′-phosphodiesterase