Advances in platelet granule biology

Koseoglu, Secil; Flaumenhaft, Robert

doi:10.1097/moh.0b013e3283632e6b

Cited by 65 publications

(64 citation statements)

References 56 publications

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“…Much recent information suggests that multiple proteins combine to influence platelet a-granule number and content; and to ensure rapid secretion of their contents after appropriate stimulation [35]. Formed from multivesicular precursors, there is accumulating evidence for a-granule heterogeneity although there are conflicting reports on whether this is due to specific granule subtypes with proor anti-angiogenic cargos or simply that some a-granule contents are enriched in specific compartments of the organelle [reviewed in Ref.…”

Section: Discussionmentioning

confidence: 99%

Should any genetic defect affecting α‐granules in platelets be classified as gray platelet syndrome?

Nurden

2016

American J Hematol

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There is much current interest in the role of the platelet storage pool of α‐granule proteins both in hemostasis and non‐hemostatic events. As well as in the arrest of bleeding, the secreted proteins participate in wound healing, inflammation, and innate immunity while in pathology they may be actors in arterial thrombosis and atherosclerosis as well as cancer and metastasis. For a long time, gray platelet syndrome (GPS) has been regarded as the classic inherited platelet disorder caused by an absence of α‐granules and their contents. While NBEAL2 is the major source of mutations in GPS, other gene variants may give rise to significant α‐granule deficiencies in platelets. These include GATA1, VPS33B, or VIPAS39 in the arthrogryposis, renal dysfunction, and cholestasis (ARC) syndrome and now GFI1B. Nevertheless, many phenotypic differences are associated with mutations in these genes. This critical review was aimed to assess genotype/phenotype variability in disorders of platelet α‐granule biogenesis and to urge caution in grouping all genetic defects of α‐granules as GPS. Am. J. Hematol. 91:714–718, 2016. © 2016 Wiley Periodicals, Inc.

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Section: Discussionmentioning

confidence: 99%

Should any genetic defect affecting α‐granules in platelets be classified as gray platelet syndrome?

Nurden

2016

American J Hematol

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“…SNAREs proteins that are localized in opposing membranes drive membrane fusion by the formation of a four-helix bundle complex [14]. It appears to be that VAMP-8, syntaxin-2, and SNAP-23 are the key SNAREs that are involved in platelet α-granule secretion [15,16]. Studies reveal that Sec/Munc18-like (SM) proteins function as clamps to 'prime' SNAREs proteins for assembly into tight SNAREs complex, which destine to fuse and release platelet α-granule.…”

Section: Oncotarget 2 Wwwimpactjournalscom/oncotargetmentioning

confidence: 99%

“…Syntaxin2, a t-SNARE, plays an important role in platelet exocytotic core complex [44]. As well, SNAP (synaptosomal-associated protein) 23, another family of t-SNAREs, is a main SNAP family member and also essential for the release of granules in platelets [16]. Thus, VAMP8, syntaxin2 and SNAP23 appear to be essential for SNAREs complex formation in platelet α-granule exocytosis.…”

Section: Figure 5: Effects Of Corm-2 On Platelet Munc18a Expression Amentioning

confidence: 99%

WITHDRAWN: "Exogenous carbon monoxide suppresses LPS-induced platelet SNAREs complex assembly and Î±-granule exocytosis via integrin Î±IIbÎ²3-mediated PKCÎ¸/Munc18a pathway"

Zhuang¹,

Song²,

Liu³

et al. 2018

Oncotarget

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Activation of coagulation occurs in sepsis and contributes to the development of thrombosis. Platelet α-granule exocytosis plays an important role in septic coagulation abnormalities. The present study aimed to investigate the effects and the underlying mechanisms of exogenous carbon monoxide, carbon monoxide-releasing molecules II (CORM-2)-liberated CO, on suppressing platelet α-granule exocytosis in sepsis. It was shown that CORM-2 weakened α-granule membrane fusion with platelet plasma membrane and attenuated α-granule contents exocytosis in LPS-Induced platelet. Further studies revealed that CORM-2 suppressed the expression of integrin αIIbβ 3 in platelets stimulated by LPS. This was accompanied by a decrease in production and phosphorylation of PKCθ and Munc18a, SNAREs complex assembly and subsequently platelet α-granule exocytosis. Taken together, we suggested that the potential mechanism of suppressive effect of CORM-2 on LPS-induced platelet SNAREs complex assembly and α-Granule Exocytosis might involve integrin αIIbβ 3 -mediated PKCθ/ Munc18a pathway activation.

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“…3D). Expression of AGGF1 in human megakaryocytes is a novel finding, adding this angiogenic mediator to many others expressed in platelets and progenitors [18][19][20].…”

Section: Growth Factors In Megakaryocytesmentioning

confidence: 99%

“…A premature protein release from the megakaryocytes due to defective storage in a-granules might contribute, as could lower uptake to the megakaryocytes by endocytosis [27]. Cytoskeleton disorganization has been found in XLTT platelets and megakaryocytes [4] and impairs protein transport mechanisms [20].…”

Section: Growth Factors In Megakaryocytesmentioning

confidence: 99%

X‐linked thrombocytopenia with thalassemia displays bone marrow reticulin fibrosis and enhanced angiogenesis: Comparisons with primary myelofibrosis

et al. 2015

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X‐linked thrombocytopenia with thalassemia (XLTT) is caused by the mutation 216R > Q in exon 4 of the GATA1 gene. Male hemizygous patients display macrothrombocytopenia, splenomegaly, and a β‐thalassemia trait. We describe two XLTT families where three males were initially misdiagnosed as having primary myelofibrosis (PMF) and all five investigated males showed mild‐moderate bone marrow (BM) reticulin fibrosis. Comparative investigations were performed on blood samples and BM biopsies from males with XLTT, PMF patients and healthy controls. Like PMF, XLTT presented with high BM microvessel density, low GATA1 protein levels in megakaryocytes, and elevated blood CD34+ cell counts. But unlike PMF, the BM microvessel pericyte coverage was low in XLTT, and no collagen fibrosis was found. Further, as evaluated by immunohistochemistry, expressions of the growth factors VEGF, AGGF1, and CTGF were low in XLTT megakaryocytes and microvessels but high in PMF. Thus, although the reticulin fibrosis in XLTT might simulate PMF, opposing stromal and megakaryocyte features may facilitate differential diagnosis. Additional comparisons between these disorders may increase the understanding of mechanisms behind BM fibrosis in relation to pathological megakaryopoiesis. Am. J. Hematol. 90:E44–E48, 2015. © 2014 Wiley Periodicals, Inc.

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Advances in platelet granule biology

Abstract: These new observations reveal a previously unappreciated complexity to platelet granule formation and exocytosis and challenge our earlier notions of how these granules are organized within platelets and contribute to the multitude of physiological activities in which platelets function.

Cited by 65 publications

References 56 publications

Should any genetic defect affecting α‐granules in platelets be classified as gray platelet syndrome?

Should any genetic defect affecting α‐granules in platelets be classified as gray platelet syndrome?

WITHDRAWN: "Exogenous carbon monoxide suppresses LPS-induced platelet SNAREs complex assembly and Î±-granule exocytosis via integrin Î±IIbÎ²3-mediated PKCÎ¸/Munc18a pathway"

X‐linked thrombocytopenia with thalassemia displays bone marrow reticulin fibrosis and enhanced angiogenesis: Comparisons with primary myelofibrosis

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