2015, Number 2
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Rev Mex Patol Clin Med Lab 2015; 62 (2)
Synaptophysin is frequently expressed in megakaryocytes: a novel immunohistochemical finding of unknow significance
Ruiz-Cordero R, Chapman J, Vega F
Language: English
References: 27
Page: 76-80
PDF size: 447.20 Kb.
ABSTRACT
Introduction: Synaptophysin is an integral membrane glycoprotein predominantly present in small synaptic vesicles in the brain. Its expression in human megakaryocytes has not been previously described.
Objective: To determine the expression of synaptophysin in human megakaryocytes by means of immunohistochemistry.
Material and methods: Bone marrow biopsies performed for evaluation of relapse, diagnostic or staging purposes in patients with hematologic diseases (neoplastic or non-neoplastic) were stained by immunohistochemistry with a monoclonal mouse anti-human antibody for synaptophysin and a polyclonal rabbit anti-human antibody for factor VIII (FVIII). Biopsies whose final interpretation was negative for tumor/disease were used as controls.
Results: A total of 20 bone marrow biopsies (15 cases/5 controls) belonging to 20 patients with a median age was 52 years (2 to 83) were studied. Eleven of the 15 cases had diagnoses of hematologic malignancy and four of idiopathic/immune thrombocytopenic purpura (ITP). Cytoplasmic expression of FVIII was observed in all megakaryocytes. Synaptophysin expression was present in all controls and in 13 of 15 (90%) cases. In two of the four (50%) ITP, the megakaryocytes did not stain for synaptophysin but stained for FVIII.
Conclusions: Synaptophysin expression was frequently detected by immunohistochemistry in megakaryocytes. However, it was not expressed in a subset of patients with ITP. Further studies are necessary to determine the clinical significance of these findings.
REFERENCES
Jahn R, Schiebler W, Ouimet C, Greengard P. A 38,000-dalton membrane protein (p38) present in synaptic vesicles. Proc Natl Acad Sci USA. 1985; 82 (12): 4137-4141.
Wiedenmann B, Franke WW. Identification and localization of synaptophysin, an integral membrane glycoprotein of Mr 38,000 characteristic of presynaptic vesicles. Cell. 1985; 41 (3): 1017-1028.
Valtorta F, Pennuto M, Bonanomi D, Benfenati F. Synaptophysin: leading actor or walk-on role in synaptic vesicle exocytosis? Bioessays. 2004; 26 (4): 445-453.
Ozcelik T, Lafreniere RG, Archer BT 3rd, Johnston PA, Willard HF, Francke U et al. Synaptophysin: structure of the human gene and assignment to the X chromosome in man and mouse. Am J Hum Genet. 1990; 47 (3): 551-561.
Knaus P, Betz H, Rehm H. Expression of synaptophysin during postnatal development of the mouse brain. J Neurochem. 1986; 47 (4): 1302-1304.
Wiedenmann B, Huttner WB. Synaptophysin and chromogranins/ secretogranins--widespread constituents of distinct types of neuroendocrine vesicles and new tools in tumor diagnosis. Virchows Arch B Cell Pathol Incl Mol Pathol. 1989; 58 (2): 95-121.
Bähler M, Cesura AM, Fischer G, Kuhn H, Klein RL, Da Prada M. Serotonin organelles of rabbit platelets contain synaptophysin. Eur J Biochem. 1990; 194 (3): 825-829.
Brunger AT. Structural insights into the molecular mechanism of calcium-dependent vesicle-membrane fusion. Curr Opin Struct Biol. 2001; 11 (2): 163-173.
Brunger AT. Structure of proteins involved in synaptic vesicle fusion in neurons. Annu Rev Biophys Biomol Struct. 2001; 30: 157-171.
Chen D, Lemons PP, Schraw T, Whiteheart SW. Molecular mechanisms of platelet exocytosis: role of SNAP-23 and syntaxin 2 and 4 in lysosome release. Blood. 2000; 96 (5): 1782-1788.
Flaumenhaft R. Molecular basis of platelet granule secretion. Arterioscler Thromb Vasc Biol. 2003; 23 (7): 1152-1160.
Lemons PP, Chen D, Bernstein AM, Bennett MK, Whiteheart SW. Regulated secretion in platelets: identification of elements of the platelet exocytosis machinery. Blood. 1997; 90 (4): 1490-1500.
Deutsch VR, Tomer A. Megakaryocyte development and platelet production. Br J Haematol. 2006; 134 (5): 453-466.
Wright J. The origin and nature of blood platelets. Bost Med Surg J. 1906; 154: 643.
Wright J. The histogenesis of the blood platelets. J Morphol. 1910; 21: 263.
Kaushansky K. Historical review: megakaryopoiesis and thrombopoiesis. Blood. 2008; 111 (3): 981-986.
Brecher G, Cronkite EP. Morphology and enumeration of human blood platelets. J Appl Physiol. 1950; 3 (6): 365-377.
Penington DG, Olsen TE. Megakaryocytes in states of altered platelet production: cell numbers, size and DNA content. Br J Haematol. 1970; 18 (4): 447-463.
Harker LA, Finch CA. Thrombokinetics in man. J Clin Invest. 1969; 48 (6): 963-974.
Kobayashi Y, Ozawa M, Maruo N, Kondo M. Megakaryocytic ploidy in myelodysplastic syndromes. Leuk Lymphoma. 1993; 9 (1-2): 55-61.
Brummitt DR, Barker HF, Pujol-Moix N. A new platelet parameter, the mean platelet component, can demonstrate abnormal platelet function and structure in myelodysplasia. Clin Lab Haematol. 2003; 25 (1): 59-62.
Hicsonmez G, Gumruk F, Cetin M, Ozbek N, Tuncer M, Gursel T. Bernard-Soulier-like functional platelet defect in myelodysplastic syndrome and in acute myeloblastic leukemia associated with trilineage myelodysplasia. Turk J Pediatr. 1995; 37 (4): 425-429.
Gerrard JM, Lint D, Sims PJ, Wiedmer T, Fugate RD, McMillan E et al. Identification of a platelet dense granule membrane protein that is deficient in a patient with the Hermansky-Pudlak syndrome. Blood. 1991; 77 (1): 101-112.
Nishibori M, Cham B, McNicol A, Shalev A, Jain N, Gerrard JM. The protein CD63 is in platelet dense granules, is deficient in a patient with Hermansky-Pudlak syndrome, and appears identical to granulophysin. J Clin Invest. 1993; 91 (4): 1775-1782.
Haass NK, Kartenbeck MA, Leube RE. Pantophysin is a ubiquitously expressed synaptophysin homologue and defines constitutive transport vesicles. J Cell Biol. 1996; 134 (3): 731-746.
Li C, Ullrich B, Zhang JZ, Anderson RG, Brose N, Sudhof TC. Ca(2+)-dependent and -independent activities of neural and nonneural synaptotagmins. Nature. 1995; 375 (6532): 594-599.
Jayakumar AR, Tong XY, Curtis KM, Ruiz-Cordero R, Shamaladevi N, Abuzamel M et al. Decreased astrocytic thrombospondin-1 secretion after chronic ammonia treatment reduces the level of synaptic proteins: in vitro and in vivo studies. J Neurochem. 2014; 131 (3): 333-347.