The cDNA of a human lymphocyte cyclic-AMP phosphodiesterase (PDE IV) reveals a multigene family

Obernolte, Rena; Bhakta, Sunil; Alvarez, Robert; Bach, Chinh; Zuppan, Patti; Mulkins, Mary A.; Jarnagin, Kurt; Shelton, Earl R.

doi:10.1016/0378-1119(93)90274-7

Cited by 77 publications

(28 citation statements)

References 23 publications

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“…terized [6,[11][12][13][14]. All of these isoforms show a high amino acid homology in the catalytic domain but less at the N-and C-terminal sequences.…”

Section: Discussionmentioning

confidence: 99%

“…Recently, four rat and four human cDNA isoforms of this subtype were identified [6,[11][12][13][14]. They are characterized by their selective 1ow-Km hydrolysis of cAMP and their sensitivity to rolipram and Ro20-1724 [1,4].…”

Section: Introductionmentioning

confidence: 99%

“…They are characterized by their selective 1ow-Km hydrolysis of cAMP and their sensitivity to rolipram and Ro20-1724 [1,4]. As for other PDE-types different splice variants have been described for most of the cloned PDE IV isoforms [6,7,11,13,14].…”

Section: Introductionmentioning

confidence: 99%

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Expression and regulation of human and rat phosphodiesterase type IV isogenes

1994

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Type IV phosphodiesterases (PDE IV) specifically hydrolyze cAMP and are inhibited by rolipram. RT-PCR was applied to analyze the expression patterns of mRNAs for four cloned human and rat phosphodiesterase type IV isogenes (PDE IV-A, -B, -C and -D). Although these patterns were mostly coincident for the human and rat PDE IV genes, some differences were found between the two species. PDE IV-A expression was detectable in human blood but not in rat blood, suggesting a species-specific difference in the expression of this PDE IV isogene. PDE IV-C was neither detected in human or rat blood nor in different cell populations of the human immune system. It is further demonstrated that the PDE IV isogene expression is differentially regulated by cAMP in different cell types.

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“…terized [6,[11][12][13][14]. All of these isoforms show a high amino acid homology in the catalytic domain but less at the N-and C-terminal sequences.…”

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Expression and regulation of human and rat phosphodiesterase type IV isogenes

1994

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“…Four PDE4 genes (PDE4A, PDE4B, PDE4C, PDE4D) are expressed in rat [16][17][18][19], mouse [20], and human [21][22][23][24][25], and their characterization has shown a close relationship between genes from two different species [14]. Furthermore, for three out of four rat and human genes, multiple mRNA variants and corresponding protein products have been detected [13,14].…”

Section: Introductionmentioning

confidence: 99%

Identification of cyclic AMP‐phosphodiesterase variants from the PDE4D gene expressed in human peripheral mononuclear cells

Némoz¹,

Zhang²,

Sette³

et al. 1996

FEBS Letters

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To determine whether the expression of different PDE4D variants is unique to the rat or conserved through evolution, we have characterized the different PDE4D mRNAs expressed in human peripheral blood mononuclear cells. RT-PCR was performed using primers based on rat sequences and mRNAs from mononuclear cells. The specifically amplified fragments had a size identical to that predicted for rat PDEAD1, PDE4D2 and PDE4D3. Sequencing confirmed that these fragments are derived from the human PDE4D gene. Their sequence was highly homologous to that reported for the rat variants, cDNAs corresponding to the entire ORF of human PDE4D2 and PDFAD3 were expressed in mammalian cells, causing a large increase in PDE activity. Western blot analysis of human peripheral blood mononuclear cell extracts demonstrated the presence of proteins corresponding to the recombinant PDE4D1 and PDE4D2. The pattern of splicing and different promoter usage of the PDE4D gene is therefore conserved during evolution, which indicates an important physiological role.

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“…[67][68][69][70][71][72][73][74][75] Rolipram, prototipik PDE4 inhibitörüdür, düşük afiniteli rolipram bağlanma sahası (LARBS) ve yüksek afiniteli bağlanma sitesi (HARBS) olarak adlandırı-lan iki siteye bağlanabilir.…”

Section: Genel Yapiunclassified

Phosphodiesterase Enzymes and Inhibitors: Review

Tuğrak¹,

Küçükoğlu²

2016

Turkiye Klinikleri J Pharm Sci

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Ö ÖZ ZE ET T Siklik nükleotid fosfodiesteraz enzimleri, vücutta her dokuda ve hücrede bulunabilen enzimlerdir. cAMP ve cGMP'yi hidroliz ettikleri için hücre sinyallerinde önemli rol oynarlar. PDE süper ailesi PDE1-PDE11 arasında olmak üzere 11 tanedir. Memeli hücrelerinde her bir aile 20'den fazla gen vermek için birdört farklı gen taşımaktadır. Bu genler 50'den fazla farklı PDE proteinini kodlarlar. PDE enzimleri içerisinde özellikle PDE1 ve PDE6 iyi karakterize edilmiş izozimlerdir. PDE'ler hücre ve dokularda spesifik dağılım gösteren enzimlerdir. Vücudun farklı doku ve organlarında bulunan PDE enzimleri farklılık gösterir. Bu sayede çeşitli hücre fonksiyonlarında farklı fizyolojik olaylara aracılık edebilirler. PDE izoenzimlerinin hücre ve doku fonksiyonlarına özel katkıları ve patofizyolojik düzenlenmeleri bugün önemli bir araştırma alanı oluşturmaktadır. Bu durum, etkileri henüz tam olarak belirlenmediği için özellikle PDE7-PDE11 gibi yeni PDE ailelerini daha çok ilgilendirmektedir. İnflamasyon, nörodejenerasyon ve kanser gibi birçok patolojik durumda meydana gelen değişiklikler, hücre içi sinyallerle ilgili PDE'lerin serbestleşmesini, bu patolojilerin önlenmesini, ayrıca bu tür patolojik durumların tedavisinde gözlemle-nen zorlukları açıklayabilir. Bu konularda yapılacak araştırmalar sonucu elde edilecek bulgular henüz kesin tedavisi bulunmayan hastalıkların tedavisinde yeni gelişmelere yol açabilir. Bu çalışmada, PDE enzimlerinin özellikleri, vücutta bulundukları doku ve organlar ile patofizyolojik olaylardaki rolleri açık-lanmış, ilaveten PDE inhibitörü ilaçlar anlatılmıştır. Ayrıca yeni geliştirilen ve ruhsatlandırma çalışmaları devam eden PDE inhibitörü bileşikler hakkında da bilgi verilmiştir.A An na ah ht ta ar r K Ke el li im me el le er r: : Fosfodiesteraz inhibitörleri; 2',3'-siklik AMP; 2',3'-siklik GMP A AB BS ST TR RA AC CT T Cyclic nucleotide phosphodiesterase enzymes can be found in every tissue and cell in the body. They play an important role in cell signaling because they hydrolyze cAMP and cGMP. PDE superfamily is 11 units, including PDE1-PDE11. Each family in mammalian cells encompasses 1 to 4 distinct genes, to give more than 20 genes. These genes encode more than 50 different PDE proteins. PDE enzymes in particular PDE1 and PDE6 are isozymes have been well characterized. PDEs are enzymes exhibiting specific distribution in cells and tissues. PDE enzymes located in different tissues and organs of the body vary. In this way, they can mediate different physiological events in various cell functions. Today, private contributions and pathophysiological regulations of PDE isoenzymes in cell and tissue functions constitute an important research field. This situation is more relevant for especially new PDE families such as PDE7-PDE11, because their effects have not been fully determined. Changes that occurs in many pathological situations such as inflammation, neurodegeneration and cancer, may explain the liberalization of PDEs related to the intracellular signaling as well as prevention of th...

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The cDNA of a human lymphocyte cyclic-AMP phosphodiesterase (PDE IV) reveals a multigene family

Cited by 77 publications

References 23 publications

Expression and regulation of human and rat phosphodiesterase type IV isogenes

Expression and regulation of human and rat phosphodiesterase type IV isogenes

Identification of cyclic AMP‐phosphodiesterase variants from the PDE4D gene expressed in human peripheral mononuclear cells

Phosphodiesterase Enzymes and Inhibitors: Review

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