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LETTERS TO THE EDITORTurk J Hematol 2018;35:75-93Reply to the Authors:To the Editor,We thank Joob and Wiwanitkit [1] for their helpful comments regarding the cause of leukoagglutination in our case [2]. Althoughthe underlying mechanism of in vitro leukoagglutination has not been fully clarified, leukoagglutination can be classified into twogroups: (1) EDTA-dependent leukoagglutination, and (2) EDTA-independent cold-induced leukoagglutination [3,4]. As pointed outby Joob and Wiwanitkit [1], both EDTA and cold agglutinin (CA) may have been implicated in our case, although high-titer CA wasdetected, and numerous erythrocyte agglutinations were observed in the peripheral blood smear.Screening for CA has shown that low-titer CAs may be found in the serum of healthy adults [5]; this may suggest the possibilitythat naturally occurring CA is somewhat involved in EDTA-dependent leukoagglutination in healthy subjects. Nonetheless, whenleukoagglutination occurs in an EDTA-anticoagulated blood sample, additional examination of the sample using other anticoagulantscould be recommended to confirm the relationship between leukoagglutination and EDTA.References1. Joob B, Wiwanitkit V. Leukoagglutination, Mycoplasma pneumoniae pneumonia and EDTA blood. Turk J Hematol 2018;35:75.Best RegardsYasushi Kubota, Shinya Kimura2. Kubota Y, Hirakawa Y, Wakayama K, Kimura S. Peculiar cold-induced leukoagglutination in Mycoplasma pneumoniae pneumonia. Turk J Hematol 2017;34:354-355.3. Goyal P, Agrawal D, Kailash J, Singh S. Cold-induced pseudoneutropenia in human immunodeficiency virus infection: first case report and review of relatedarticles. Indian J Hematol Blood Transfus 2014;30(Suppl 1):148-150.4. Lee JH. Neutrophil aggregation on the peripheral blood smear in a patient with cold agglutinin disease. Ann Hematol 2017:96:885-886.5. Dacie J. Auto-immune haemolytic anaemia (AIHA): cold-antibody syndromes II: immunochemistry and specificity of the antibodies; serum complement in autoimmunehaemolytic anaemia. In: Dacie J (ed). The Haemolytic Anaemias. Vol. 3. London, Churchill Livingstone, 1992.76
Turk J Hematol 2018;35:75-93LETTERS TO THE EDITORCyclic Guanosine Monophosphate-Dependent Protein Kinase IStimulators and Activators Are Therapeutic Alternatives for SickleCell DiseaseSiklik Guanozin Monofosfat Bağımlı Protein Kinaz I Uyarıcıları ve Aktivatörleri Orak HücreliAnemide Tedavi AlternatifleridirMohankrishna Ghanta 1 , Elango Panchanathan 1 , Bhaskar VKS Lakkakula 21Sri Ramachandra Medical College and Research Institute-DU, Faculty of Medicine, Department of Pharmacology, Chennai, Tamil Nadu, India2Sickle Cell Institute Chhattisgarh, Department of Molecular Genetics, Division of Research, Raipur, Chhattisgarh, IndiaTo the Editor,Sickle cell anemia (SCA) can lead to a host of complications,including hemolysis, vaso-occlusive episodes (painful crises),pulmonary hypertension, acute chest syndrome, and multiorgandamage. SCA has no widely available cure. Furthermore, theavailable treatments have unfavorable side effects, suchas myelosuppression of blood cells from continuous use ofhydroxyurea, iron overload from repeated blood transfusions,or immunosuppressive treatments required to sustain a bonemarrow transplant. In patients with SCA, hemoglobin-induceddamage of endothelial cells can lead to endothelial dysfunctiondue to the deficiency of nitric oxide (NO) [1]. NO is continuouslysynthesized by the endothelium to maintain vascular tone.The NO-soluble guanylate cyclase (sGC)-cyclic guanosinemonophosphate (cGMP) signaling (NO-sGC-cGMaP) pathway isone of the three important signaling pathways that are regulatedby NO in maintaining the vascular tone. NO stimulates sGC inthe vascular smooth muscle cells to induce formation of cGMP.This produced cGMP causes stimulation of cGMP-dependentprotein kinases (cGKs), which in turn stimulate voltagedependention channels. The cGKs are serene and threoninekinases, substrates for cGMP to elicit physiological functions.cGKs inhibit calcium release from the endoplasmic reticulumthrough the inositol 1,4,5-trisphosphate receptor-associatedcGMP kinase substrate (IRAG) and alternatively activate myosinlight-chainphosphatase by inhibiting the MLC kinases, withboth mechanisms resulting in smooth muscle relaxation [2].Two types of cGKs have been revealed to date. Mammalian cGKsexist as two isoforms, cGKI and cGKII, which are coded by theprkg1 and prkg2 genes, respectively. In humans two isoforms ofcGKI have been described, cGKI-α and cGKI-β, differing only intheir N-terminal parts and generated by alternative splicing of asingle gene. Northern blot analysis revealed that human cGKI-αmRNA was present in the aorta, heart, kidneys, and adrenalglands. In contrast, human cGKI-β mRNA was present only inthe uterus.In SCA, vascular tone control is compromised due tovasculopathy associated with hemolysis. As NO is consideredbeneficial, hydroxyurea and inhalational NO were administeredto increase the bioavailability of NO, which raises cGMP levels[3]. Phosphodiesterases (PDEs) are enzymes that catalyzecGMP to GMP. Inhibitors of PDEs also increase cGMP levelsby decreasing the degradation of cGMP. Inhibition of PDE9Aenzyme with the specific inhibitor BAY73-6691 reversed theincreased adhesive properties of neutrophils in sickle cell diseaseand increased production of the γ-globin gene (HBG) in K562cells. Furthermore, sGC activators were suggested for treatmentof sickle cell disease (Figure 1) [4].Figure 1. Schema of the nitric oxide-soluble guanylate cyclasecyclicguanosine monophosphate-protein kinases I signalingpathway in the treatment of sickle cell anemia vasculopathies.NO: Nitric oxide, sGC: soluble guanylate cyclase, cGMP: cyclic guanosinemonophosphate, cGKI: protein kinases.77
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