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Cyclic nucleotide phosphodiesterase enzyme - an overview

Prologue

1.3. Cyclic nucleotide phosphodiesterase enzyme - an overview

most diverse region of the phosphodiesterase enzyme structure, based on which the superfamily can also be classified in different groups, as shown in figure 1.4.

Figure 1.4 Structure based classification of PDEs based on regulatory domain

Phosphodiesterase members also differ in terms of substrate specificity and subcellular localization. These differences can be exploited for development of specific inhibitors (Russell et al., 1973). Table 1.1 provides complete details of various members of PDE superfamily. The table talks about various subtypes of PDE superfamily, their reported Km values for cGMP/cAMP, sites of expression, available inhibitors and the cellular activities influenced by inhibition of PDE.

Based on the substrate specificity, phosphodiesterases are divided into three groups (1) cAMP specific - PDE 4, 7 and 8 (2) cGMP specific - PDE 5, 6 and 9 and (3) dual specific (both cAMP and cGMP specific)- PDE 1, 2, 3, 10 and 11 (Conti and Beavo, 2007; Mehats et al., 2002). These specificity are determined by the catalytic domain but mechanism of specific recognition of substrate by phosphodiesterases is still a question [Ke et al., 2011;

Hou et al., 2011] (Hou et al., 2011; Ke et al., 2011). According to Zhang et al (2004),

“Glutamine switch mechanism” might be an important reason behind such selectivity. This is because γ-amino group of conserved invariant glutamine in the active site of PDEs can alternatively adopt two different orientations. In one orientation the hydrogen bond network supports guanine binding, resulting in cGMP selectivity, and in the second orientation the network supports adenine binding, leading to selectivity towards cAMP. Whereas in case of dual-specificity, the side chain of glutamine can switch over between the two orientations, resulting in specificity towards both the cyclic nucleotides (Jeon et al., 2005; Zhang et al., 2004). Binding patterns of invariant glutamine of different phosphodiesterases have been represented in figure 1.5.

Figure 1.5 Comparative binding patterns of invariant glutamine: (A) interaction of AMP with cAMP specific PDE4D by making two H-bonds between adenine moiety of AMP and invarient Q369; (B) interaction of GMP with cGMP specific PDE5A by two H-bonds between guanine base of GMP and invariant Q817, this interaction is in the opposite orientation of glutamine side chain as shown in AMP-PDE4D interaction; (C) Interaction pattern of dual specific PDE10A with AMP; (D) Interaction pattern of dual specific PDE10A with GMP

Phosphodiesterase 9A (PDE9A) is one of the most prominent phosphodiesterases among all PDEs due to its highest expression in brain and has highest affinity for cGMP. But complexity in structure and side effects associated with other PDEs makes the development of specific inhibitors targeting PDE9A a challenging task.

Table 1.1 Overview of cyclic nucleotide phosphodiesterase superfamily

PDE Sub- types

Properties Km Value Tissue expression

Therapeutic target Inhibitors Cellular function associated with PDE inhibition

References

PDE1 3 Ca++/ calmoduline- stimulated

PDE1A=112.7⁄

5.0µM [cAMP⁄cGMP]

PDE1B=

24.3⁄2.7µM [cAMP⁄cGMP]

PDE1C=1.7⁄1.3 µM

[cAMP⁄cGMP]

Brain, lung, Heart, smooth muscle

Neurodegenerative diseases such as Neuronal ischemia, epilepsy, Parkinson’s

& Alzheimer's disease (AD)

Calimidazolium, Dioclein, Phenethiazines,

SCH51866, Vinpocetine, Zaprinast

Apoptosis,

phosphorylation of AMPA receptors, enhancement of pulmonary

vasodilation

(Bender, 2006;

Dunkern and

Hatzelmann, 2007;

Evgenov et al., 2006; Gonçalves et al., 2009; Jiang et al., 1996; Medina, 2011)

PDE2 1 cGMP

stimulated

PDE2=10/30µ M

[cAMP⁄cGMP]

Adrenal gland, heart, lung, liver, platelets

Acute respiratory Distress Syndrome (ARDS), sepsis

EHNA, Bay 60-7550, MPB–forskolin, PDP

Endothelial cell permeability,

presynaptic inhibition

(Boess et al., 2004;

Hu et al., 2012;

Michie et al., 1996;

Surapisitchat et al., 2007; Witzenrath et al., 2009; Wunder et al., 2009)

PDE3 2 cGMP-

inhibited, cAMP- selective

PDE3=0.2/0.1µ M

[cAMP⁄cGMP]

Adipose tissue, heart, lung, liver, inflammatory cells, platelets

Asthma , chronic heart disease, cardiovascular disease, intermittent caudation, vascular smooth muscle relaxation

Amrinone, Bucladesine, Cilostazol, Cilostamide Enoximone, , Milrinone, Org 9935, Olprinone, SK&F 95654, Siguazodan, Saterinone

Induction of insulin secretion

(Ahmad et al., 2000;

Kieback and

Baumann, 2006;

Surapisitchat et al., 2007)

PDE4 4 cGMP-

insensitive, cAMP- specific

2–4 µM for cAMP

Sertoli cells, kidney, brain,liver, lung, inflammatory cells

Autoimmune disease, inflammatory disease,

neurodegenarative disease, cancer, allergic disorder.

Apremilast, NCS 613, Rolipram, Roflumilast

Long-term potentiation

(Mackenzie and Houslay, 2000;

Rabe, 2011; Schett et al., 2010;

Yougbare et al., 2011)

cGMP (catalytic domain PDE5A)

smooth muscle, hypertension, renal failure, sexual dysfunction, stroke

Wang et al., 2006;

Westermann et al., 2012; Zoraghi et al., 2007)

PDE6 3 Transducin- activated, cGMP specific

2.5 µM for cGMP

Photoreceptors, pineal gland

Sometime adverse effect on vision

Dipyridamole, Sildenafil, Vardenafil, Zaprinast

N/A (Cahill et al., 2012;

Lugnier, 2006)

PDE7 2 cAMP

specific, Rolipram- insensitive

0.03-0.2 µM for cAMP

Lung, hematopoietic cells, placenta, pancreas, brain, heart, thyroid, skeletal muscle, immune cells

Immune and inflammatory disorders,

neurological disease such as spinal cord injury

ASB16165, BAY 73-6691, PF-04447943, S14, VP1.15

Lessen inflammatory response, regulation of pro-inflammatory and immune T-cell functions, reduction in tissue injury, reduction in TNF-α, IL-6, COX-2 and iNOS expression

(Bender, 2006;

Castaño et al., 2009;

Paterniti et al., 2011)

PDE8 2 cAMP

specific, Rolipram- insensitive IBMX- insensitive

0.04–0.15 µM for cAMP

Testes, eye, liver, skeletal muscle, heart, kidney, ovary, brain, T lymphocytes

Polycystic ovary syndrome (PCOS)

Dipyridamole Suppression of Teff cell functions, lipid accumulation

(Lugnier, 2006;

Shimizu-Albergine et al., 2008; Vang et al., 2010)

PDE9 1 cGMP

specific, IBMX- insensitive

0.070-0.25 µM for cGMP 230 µM for cAMP

Brain, kidney, spleen, small intestine.

cardiovascular diseases, Insulin- resistance syndrome and diabetes, obesity,

neurodegenerative disorders

BAY73-6691, PF- 04447943

Synaptic plasticity, LTP(long term potentiation)

(Fisher et al., 1998;

Huai et al., 2004;

Soderling et al., 1998; Wang et al., 2010)

PDE10 1 Dual specific 0.05–0.26 µM for cAMP 3–7.2 µM for cGMP

Testes, striatum (brain)

Anxiety, cognition deficiency disorder, neurodegenerative disease

MP10 Long-term

potentiation

(Abdel-Magid, 2013)

PDE11 1 Dual specific 0.52 µM for cAMP

Skeletal muscle,

Asthma, adrenal, testicular, bipolar

Tadalafil Spermatogenesis (Makhlouf et al., 2006)