Neutropenia and Primary Immunodeficiency Diseases

REFERENCES

• Rezaei N., Bonilla F. A., Sullivan K. E., de Vries E., Orange J. S. An introduction to primary immunodeficiency diseases. Primary Immunodeficiency Diseases: Definition, Diagnosis and Management, N. Rezaei, A. Aghamohammadi, L. D. Notarangelo. Springer-Verlag, Berlin Heidelberg 2008; 1–38
   Google Scholar
• Geha R. S., Notarangelo L. D., Casanova J. L., Chapel H., Conley M. E., Fischer A., et al. Primary immunodeficiency diseases: An update from the International Union of Immunological Societies Primary Immunodeficiency Diseases Classification Committee. J Allergy Clin Immunol 2007; 120: 776–794
   PubMed Web of Science ®Google Scholar
• Aghamohammadi A., Moein M., Farhoudi A., Pourpak Z., Rezaei N., Abolmaali K., et al. Primary immunodeficiency in Iran: First report of the National Registry of PID in Children and Adults. J Clin Immunol 2002; 22: 375–380
   PubMed Web of Science ®Google Scholar
• Rezaei N., Moin M., Pourpak Z., Ramyar A., Izadyar M., Chavoshzadeh Z., et al. The clinical, immunohematological, and molecular study of Iranian patients with severe congenital neutropenia. J Clin Immunol 2007; 27: 525–533
   Google Scholar
• Arkwright P. D., Abinun M., Cant A. J. Autoimmunity in human primary immunodeficiency diseases. Blood 2002; 99: 2694–2702
   PubMed Web of Science ®Google Scholar
• Cunningham-Rundles C. Hematologic complications of primary immune deficiencies. Blood Rev 2002; 16: 61–64
   PubMed Web of Science ®Google Scholar
• Constantinou C. L. Differential diagnosis of neutropenia. Primary Hematology, A. Tefferi. Humana Press, Totowa, NJ 2001; 93–105
   Google Scholar
• Cham B., Bonilla M. A., Winkelstein J. Neutropenia associated with primary immunodeficiency syndromes. Semin Hematol 2002; 39: 107–112
   PubMed Web of Science ®Google Scholar
• Rezaei N., Farhoudi A., Pourpak Z., Aghamohammadi A., Moin M., Movahedi M., Gharagozlou M. Neutropenia in Iranian patients with primary immunodeficiency disorders. Haematologica 2005; 90: 554–556
   PubMedGoogle Scholar
• Bohn G., Welte K., Klein C. Severe congenital neutropenia: New genes explain an old disease. Curr Opin Rheumatol 2007; 19: 644–650
   PubMed Web of Science ®Google Scholar
• Schaffer A. A., Klein C. Genetic heterogeneity in severe congenital neutropenia: How many aberrant pathways can kill a neutrophil?. Curr Opin Allergy Clin Immunol 2007; 7: 481–494
   PubMedGoogle Scholar
• Boztug K., Welte K., Zeidler C., Klein C. Congenital neutropenia syndromes. Immunol Allergy Clin North Am 2008; 28: 259–275; vii–viii
   Google Scholar
• Welte K., Zeidler C., Dale D. C. Severe congenital neutropenia. Semin Hematol 2006; 43: 189–195
   PubMed Web of Science ®Google Scholar
• Skokowa J., Germeshausen M., Zeidler C., Welte K. Severe congenital neutropenia: Inheritance and pathophysiology. Curr Opin Hematol 2007; 14: 22–28
   PubMed Web of Science ®Google Scholar
• Wintergerst U., Rosenzweig S. D., Abinun M., Malech H. L., Holland S. M., Rezaei N. Phagocytes defects. Primary Immunodeficiency Diseases: Definition, Diagnosis and Management, N. Rezaei, A. Aghamohammadi, L. D. Notarangelo. Springer-Verlag, Berlin Heidelberg 2008; 1–38
   Google Scholar
• Dale D. C., Bolyard A. A., Schwinzer B. G., Pracht G., Bonilla M. A., Boxer L., et al. The Severe Chronic Neutropenia International Registry: 10-Year Follow-up Report. Support Cancer Ther 2006; 3: 220–231
   PubMedGoogle Scholar
• Rezaei N., Farhoudi A., Ramyar A., Pourpak Z., Aghamohammadi A., Mohammadpour B., et al. Congenital neutropenia and primary immunodeficiency disorders: A survey of 26 Iranian patients. J Pediatr Hematol Oncol 2005; 27: 351–356
   Google Scholar
• Fahimzad A., Chavoshzadeh Z., Abdollahpour H., Klein C., Rezaei N. Necrosis of nasal cartilage due to mucormycosis in a patient with severe congenital neutropenia due to HAX1 deficiency. J Investig Allergol Clin Immunol 2008; 18: 469–472
   PubMed Web of Science ®Google Scholar
• Germeshausen M., Grudzien M., Zeidler C., Abdollahpour H., Yetgin S., Rezaei N., et al. Novel HAX1 mutations in patients with severe congenital neutropenia reveal isoform-dependent genotype-phenotype associations. Blood 2008; 111: 4954–4957
   PubMed Web of Science ®Google Scholar
• Rezaei N., Chavoshzadeh Z., Sandrock R. A. O. I., Klein C. Association of HAX1 deficiency with neurological disorder. Neuropediatrics 2007; 38: 261–263
   PubMedGoogle Scholar
• Ishikawa N., Okada S., Miki M., Shirao K., Kihara H., Tsumura M., et al. Neurodevelopmental abnormalities associated with severe congenital neutropenia due to the R86X mutation in the HAX1 gene. J Med Genet 2008; 45: 802–807
   PubMed Web of Science ®Google Scholar
• Boztug K., Appaswamy G., Ashikov A., Schäffer A. A., Salzer U., Diestelhorst J., et al. A syndrome with congenital neutropenia and mutations in G6PC3. N Engl J Med 2009; 360: 32–43
   PubMed Web of Science ®Google Scholar
• Ward A. C., Dale D. C. Genetic and molecular diagnosis of severe congenital neutropenia. Curr Opin Hematol 2009; 16: 9–13
   PubMed Web of Science ®Google Scholar
• Dale D. C., Person R. E., Bolyard A. A., Aprikyan A. G., Bos C., Bonilla M. A., et al. Mutations in the gene encoding neutrophil elastase in congenital and cyclic neutropenia. Blood 2000; 96: 2317–2322
   PubMed Web of Science ®Google Scholar
• Xia J., Bolyard A. A., Rodger E., Stein S., Aprikyan A. A. G., Dale D. C., Link D. C. Incidence of SCN-associated gene mutations in severe congenital neutropenia patients in North America. 50th American Society of Hematology Annual Meeting. 2008
   Google Scholar
• Bellanne-Chantelot C., Clauin S., Leblanc T., Cassinat B., Rodrigues-Lima F., Beaufils S., et al. Mutations in the ELA2 gene correlate with more severe expression of neutropenia: A study of 81 patients from the French Neutropenia Register. Blood 2004; 103: 4119–4125
   PubMed Web of Science ®Google Scholar
• Takahashi H., Nukiwa T., Basset P., Crystal R. G. Myelomonocytic cell lineage expression of the neutrophil elastase gene. J Biol Chem 1988; 263: 2543–2547
   PubMed Web of Science ®Google Scholar
• Salipante S. J., Benson K. F., Luty J., Hadavi V., Kariminejad R., Kariminejad M. H., et al. Double de novo mutations of ELA2 in cyclic and severe congenital neutropenia. Hum Mutat 2007; 28: 874–881
   PubMedGoogle Scholar
• Kollner I., Sodeik B., Schreek S., Heyn H., von Neuhoff N., Germeshausen M., et al. Mutations in neutrophil elastase causing congenital neutropenia lead to cytoplasmic protein accumulation and induction of the unfolded protein response. Blood 2006; 108: 493–500
   PubMed Web of Science ®Google Scholar
• Grenda D. S., Murakami M., Ghatak J., Xia J., Boxer L. A., Dale D., et al. Mutations of the ELA2 gene found in patients with severe congenital neutropenia induce the unfolded protein response and cellular apoptosis. Blood 2007; 110: 4179–4187
   PubMed Web of Science ®Google Scholar
• Xia J., Link D. C. Severe congenital neutropenia and the unfolded protein response. Curr Opin Hematol 2008; 15: 1–7
   PubMedGoogle Scholar
• Benson K. F., Li F. Q., Person R. E., Albani D., Duan Z., Wechsler J., et al. Mutations associated with neutropenia in dogs and humans disrupt intracellular transport of neutrophil elastase. Nat Genet 2003; 35: 90–96
   PubMed Web of Science ®Google Scholar
• Horwitz M., Benson K. F., Duan Z., Li F. Q., Person R. E. Hereditary neutropenia: Dogs explain human neutrophil elastase mutations. Trends Mol Med 2004; 10: 163–170
   PubMed Web of Science ®Google Scholar
• Aprikyan A. A., Kutyavin T., Stein S., Aprikian P., Rodger E., Liles W. C., et al. Cellular and molecular abnormalities in severe congenital neutropenia predisposing to leukemia. Exp Hematol 2003; 31: 372–381
   Google Scholar
• Klein C., Grudzien M., Appaswamy G., Germeshausen M., Sandrock I., Schaffer A. A., et al. HAX1 deficiency causes autosomal recessive severe congenital neutropenia (Kostmann disease). Nat Genet 2007; 39: 86–92
   PubMed Web of Science ®Google Scholar
• Suzuki Y., Demoliere C., Kitamura D., Takeshita H., Deuschle U., Watanabe T. HAX-1, a novel intracellular protein, localized on mitochondria, directly associates with HS1, a substrate of Src family tyrosine kinases. J Immunol 1997; 158: 2736–2744
   PubMed Web of Science ®Google Scholar
• Gallagher A. R., Cedzich A., Gretz N., Somlo S., Witzgall R. The polycystic kidney disease protein PKD2 interacts with Hax-1, a protein associated with the actin cytoskeleton. Proc Natl Acad Sci U S A 2000; 97: 4017–4022
   PubMedGoogle Scholar
• Radhika V., Onesime D., Ha J. H., Dhanasekaran N. Galpha13 stimulates cell migration through cortactin-interacting protein Hax-1. J Biol Chem 2004; 279: 49406–49413
   PubMedGoogle Scholar
• Chao J. R., Parganas E., Boyd K., Hong C. Y., Opferman J. T., Ihle J. N. Hax1-mediated processing of HtrA2 by Parl allows survival of lymphocytes and neurons. Nature 2008; 452: 98–102
   PubMed Web of Science ®Google Scholar
• Devriendt K., Kim A. S., Mathijs G., Frints S. G., Schwartz M., Van Den Oord J. J., et al. Constitutively activating mutation in WASP causes X-linked severe congenital neutropenia. Nat Genet 2001; 27: 313–317
   PubMed Web of Science ®Google Scholar
• Burns S., Cory G. O., Vainchenker W., Thrasher A. J. Mechanisms of WASp-mediated hematologic and immunologic disease. Blood 2004; 104: 3454–3462
   PubMed Web of Science ®Google Scholar
• Ancliff P. J., Blundell M. P., Cory G. O., Calle Y., Worth A., Kempski H., et al. Two novel activating mutations in the Wiskott-Aldrich syndrome protein result in congenital neutropenia. Blood 2006; 108: 2182–2189
   PubMed Web of Science ®Google Scholar
• Moulding D. A., Blundell M. P., Spiller D. G., White M. R., Cory G. O., Calle Y., et al. Unregulated actin polymerization by WASp causes defects of mitosis and cytokinesis in X-linked neutropenia. J Exp Med 2007; 204: 2213–2224
   PubMed Web of Science ®Google Scholar
• Ochs H. D., Thrasher A. J. The Wiskott-Aldrich syndrome. J Allergy Clin Immunol 2006; 117: 725–738, quiz 739
   PubMed Web of Science ®Google Scholar
• Cohen P., Frame S. The renaissance of GSK3. Nat Rev Mol Cell Biol 2001; 2: 769–776
   PubMed Web of Science ®Google Scholar
• Person R. E., Li F. Q., Duan Z., Benson K. F., Wechsler J., Papadaki H. A., et al. Mutations in proto-oncogene GFI1 cause human neutropenia and target ELA2. Nat Genet 2003; 34: 308–312
   PubMed Web of Science ®Google Scholar
• Moroy T., Zeng H., Jin J., Schmid K. W., Carpinteiro A., Gulbins E. The zinc finger protein and transcriptional repressor Gfi1 as a regulator of the innate immune response. Immunobiology 2008; 213: 341–352
   PubMedGoogle Scholar
• Hock H., Hamblen M. J., Rooke H. M., Schindler J. W., Saleque S., Fujiwara Y., Orkin S. H. Gfi-1 restricts proliferation and preserves functional integrity of haematopoietic stem cells. Nature 2004; 431: 1002–1007
   PubMed Web of Science ®Google Scholar
• Rosenberg P. S., Alter B. P., Bolyard A. A., Bonilla M. A., Boxer L. A., Cham B., et al. The incidence of leukemia and mortality from sepsis in patients with severe congenital neutropenia receiving long-term G-CSF therapy. Blood 2006; 107: 4628–4635
   PubMed Web of Science ®Google Scholar
• Dong F., Brynes R. K., Tidow N., Welte K., Lowenberg B., Touw I. P. Mutations in the gene for the granulocyte colony-stimulating-factor receptor in patients with acute myeloid leukemia preceded by severe congenital neutropenia. N Engl J Med 1995; 333: 487–493
   PubMed Web of Science ®Google Scholar
• Germeshausen M., Ballmaier M., Welte K. Incidence of CSF3R mutations in severe congenital neutropenia and relevance for leukemogenesis: Results of a long-term survey. Blood 2007; 109: 93–99
   PubMed Web of Science ®Google Scholar
• Salipante S. J., Benson K. F., Person R. E. Neutropenia-associated mutations of PFAAP5, a novel protein mediating transcriptional repressor interaction between Gfi1 and neutrophil elastase. ASH Annual Meeting Abstracts: Blood. 2006, Abstract 501
   Google Scholar
• Duan Z., Huang S., Person R. E. Neutropenia-associated mutations in PRDM5, a novel epigenetic regulator of hematopoiesis. ASH Annual Meeting Abstracts: Blood. 2006, Abstract 503
   Google Scholar
• Berliner N., Horwitz M., Loughran T. P., Jr. Congenital and acquired neutropenia. Hematology Am Soc Hematol Educ Program 2004; 63–79
   PubMedGoogle Scholar
• Dale D. C., Hammond W. P. T. Cyclic neutropenia: a clinical review. Blood Rev 1988; 2: 178–185
   PubMed Web of Science ®Google Scholar
• Rezaei N., Farhoudi A., Pourpak Z., Aghamohammadi A., Ramyar A., Moin M., et al. Clinical and laboratory findings in Iranian children with cyclic neutropenia. Iran J Allergy Asthma Immunol 2004; 3: 37–40
   Google Scholar
• Sera Y., Kawaguchi H., Nakamura K., Sato T., Habara M., Okada S., et al. A comparison of the defective granulopoiesis in childhood cyclic neutropenia and in severe congenital neutropenia. Haematologica 2005; 90: 1032–1041
   Google Scholar
• Horwitz M. S., Duan Z., Korkmaz B., Lee H. H., Mealiffe M. E., Salipante S. J. Neutrophil elastase in cyclic and severe congenital neutropenia. Blood 2007; 109: 1817–1824
   PubMed Web of Science ®Google Scholar
• Horwitz M., Benson K. F., Person R. E., Aprikyan A. G., Dale D. C. Mutations in ELA2, encoding neutrophil elastase, define a 21-day biological clock in cyclic haematopoiesis. Nat Genet 1999; 23: 433–436
   PubMed Web of Science ®Google Scholar
• Smith O. P., Hann I. M., Chessells J. M., Reeves B. R., Milla P. Haematological abnormalities in Shwachman-Diamond syndrome. Br J Haematol 1996; 94: 279–284
   PubMed Web of Science ®Google Scholar
• Dror Y., Durie P., Ginzberg H., Herman R., Banerjee A., Champagne M., et al. Clonal evolution in marrows of patients with Shwachman-Diamond syndrome: A prospective 5-year follow-up study. Exp Hematol 2002; 30: 659–669
   PubMed Web of Science ®Google Scholar
• Ginzberg H., Shin J., Ellis L., Morrison J., Ip W., Dror Y., et al. Shwachman syndrome: Phenotypic manifestations of sibling sets and isolated cases in a large patient cohort are similar. J Pediatr 1999; 135: 81–88
   PubMed Web of Science ®Google Scholar
• Dror Y. Shwachman-Diamond syndrome. Pediatr Blood Cancer 2005; 45: 892–901
   PubMed Web of Science ®Google Scholar
• Smith O. P. Shwachman-Diamond syndrome. Semin Hematol 2002; 39: 95–102
   Google Scholar
• Shimamura A. Shwachman-Diamond syndrome. Semin Hematol 2006; 43: 178–188
   PubMed Web of Science ®Google Scholar
• Kent A., Murphy G. H., Milla P. Psychological characteristics of children with Shwachman syndrome. Arch Dis Child 1990; 65: 1349–1352
   PubMedGoogle Scholar
• Aggett P. J., Cavanagh N. P., Matthew D. J., Pincott J. R., Sutcliffe J., Harries J. T. Shwachman's syndrome. A review of 21 cases. Arch Dis Child 1980; 55: 331–347
   PubMed Web of Science ®Google Scholar
• Boocock G. R., Morrison J. A., Popovic M., Richards N., Ellis L., Durie P. R., Rommens J. M. Mutations in SBDS are associated with Shwachman-Diamond syndrome. Nat Genet 2003; 33: 97–101
   PubMed Web of Science ®Google Scholar
• Austin K. M., Gupta M. L., Coats S. A., Tulpule A., Mostoslavsky G., Balazs A. B., et al. Mitotic spindle destabilization and genomic instability in Shwachman-Diamond syndrome. J Clin Invest 2008; 118: 1511–1518
   PubMed Web of Science ®Google Scholar
• Ganapathi K. A., Shimamura A. Ribosomal dysfunction and inherited marrow failure. Br J Haematol 2008; 141: 376–387
   PubMed Web of Science ®Google Scholar
• Davis W. C., Douglas S. D. Defective granule formation and function in the Chediak-Higashi syndrome in man and animals. Semin Hematol 1972; 9: 431–450
   Google Scholar
• Abo T., Roder J. C., Abo W., Cooper M. D., Balch C. M. Natural killer (HNK-1+) cells in Chediak-Higashi patients are present in normal numbers but are abnormal in function and morphology. J Clin Invest 1982; 70: 193–197
   PubMed Web of Science ®Google Scholar
• Ward D. M., Griffiths G. M., Stinchcombe J. C., Kaplan J. Analysis of the lysosomal storage disease Chediak-Higashi syndrome. Traffic 2000; 1: 816–822
   PubMed Web of Science ®Google Scholar
• Ward D. M., Shiflett S. L., Kaplan J. Chediak-Higashi syndrome: A clinical and molecular view of a rare lysosomal storage disorder. Curr Mol Med 2002; 2: 469–477
   Google Scholar
• Certain S., Barrat F., Pastural E., Le Deist F., Goyo-Rivas J., Jabado N., et al. Protein truncation test of LYST reveals heterogenous mutations in patients with Chediak-Higashi syndrome. Blood 2000; 95: 979–983
   Google Scholar
• Zhao H., Boissy Y. L., Abdel-Malek Z., King R. A., Nordlund J. J., Boissy R. E. On the analysis of the pathophysiology of Chediak-Higashi syndrome. Defects expressed by cultured melanocytes. Lab Invest 1994; 71: 25–34
   Google Scholar
• Barbosa M. D., Barrat F. J., Tchernev V. T., Nguyen Q. A., Mishra V. S., Colman S. D., et al. Identification of mutations in two major mRNA isoforms of the Chediak-Higashi syndrome gene in human and mouse. Hum Mol Genet 1997; 6: 1091–1098
   Google Scholar
• Clark R., Griffiths G. M. Lytic granules, secretory lysosomes and disease. Curr Opin Immunol 2003; 15: 516–521
   PubMed Web of Science ®Google Scholar
• Kaplan J., De Domenico I., Ward D. M. Chediak-Higashi syndrome. Curr Opin Hematol 2008; 15: 22–29
   PubMed Web of Science ®Google Scholar
• Tomita Y., Suzuki T. Genetics of pigmentary disorders. Am J Med Genet C Semin Med Genet 2004; 131C: 75–81
   PubMedGoogle Scholar
• Griscelli C., Durandy A., Guy-Grand D., Daguillard F., Herzog C., Prunieras M. A syndrome associating partial albinism and immunodeficiency. Am J Med 1978; 65: 691–702
   PubMed Web of Science ®Google Scholar
• Wilson S. M., Yip R., Swing D. A., O'Sullivan T. N., Zhang Y., Novak E. K., et al. A mutation in Rab27a causes the vesicle transport defects observed in ashen mice. Proc Natl Acad Sci U S A 2000; 97: 7933–7938
   PubMed Web of Science ®Google Scholar
• Stinchcombe J. C., Barral D. C., Mules E. H., Booth S., Hume A. N., Machesky L. M., et al. Rab27a is required for regulated secretion in cytotoxic T lymphocytes. J Cell Biol 2001; 152: 825–834
   PubMedGoogle Scholar
• Munafo D. B., Johnson J. L., Ellis B. A., Rutschmann S., Beutler B., Catz S. D. Rab27a is a key component of the secretory machinery of azurophilic granules in granulocytes. Biochem J 2007; 402: 229–239
   Google Scholar
• Shotelersuk V., Dell'Angelica E. C., Hartnell L., Bonifacino J. S., Gahl W. A. A new variant of Hermansky-Pudlak syndrome due to mutations in a gene responsible for vesicle formation. Am J Med 2000; 108: 423–427
   PubMedGoogle Scholar
• Huizing M., Scher C. D., Strovel E., Fitzpatrick D. L., Hartnell L. M., Anikster Y., Gahl W. A. Nonsense mutations in ADTB3A cause complete deficiency of the beta3A subunit of adaptor complex-3 and severe Hermansky-Pudlak syndrome type 2. Pediatr Res 2002; 51: 150–158
   PubMed Web of Science ®Google Scholar
• Clark R. H., Stinchcombe J. C., Day A., Blott E., Booth S., Bossi G., et al. Adaptor protein 3-dependent microtubule-mediated movement of lytic granules to the immunological synapse. Nat Immunol 2003; 4: 1111–1120
   PubMed Web of Science ®Google Scholar
• Fontana S., Parolini S., Vermi W., Booth S., Gallo F., Donini M., et al. Innate immunity defects in Hermansky-Pudlak type 2 syndrome. Blood 2006; 107: 4857–4864
   PubMed Web of Science ®Google Scholar
• Jung J., Bohn G., Allroth A., Boztug K., Brandes G., Sandrock I., et al. Identification of a homozygous deletion in the AP3B1 gene causing Hermansky-Pudlak syndrome, type 2. Blood 2006; 108: 362–369
   PubMedGoogle Scholar
• Stinchcombe J., Bossi G., Griffiths G. M. Linking albinism and immunity: the secrets of secretory lysosomes. Science 2004; 305: 55–59
   PubMed Web of Science ®Google Scholar
• Huizing M., Gahl W. A. Disorders of vesicles of lysosomal lineage: The Hermansky-Pudlak syndromes. Curr Mol Med 2002; 2: 451–467
   PubMedGoogle Scholar
• Badolato R., Parolini S. Novel insights from adaptor protein 3 complex deficiency. J Allergy Clin Immunol 2007; 120: 735–741, quiz 742–733
   PubMedGoogle Scholar
• Bossi G., Griffiths G. M. CTL secretory lysosomes: Biogenesis and secretion of a harmful organelle. Semin Immunol 2005; 17: 87–94
   PubMed Web of Science ®Google Scholar
• Bohn G., Allroth A., Brandes G., Thiel J., Glocker E., Schaffer A. A., et al. A novel human primary immunodeficiency syndrome caused by deficiency of the endosomal adaptor protein p14. Nat Med 2007; 13: 38–45
   PubMed Web of Science ®Google Scholar
• Speckmann C., Rohr J., Ehl S. Genetic disorders of immune regulation. Primary Immunodeficiency Diseases: Definition, Diagnosis and Management, N. Rezaei, A. Aghamohammadi, L. D. Notarangelo. Springer-Verlag, Berlin Heidelberg 2008; 167–194
   Google Scholar
• Teis D., Taub N., Kurzbauer R., Hilber D., de Araujo M. E., Erlacher M., et al. p14-MP1-MEK1 signaling regulates endosomal traffic and cellular proliferation during tissue homeostasis. J Cell Biol 2006; 175: 861–868
   PubMed Web of Science ®Google Scholar
• Gorlin R. J., Gelb B., Diaz G. A., Lofsness K. G., Pittelkow M. R., Fenyk J. R., Jr. WHIM syndrome, an autosomal dominant disorder: clinical, hematological, and molecular studies. Am J Med Genet 2000; 91: 368–376
   PubMed Web of Science ®Google Scholar
• Aprikyan A. A., Liles W. C., Park J. R., Jonas M., Chi E. Y., Dale D. C. Myelokathexis, a congenital disorder of severe neutropenia characterized by accelerated apoptosis and defective expression of bcl-x in neutrophil precursors. Blood 2000; 95: 320–327
   PubMed Web of Science ®Google Scholar
• Diaz G. A., Gulino A. V. WHIM syndrome: A defect in CXCR4 signaling. Curr Allergy Asthma Rep 2005; 5: 350–355
   Google Scholar
• Gulino A. V. WHIM syndrome: A genetic disorder of leukocyte trafficking. Curr Opin Allergy Clin Immunol 2003; 3: 443–450
   PubMed Web of Science ®Google Scholar
• Latger-Cannard V., Bensoussan D., Bordigoni P. The WHIM syndrome shows a peculiar dysgranulopoiesis: Myelokathexis. Br J Haematol 2006; 132: 669
   Google Scholar
• Wetzler M., Talpaz M., Kleinerman E. S., King A., Huh Y. O., Gutterman J. U., Kurzrock R. A new familial immunodeficiency disorder characterized by severe neutropenia, a defective marrow release mechanism, and hypogammaglobulinemia. Am J Med 1990; 89: 663–672
   PubMed Web of Science ®Google Scholar
• Balabanian K., Lagane B., Pablos J. L., Laurent L., Planchenault T., Verola O., et al. WHIM syndromes with different genetic anomalies are accounted for by impaired CXCR4 desensitization to CXCL12. Blood 2005; 105: 2449–2457
   PubMed Web of Science ®Google Scholar
• Roland J., Murphy B. J., Ahr B., Robert-Hebmann V., Delauzun V., Nye K. E., et al. Role of the intracellular domains of CXCR4 in SDF-1-mediated signaling. Blood 2003; 101: 399–406
   Google Scholar
• Martin C., Burdon P. C., Bridger G., Gutierrez-Ramos J. C., Williams T. J., Rankin S. M. Chemokines acting via CXCR2 and CXCR4 control the release of neutrophils from the bone marrow and their return following senescence. Immunity 2003; 19: 583–593
   PubMed Web of Science ®Google Scholar
• Suratt B. T., Petty J. M., Young S. K., Malcolm K. C., Lieber J. G., Nick J. A., et al. Role of the CXCR4/SDF-1 chemokine axis in circulating neutrophil homeostasis. Blood 2004; 104: 565–571
   Web of Science ®Google Scholar
• Semerad C. L., Liu F., Gregory A. D., Stumpf K., Link D. C. G-CSF is an essential regulator of neutrophil trafficking from the bone marrow to the blood. Immunity 2002; 17: 413–423
   PubMed Web of Science ®Google Scholar
• Valenzuela-Fernandez A., Planchenault T., Baleux F., Staropoli I., Le-Barillec K., Leduc D., et al. Leukocyte elastase negatively regulates stromal cell-derived factor-1 (SDF-1]/CXCR4 binding and functions by amino-terminal processing of SDF-1 and CXCR4. J Biol Chem 2002; 277: 15677–15689
   PubMed Web of Science ®Google Scholar
• Notarangelo L. D., Duse M., Ugazio A. G. Immunodeficiency with hyper-IgM (HIM). Immunodefic Rev 1992; 3: 101–121
   PubMedGoogle Scholar
• Fuleihan R., Ramesh N., Loh R., Jabara H., Rosen R. S., Chatila T., et al. Defective expression of the CD40 ligand in X chromosome-linked immunoglobulin deficiency with normal or elevated IgM. Proc Natl Acad Sci U S A 1993; 90: 2170–2173
   PubMed Web of Science ®Google Scholar
• Levy J., Espanol-Boren T., Thomas C., Fischer A., Tovo P., Bordigoni P., et al. Clinical spectrum of X-linked hyper-IgM syndrome. J Pediatr 1997; 131: 47–54
   PubMed Web of Science ®Google Scholar
• Rezaei N., Aghamohammadi A., Ramyar A., Pan-Hammarstrom Q., Hammarstrom L. Severe congenital neutropenia or hyper-IgM syndrome? A novel mutation of CD40 ligand in a patient with severe neutropenia. Int Arch Allergy Immunol 2008; 147: 255–259
   PubMed Web of Science ®Google Scholar
• Hayward A. R., Levy J., Facchetti F., Notarangelo L., Ochs H. D., Etzioni A., et al. Cholangiopathy and tumors of the pancreas, liver, and biliary tree in boys with X-linked immunodeficiency with hyper-IgM. J Immunol 1997; 158: 977–983
   PubMed Web of Science ®Google Scholar
• Nagaraj N., Egwim C., Adler D. G. X-linked hyper-IgM syndrome associated with poorly differentiated neuroendocrine tumor presenting as obstructive jaundice secondary to extensive adenopathy. Dig Dis Sci 2007; 52: 2312–2316
   PubMed Web of Science ®Google Scholar
• Aruffo A., Farrington M., Hollenbaugh D., Li X., Milatovich A., Nonoyama S., et al. The CD40 ligand, gp39, is defective in activated T cells from patients with X-linked hyper-IgM syndrome. Cell 1993; 72: 291–300
   PubMed Web of Science ®Google Scholar
• Kroczek R. A., Graf D., Brugnoni D., Giliani S., Korthuer U., Ugazio A., et al. Defective expression of CD40 ligand on T cells causes “X-linked immunodeficiency with hyper-IgM (HIGM1)”. Immunol Rev 1994; 138: 39–59
   PubMed Web of Science ®Google Scholar
• Atarod L., Aghamohammadi A., Moin M., Kanegane H., Rezaei N., Rezaei Kalantari K., et al. Successful management of neutropenia in a patient with CD40 ligand deficiency by immunoglobulin replacement therapy. Iran J Allergy Asthma Immunol 2007; 6: 37–40
   PubMed Web of Science ®Google Scholar
• Mori M., Nonoyama S., Neubauer M., Mitsuda T., Kosuge K., Yokota S. Mutation analysis and therapeutic response to granulocyte colony-stimulating factor in a case of hyperimmunoglobulin M syndrome with chronic neutropenia. J Pediatr Hematol Oncol 2000; 22: 288–289
   PubMed Web of Science ®Google Scholar
• Aghamohammadi A., Lougaris V., Plebani A., Miyawaki M., Durandy A., Hammarstorm L. Predominantly antibody deficiencies. Primary Immunodeficiency Diseases, N. Rezaei, A. Aghamohammadi, L. D. Notarangelo. Springer, Berlin Heidelburg 2008; 97–130
   Google Scholar
• Aghamohammadi A., Fiorini M., Moin M., Parvaneh N., Teimourian S., Yeganeh M., et al. Clinical, immunological and molecular characteristics of 37 Iranian patients with X-linked agammaglobulinemia. Int Arch Allergy Immunol 2006; 141: 408–414
   PubMed Web of Science ®Google Scholar
• Moin M., Aghamohammadi A., Farhoudi A., Pourpak Z., Rezaei N., Movahedi M., et al. X-linked agammaglobulinemia: A survey of 33 Iranian patients. Immunol Invest 2004; 33: 81–93
   PubMed Web of Science ®Google Scholar
• Conley M. E., Howard V. Clinical findings leading to the diagnosis of X-linked agammaglobulinemia. J Pediatr 2002; 141: 566–571
   PubMed Web of Science ®Google Scholar
• Kanegane H., Taneichi H., Nomura K., Futatani T., Miyawaki T. Severe neutropenia in Japanese patients with x-linked agammaglobulinemia. J Clin Immunol 2005; 25: 491–495
   PubMed Web of Science ®Google Scholar
• Aghamohammadi A., Cheraghi T., Rezaei N., Kanegane H., Abdollahzede S., Talaei-Khoei M., et al. Neutropenia associated with x-linked agammaglobulinemia in an Iranian referral center. Iran J Allergy Asthma Immunol 2009; 8: 43–47
   Google Scholar
• Lederman H. M., Winkelstein J. A. X-linked agammaglobulinemia: An analysis of 96 patients. Medicine (Baltimore) 1985; 64: 145–156
   PubMed Web of Science ®Google Scholar
• Verbruggen G., De Backer S., Deforce D., Demetter P., Cuvelier C., Veys E., Elewaut D. X linked agammaglobulinaemia and rheumatoid arthritis. Ann Rheum Dis 2005; 64: 1075–1078
   PubMed Web of Science ®Google Scholar
• Ferrari S., Zuntini R., Lougaris V., Soresina A., Sourkova V., Fiorini M., et al. Molecular analysis of the pre-BCR complex in a large cohort of patients affected by autosomal-recessive agammaglobulinemia. Genes Immun 2007; 8: 325–333
   PubMed Web of Science ®Google Scholar
• Yel L., Minegishi Y., Coustan-Smith E., Buckley R. H., Trubel H., Pachman L. M., et al. Mutations in the mu heavy-chain gene in patients with agammaglobulinemia. N Engl J Med 1996; 335: 1486–1493
   PubMed Web of Science ®Google Scholar
• Tsukada S., Saffran D. C., Rawlings D. J., Parolini O., Allen R. C., Klisak I., et al. Deficient expression of a B cell cytoplasmic tyrosine kinase in human X-linked agammaglobulinemia. Cell 1993; 72: 279–290
   PubMed Web of Science ®Google Scholar
• Valiaho J., Smith C. I., Vihinen M. BTKbase: The mutation database for X-linked agammaglobulinemia. Hum Mutat 2006; 27: 1209–1217
   PubMed Web of Science ®Google Scholar
• Minegishi Y., Coustan-Smith E., Wang Y. H., Cooper M. D., Campana D., Conley M. E. Mutations in the human lambda5/14.1 gene result in B cell deficiency and agammaglobulinemia. J Exp Med 1998; 187: 71–77
   PubMed Web of Science ®Google Scholar
• Wang Y., Kanegane H., Sanal O., Tezcan I., Ersoy F., Futatani T., Miyawaki T. Novel Igalpha (CD79a) gene mutation in a Turkish patient with B cell-deficient agammaglobulinemia. Am J Med Genet 2002; 108: 333–336
   PubMed Web of Science ®Google Scholar
• Dobbs A. K., Yang T., Farmer D., Kager L., Parolini O., Conley M. E. Cutting edge: A hypomorphic mutation in Igbeta (CD79b) in a patient with immunodeficiency and a leaky defect in B cell development. J Immunol 2007; 179: 2055–2059
   PubMed Web of Science ®Google Scholar
• Ferrari S., Lougaris V., Caraffi S., Zuntini R., Yang J., Soresina A., et al. Mutations of the Igbeta gene cause agammaglobulinemia in man. J Exp Med 2007; 204: 2047–2051
   PubMed Web of Science ®Google Scholar
• Minegishi Y., Rohrer J., Coustan-Smith E., Lederman H. M., Pappu R., Campana D., et al. An essential role for BLNK in human B cell development. Science 1999; 286: 1954–1957
   PubMed Web of Science ®Google Scholar
• Farrar J. E., Rohrer J., Conley M. E. Neutropenia in X-linked agammaglobulinemia. Clin Immunol Immunopathol 1996; 81: 271–276
   PubMedGoogle Scholar
• Tavil B., Sipahi T. Is neutropenia a clue for early diagnosis of X-linked agammaglobulinemia?. Pediatr Hematol Oncol 2003; 20: 657–658
   Google Scholar
• Le Deist F., Moshous D., Howe S. J., Nahum A., Kavadas F. D., Lavine E., . Combined T and B cell immunodeficiencies. Primary Immunodeficiency Diseases, N. Rezaei, A. Aghamohammadi, L. D. Notarangelo, et al. Springer, Heidelberg, Berlin 2008; 39–95
   Google Scholar
• Cacciapuoti G., Porcelli M., Bertoldo C., Fusco S., De Rosa M., Zappia V. Extremely thermophilic and thermostable 5′-methylthioadenosine phosphorylase from the archaeon sulfolobus solfataricus. Gene cloning and amino acid sequence determination. Eur J Biochem 1996; 239: 632–637
   Google Scholar
• Dalal I., Grunebaum E., Cohen A., Roifman C. M. Two novel mutations in a purine nucleoside phosphorylase (PNP)-deficient patient. Clin Genet 2001; 59: 430–437
   PubMed Web of Science ®Google Scholar
• Hallett R. J., Cronin S. M., Morgan G., Duley J. A., Fairbanks L. D., Simmonds H. A. Normal uric acid concentrations in a purine nucleoside phosphorylase (PNP) deficient child presenting with severe chicken pox, possible immunodeficiency and developmental delay. Adv Exp Med Biol 1994; 370: 387–389
   PubMedGoogle Scholar
• Fleischman A., Hershfield M. S., Toutain S., Lederman H. M., Sullivan K. E., Fasano M. B., et al. Adenosine deaminase deficiency and purine nucleoside phosphorylase deficiency in common variable immunodeficiency. Clin Diagn Lab Immunol 1998; 5: 399–400
   PubMedGoogle Scholar
• Gudas L. J., Ullman B., Cohen A., Martin D. W., Jr. Deoxyguanosine toxicity in a mouse T lymphoma: Relationship to purine nucleoside phosphorylase-associated immune dysfunction. Cell 1978; 14: 531–538
   PubMedGoogle Scholar
• Sidi Y., Gelvan I., Brosh S., Pinkhas J., Sperling O. Guanine nucleotide metabolism in red blood cells: The metabolic basis for GTP depletion in HGPRT and PNP deficiency. Adv Exp Med Biol 1989; 253A: 67–71
   PubMedGoogle Scholar
• Simmonds H. A., Fairbanks L. D., Morris G. S., Morgan G., Watson A. R., Timms P., Singh B. Central nervous system dysfunction and erythrocyte guanosine triphosphate depletion in purine nucleoside phosphorylase deficiency. Arch Dis Child 1987; 62: 385–391
   PubMed Web of Science ®Google Scholar
• Worth A., Thrasher A. J., Gaspar H. B. Autoimmune lymphoproliferative syndrome: Molecular basis of disease and clinical phenotype. Br J Haematol 2006; 133: 124–140
   PubMed Web of Science ®Google Scholar
• Bleesing J. J., Brown M. R., Novicio C., Guarraia D., Dale J. K., Straus S. E., Fleisher T. A. A composite picture of TcR alpha/beta(+) CD4(-)CD8(-) T cells (alpha/beta-DNTCs) in humans with autoimmune lymphoproliferative syndrome. Clin Immunol 2002; 104: 21–30
   PubMed Web of Science ®Google Scholar
• Lopatin U., Yao X., Williams R. K., Bleesing J. J., Dale J. K., Wong D., et al. Increases in circulating and lymphoid tissue interleukin-10 in autoimmune lymphoproliferative syndrome are associated with disease expression. Blood 2001; 97: 3161–3170
   PubMed Web of Science ®Google Scholar
• Kwon S. W., Procter J., Dale J. K., Straus S. E., Stroncek D. F. Neutrophil and platelet antibodies in autoimmune lymphoproliferative syndrome. Vox Sang 2003; 85: 307–312
   PubMed Web of Science ®Google Scholar
• Fuss I. J., Strober W., Dale J. K., Fritz S., Pearlstein G. R., Puck J. M., et al. Characteristic T helper 2 T cell cytokine abnormalities in autoimmune lymphoproliferative syndrome, a syndrome marked by defective apoptosis and humoral autoimmunity. J Immunol 1997; 158: 1912–1918
   PubMed Web of Science ®Google Scholar
• Wu J., Wilson J., He J., Xiang L., Schur P. H., Mountz J. D. Fas ligand mutation in a patient with systemic lupus erythematosus and lymphoproliferative disease. J Clin Invest 1996; 98: 1107–1113
   PubMed Web of Science ®Google Scholar
• Chun H. J., Zheng L., Ahmad M., Wang J., Speirs C. K., Siegel R. M., et al. Pleiotropic defects in lymphocyte activation caused by caspase-8 mutations lead to human immunodeficiency. Nature 2002; 419: 395–399
   PubMed Web of Science ®Google Scholar
• Wang J., Zheng L., Lobito A., Chan F. K., Dale J., Sneller M., et al. Inherited human caspase 10 mutations underlie defective lymphocyte and dendritic cell apoptosis in autoimmune lymphoproliferative syndrome type II. Cell 1999; 98: 47–58
   PubMed Web of Science ®Google Scholar
• Makitie O., Rajantie J., Kaitila I. Anaemia and macrocytosis—Unrecognized features in cartilage-hair hypoplasia. Acta Paediatr 1992; 81: 1026–1029
   Google Scholar
• Lux S. E., Johnston R. B., Jr., August C. S., Say B., Penchaszadeh V. B., Rosen F. S., McKusick V. A. Chronic neutropenia and abnormal cellular immunity in cartilage-hair hypoplasia. N Engl J Med 1970; 282: 231–236
   PubMed Web of Science ®Google Scholar
• Virolainen M., Savilahti E., Kaitila I., Perheentupa J. Cellular and humoral immmunity in cartilage-hair hypoplasia. Pediatr Res 1978; 12: 961–966
   Google Scholar
• Makitie O., Kaitila I., Savilahti E. Susceptibility to infections and in vitro immune functions in cartilage-hair hypoplasia. Eur J Pediatr 1998; 157: 816–820
   Google Scholar
• Makitie O., Kaitila I., Savilahti E. Deficiency of humoral immunity in cartilage-hair hypoplasia. J Pediatr 2000; 137: 487–492
   Google Scholar
• Makitie O., Marttinen E., Kaitila I. Skeletal growth in cartilage-hair hypoplasia. A radiological study of 82 patients. Pediatr Radiol 1992; 22: 434–439
   Google Scholar
• Makitie O., Heikkinen M., Kaitila I., Rintala R. Hirschsprung's disease in cartilage-hair hypoplasia has poor prognosis. J Pediatr Surg 2002; 37: 1585–1588
   Google Scholar
• Ridanpaa M., van Eenennaam H., Pelin K., Chadwick R., Johnson C., Yuan B., et al. Mutations in the RNA component of RNase MRP cause a pleiotropic human disease, cartilage-hair hypoplasia. Cell 2001; 104: 195–203
   PubMed Web of Science ®Google Scholar
• Gitzelmann R., Bosshard N. U. Defective neutrophil and monocyte functions in glycogen storage disease type Ib: A literature review. Eur J Pediatr 1993; 152(Suppl 1)S33–S38
   Google Scholar
• Garty B. Z., Douglas S. D., Danon Y. L. Immune deficiency in glycogen storage disease type 1B. Isr J Med Sci 1996; 32: 1276–1281
   PubMedGoogle Scholar
• Rake J. P., Visser G., Labrune P., Leonard J. V., Ullrich K., Smit G. P. Glycogen storage disease type I: Diagnosis, management, clinical course and outcome. Results of the European Study on Glycogen Storage Disease Type I (ESGSD I). Eur J Pediatr 2002; 161(Suppl 1)S20–S34
   Google Scholar
• Chou J. Y., Matern D., Mansfield B. C., Chen Y. T. Type I glycogen storage diseases: Disorders of the glucose-6-phosphatase complex. Curr Mol Med 2002; 2: 121–143
   PubMedGoogle Scholar
• Lei K. J., Chen H., Pan C. J., Ward J. M., Mosinger B., Jr., Lee E. J., et al. Glucose-6-phosphatase dependent substrate transport in the glycogen storage disease type-1a mouse. Nat Genet 1996; 13: 203–209
   PubMed Web of Science ®Google Scholar
• Hiraiwa H., Pan C. J., Lin B., Moses S. W., Chou J. Y. Inactivation of the glucose 6-phosphate transporter causes glycogen storage disease type 1b. J Biol Chem 1999; 274: 5532–5536
   PubMedGoogle Scholar
• Lee A. S. The glucose-regulated proteins: Stress induction and clinical applications. Trends Biochem Sci 2001; 26: 504–510
   PubMed Web of Science ®Google Scholar
• Kim S. Y., Jun H. S., Mead P. A., Mansfield B. C., Chou J. Y. Neutrophil stress and apoptosis underlie myeloid dysfunction in glycogen storage disease type Ib. Blood 2008; 111: 5704–5711
   PubMed Web of Science ®Google Scholar
• Kelley R. I., Cheatham J. P., Clark B. J., Nigro M. A., Powell B. R., Sherwood G. W., et al. X-linked dilated cardiomyopathy with neutropenia, growth retardation, and 3-methylglutaconic aciduria. J Pediatr 1991; 119: 738–747
   PubMed Web of Science ®Google Scholar
• Mazzocco M. M., Kelley R. I. Preliminary evidence for a cognitive phenotype in Barth syndrome. Am J Med Genet 2001; 102: 372–378
   PubMed Web of Science ®Google Scholar
• Barth P. G., Valianpour F., Bowen V. M., Lam J., Duran M., Vaz F. M., Wanders R. J. X-linked cardioskeletal myopathy and neutropenia (Barth syndrome): An update. Am J Med Genet A 2004; 126A: 349–354
   PubMed Web of Science ®Google Scholar
• Barth P. G., Van den Bogert C., Bolhuis P. A., Scholte H. R., van Gennip A. H., Schutgens R. B., Ketel A. G. X-linked cardioskeletal myopathy and neutropenia (Barth syndrome): Respiratory-chain abnormalities in cultured fibroblasts. J Inherit Metab Dis 1996; 19: 157–160
   PubMed Web of Science ®Google Scholar
• Bione S., D'Adamo P., Maestrini E., Gedeon A. K., Bolhuis P. A., Toniolo D. A novel X-linked gene, G4.5. is responsible for Barth syndrome. Nat Genet 1996; 12: 385–389
   PubMed Web of Science ®Google Scholar
• Kuijpers T. W., Maianski N. A., Tool A. T., Becker K., Plecko B., Valianpour F., et al. Neutrophils in Barth syndrome (BTHS) avidly bind annexin-V in the absence of apoptosis. Blood 2004; 103: 3915–3923
   PubMed Web of Science ®Google Scholar
• Alter B. P. Diagnosis, genetics, and management of inherited bone marrow failure syndromes. Hematology Am Soc Hematol Educ Program 2007; 2007: 29–39
   Google Scholar
• Dokal I. Dyskeratosis congenita in all its forms. Br J Haematol 2000; 110: 768–779
   PubMed Web of Science ®Google Scholar
• Heiss N. S., Knight S. W., Vulliamy T. J., Klauck S. M., Wiemann S., Mason P. J., et al. X-linked dyskeratosis congenita is caused by mutations in a highly conserved gene with putative nucleolar functions. Nat Genet 1998; 19: 32–38
   PubMed Web of Science ®Google Scholar
• Vulliamy T. J., Marrone A., Knight S. W., Walne A., Mason P. J., Dokal I. Mutations in dyskeratosis congenita: Their impact on telomere length and the diversity of clinical presentation. Blood 2006; 107: 2680–2685
   PubMed Web of Science ®Google Scholar
• Vulliamy T. J., Walne A., Baskaradas A., Mason P. J., Marrone A., Dokal I. Mutations in the reverse transcriptase component of telomerase (TERT) in patients with bone marrow failure. Blood Cells Mol Dis 2005; 34: 257–263
   PubMed Web of Science ®Google Scholar
• Walne A. J., Vulliamy T., Marrone A., Beswick R., Kirwan M., Masunari Y., et al. Genetic heterogeneity in autosomal recessive dyskeratosis congenita with one subtype due to mutations in the telomerase-associated protein NOP10. Hum Mol Genet 2007; 16: 1619–1629
   PubMed Web of Science ®Google Scholar
• Vulliamy T., Dokal I. Dyskeratosis congenita. Semin Hematol 2006; 43: 157–166
   PubMed Web of Science ®Google Scholar
• Roper M., Parmley R. T., Crist W. M., Kelly D. R., Cooper M. D. Severe congenital leukopenia (reticular dysgenesis). Immunologic and morphologic characterizations of leukocytes. Am J Dis Child 1985; 139: 832–835
   Google Scholar
• Haas R. J., Niethammer D., Goldmann S. F., Heit W., Bienzle U., Kleihauer E. Congenital immunodeficiency and agranulocytosis (reticular dysgenesia). Acta Paediatr Scand 1977; 66: 279–283
   Google Scholar
• Pannicke U., Honig M., Hess I., Friesen C., Holzmann K., Rump E. M., et al. Reticular dysgenesis (aleukocytosis) is caused by mutations in the gene encoding mitochondrial adenylate kinase 2. Nat Genet 2009; 41: 101–105
   PubMedGoogle Scholar
• Lagresle-Peyrou C., Six E. M., Picard C., Rieux-Laucat F., Michel V., Ditadi A., et al. Human adenylate kinase 2 deficiency causes a profound hematopoietic defect associated with sensorineural deafness. Nat Genet 2009; 41: 106–111
   PubMed Web of Science ®Google Scholar
• Kivitie-Kallio S., Norio R. Cohen syndrome: Essential features, natural history, and heterogeneity. Am J Med Genet 2001; 102: 125–135
   PubMed Web of Science ®Google Scholar
• Kivitie-Kallio S., Rajantie J., Juvonen E., Norio R. Granulocytopenia in Cohen syndrome. Br J Haematol 1997; 98: 308–311
   Google Scholar
• Alaluusua S., Kivitie-Kallio S., Wolf J., Haavio M. L., Asikainen S., Pirinen S. Periodontal findings in Cohen syndrome with chronic neutropenia. J Periodontol 1997; 68: 473–478
   Google Scholar
• Olivieri O., Lombardi S., Russo C., Corrocher R. Increased neutrophil adhesive capability in Cohen syndrome, an autosomal recessive disorder associated with granulocytopenia. Haematologica 1998; 83: 778–782
   Google Scholar
• Kolehmainen J., Black G. C., Saarinen A., Chandler K., Clayton-Smith J., Traskelin A. L., et al. Cohen syndrome is caused by mutations in a novel gene, COH1, encoding a transmembrane protein with a presumed role in vesicle-mediated sorting and intracellular protein transport. Am J Hum Genet 2003; 72: 1359–1369
   PubMed Web of Science ®Google Scholar
• Velayos-Baeza A., Vettori A., Copley R. R., Dobson-Stone C., Monaco A. P. Analysis of the human VPS13 gene family. Genomics 2004; 84: 536–549
   PubMed Web of Science ®Google Scholar
• Dale D. C., Cottle T. E., Fier C. J., Bolyard A. A., Bonilla M. A., Boxer L. A., et al. Severe chronic neutropenia: Treatment and follow-up of patients in the Severe Chronic Neutropenia International Registry. Am J Hematol 2003; 72: 82–93
   PubMed Web of Science ®Google Scholar
• Dale D. C., Bonilla M. A., Davis M. W., Nakanishi A. M., Hammond W. P., Kurtzberg J., et al. A randomized controlled phase III trial of recombinant human granulocyte colony-stimulating factor (filgrastim) for treatment of severe chronic neutropenia. Blood 1993; 81: 2496–2502
   PubMed Web of Science ®Google Scholar
• Bonilla M. A., Gillio A. P., Ruggeiro M., Kernan N. A., Brochstein J. A., Abboud M., et al. Effects of recombinant human granulocyte colony-stimulating factor on neutropenia in patients with congenital agranulocytosis. N Engl J Med 1989; 320: 1574–1580
   PubMed Web of Science ®Google Scholar
• Berliner N. Lessons from congenital neutropenia: 50 years of progress in understanding myelopoiesis. Blood 2008; 111: 5427–5432
   Google Scholar
• Lord B. I., Bronchud M. H., Owens S., Chang J., Howell A., Souza L., Dexter T. M. The kinetics of human granulopoiesis following treatment with granulocyte colony-stimulating factor in vivo. Proc Natl Acad Sci U S A 1989; 86: 9499–9503
   PubMed Web of Science ®Google Scholar
• Anderlini P., Przepiorka D., Champlin R., Korbling M. Biologic and clinical effects of granulocyte colony-stimulating factor in normal individuals. Blood 1996; 88: 2819–2825
   PubMed Web of Science ®Google Scholar
• Rex J. H., Bhalla S. C., Cohen D. M., Hester J. P., Vartivarian S. E., Anaissie E. J. Protection of human polymorphonuclear leukocyte function from the deleterious effects of isolation, irradiation, and storage by interferon-gamma and granulocyte-colony-stimulating factor. Transfusion 1995; 35: 605–611
   PubMed Web of Science ®Google Scholar
• Maianski N. A., Mul F. P., van Buul J. D., Roos D., Kuijpers T. W. Granulocyte colony-stimulating factor inhibits the mitochondria-dependent activation of caspase-3 in neutrophils. Blood 2002; 99: 672–679
   PubMed Web of Science ®Google Scholar
• Freedman M. H., Bonilla M. A., Fier C., Bolyard A. A., Scarlata D., Boxer L. A., et al. Myelodysplasia syndrome and acute myeloid leukemia in patients with congenital neutropenia receiving G-CSF therapy. Blood 2000; 96: 429–436
   PubMed Web of Science ®Google Scholar
• Zeidler C., Welte K., Barak Y., Barriga F., Bolyard A. A., Boxer L., et al. Stem cell transplantation in patients with severe congenital neutropenia without evidence of leukemic transformation. Blood 2000; 95: 1195–1198
   PubMed Web of Science ®Google Scholar