Two molecular forms of the isolated brain enzyme 2′,3′‐cyclic nucleotide 3′‐phosphodiesterase

Müller, Hans; Clapshaw, Patric A.; Seifert, W.

doi:10.1016/0014-5793(81)80882-4

Cited by 15 publications

(4 citation statements)

References 27 publications

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“…Most CNPase expression studies have focused on its roles in myelinogenesis and myelin‐producing glial cells. However, recent studies have shown the existence of CNPase in non‐myelinating cells, such as neuroblastoma and adrenal cells (McFerran & Burgoyne, 1997; Müller et al, 1981). Moreover, some studies detected a remarkable level of CNPase expression and CNPase‐like enzyme activity in membranes of cells in the bone marrow, skeletal muscles, heart, spleen, liver, and kidney (Brdiczka et al, 1998; Cao et al, 2007; Halestrap & Brenner, 2003).…”

Section: Discussionmentioning

confidence: 99%

Identification of some calcium binding proteins and neural cell markers in rat testis and epididymis during postnatal development

et al. 2022

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Calcium‐binding proteins (CaBPs) have an essential role in male reproduction by modulating calcium ion metabolism. Although the brain and testis are structurally and functionally different, they show a high degree of transcriptomic and proteomic similarities. The purpose of the present study was to explore some CaBPs (Iba‐1, Calbindin, Calretinin and Parvalbumin) and neural cell markers (CNPase, NG2 and Drebrin) expression in rat testis and epididymis during postnatal periods by using immunohistochemistry. Iba‐1, calbindin, calretinin, parvalbumin, CNPase, NG2 and drebrin were expressed in the epididymal epithelium in each postnatal period. Iba‐1 and calbindin expression showed stage‐dependent expression in spermatids. CaBPs and neural cell markers showed a positive reaction in Leydig cells in the postpubertal and mature periods. Sertoli cells, gonocytes, spermatogonium, and peritubular myoid cells showed heterogeneity in the expression of CaBPs and nerve markers throughout postnatal development. Interestingly, CNPase, NG2 and drebrin were positive in spermatocytes, spermatids, and sperm. Expression dynamics of calcium‐binding proteins and nerve markers showed differences in germ cells and somatic cells during postnatal development. The expression of these proteins in the testis and epididymis supports that they may have important roles in reproductive physiology.

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Section: Discussionmentioning

confidence: 99%

Identification of some calcium binding proteins and neural cell markers in rat testis and epididymis during postnatal development

et al. 2022

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“…2′,3′-cyclic nucleotide 3′-phosphodiesterase (CNPase) is a protein that hydrolyzes cyclic nucleotides to monophosphates (2′ nucleotides). CNPase has two isoforms, CNPase1 (46 kDa) and CNPase2 (48 kDa) [ 1 ], which are encoded separately by different promoters of the same gene [ 2 , 3 ] and have different structural properties and subcellular localizations [ 4 , 5 ]. The majority of studies involving CNPase expression have focused on its roles in myelin-producing glial cells (oligodendrocytes and Schwann cells) and myelinogenesis.…”

Section: Introductionmentioning

confidence: 99%

“…The majority of studies involving CNPase expression have focused on its roles in myelin-producing glial cells (oligodendrocytes and Schwann cells) and myelinogenesis. However, growing evidence has revealed the existence of this enzyme in non-myelinating cells, such as adrenal cells [ 6 ] and neuroblastoma cells (B104) [ 1 ]. Indeed, a considerable level of CNPase expression and CNPase-like enzyme activity were found in membranes of cells in the spleen, liver, kidney, heart, and skeletal muscles [ 7 , 8 ].…”

Section: Introductionmentioning

confidence: 99%

Expression of 2′,3′-cyclic nucleotide 3′-phosphodiesterase (CNPase) and its roles in activated microglia in vivo and in vitro

Yang

Kan

et al. 2014

J Neuroinflammation

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Background: We reported previously that amoeboid microglial cells in the postnatal rat brain expressed 2′,3′-cyclic nucleotide 3′-phosphodiesterase (CNPase) both in vivo and in vitro; however, the functional role of CNPase in microglia has remained uncertain. This study extended the investigation to determine CNPase expression in activated microglia derived from cell culture and animal models of brain injury with the objective to clarify its putative functions. Methods: Three-day-old Wistar rats were given an intraperitoneal injection of lipopolysaccharide to induce microglial activation, and the rats were killed at different time points. Along with this, primary cultured microglial cells were subjected to lipopolysaccharide treatment, and expression of CNPase was analyzed by real-time reverse transcription PCR and immunofluorescence. Additionally, siRNA transfection was employed to downregulate CNPase in BV-2 cells. Following this, inducible nitric oxide synthase, IL-1β and TNF-α were determined at mRNA and protein levels. Reactive oxygen species and nitric oxide were also assessed by flow cytometry and colorimetric assay, respectively. In parallel to this, CNPase expression in activated microglia was also investigated in adult rats subjected to fluid percussion injury as well as middle cerebral artery occlusion.

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“…Although CNPase is capable of hydrolysing 2',3'-cyclic nucleotides to their 2'-derivatives in vitro, the in vivo substrate and biological function of the enzyme remain unknown. CNPase has an apparent molecular mass of approximately 100 kDa under non-denaturing conditions (Drummond et al 1978 ;Sprinkle et al 1980;Muller et al 1981). However, two CNPase polypeptides can be resolved on sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) with a size range (44-54 kDa) and relative proportion that varies from species to species (Vogel & Thompson 1988;Sprinkle 1989).…”

Section: Introductionmentioning

confidence: 99%

Structure and chromosomal localization of the human 2‘,3’‐cyclic nucleotide 3‘‐phosphodiesterase gene

Douglas

Fox

Abbott

et al. 1992

Annals of Human Genetics

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Human brain cDNA clones for the myelin associated enzyme 2',3'-cyclic nucleotide 3'-phosphodiesterase (CNPase) have been isolated and sequenced. The only 5' untranslated region (UTR) sequence found was that of a human CNPII mRNA, with no direct evidence for a CNPI mRNA. Human CNPase cDNAs were used to isolate genomic clones containing the human CNPase gene which is 9 kb long. Four exons were identified, separated by three introns, and the sequence of each exon and intron/exon boundary has been established. The polymerase chain reaction (PCR) was used to detect the presence of the human CNPase gene in DNA from a panel of rodent/human somatic cell hybrids. By this means the human CNPase gene was mapped to chromosome 17. In situ hybridization of a human CNPase genomic clone to metaphase chromosomes further localized this gene to chromosomal band 17q21.

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Two molecular forms of the isolated brain enzyme 2′,3′‐cyclic nucleotide 3′‐phosphodiesterase

Cited by 15 publications

References 27 publications

Identification of some calcium binding proteins and neural cell markers in rat testis and epididymis during postnatal development

Identification of some calcium binding proteins and neural cell markers in rat testis and epididymis during postnatal development

Expression of 2′,3′-cyclic nucleotide 3′-phosphodiesterase (CNPase) and its roles in activated microglia in vivo and in vitro

Structure and chromosomal localization of the human 2‘,3’‐cyclic nucleotide 3‘‐phosphodiesterase gene

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