Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.6.1 (sulfatase)
 3,205 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Platelets secrete lysosmal enzymes during the "platelet release reaction" early in clot formation. This study was undertaken to identify primary lysosomes of platelets and to detemine their origin in megakaryocytes. Using electron microscopy and cytochemistry, we localized two lysosomal enzymes, arylsulfatase and acid phosphatase, in megakaryocytes and platelets of normal and thrombocytopenic rats. In platelets and mature megakaryocytes, reaction product for both enzymes is confined to vesicles measuring 175-250 nm. These vesicles, which are primary lysosmes, first appear in the earliest recognizable megakaryocytes and increase in number during cellular maturation. In immature and maturing megakaryocytes, arylsulfatase and acid phosphatase can also be demonstrated in an organell similar to GERL (Golgi-endoplasmic reticulumlysosome), i.e., single smooth-surfaced cisternal with associated vesicles near the stacked Golgi cisternae. Scant reaction product for acid phosphatase is also sometimes seen in Golgi cisternae and endoplasmic reticulum. No reaction product was found in alpha-granules at any stage of megakaryocyte maturation, nor in alpha- or serotonin granules of platelets. Thus, our findings indicate that the primay lysosomes of megakaryocytes and platelets are small vesicles derived from GERL early in megakaryocyte differentiation. They can be indentified only after cytochemical staining and are distinct from both alpha- and serotonin granules.
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PMID:Cytochemical localization of lysosomal enzymes in rat megakaryocytes and platelets. 120 88

A previous investigation detailed the pathology of platelets in a family with the X-linked GATA-1 G208S mutation causing dyserythropoiesis and megathrombocytopenia. The present study has used ultrastructural immunocytochemistry, cytochemistry, and tannic acid staining to answer questions raised in the original investigation. Earlier studies, as well as ours, had shown that GATA-1 megathrombocytes are hypogranular, but did not definitively determine which organelles are decreased. Cytochemical localization of aryl sulfatase revealed that lysosomes were present in normal numbers, and the whole mount technique showed a normal frequency of dense bodies rich in arlenine nucleotides and serotonin. Thus alpha granules were the only organelles deficient in GATA-1 platelets. Tannic acid staining confirmed that the membranes wrapped around each other to form tubular inclusions come from elements of the dense tubular system. The unique tubular membrane inclusions in GATA-1 megathrombocytes, thought originally to derive from endoplasmic reticulum in the parent cell, were shown to be in direct continuity with elements of the surface connected open canalicular system (OCS), and to drive from the demarcation membrane system (DMS) of the megakaryocyte. Platelets in platelets and platelets in platelets in platelets were independent cells, and not derived by cytoplasmic sequestration in the enclosing macrothrombocytes. Fully spread GATA-1 platelets incubated with fibrinogen coated gold (Fgn/Au) particles before or after fixation bound as many Fgn/Au particles as normal spread platelets and moved the Fgn/Au- GPIIb/IIIa complexes from peripheral margins to cell centers and into channels of the OCS as efficiently. Exposure of spread normal platelets to bovine vWF resulted in coverage of the surface from edge to edge with multimers detected by anti-vWF antibody and protein A gold. Spread GATA-1 platelets bound very few vWF multimers, which were much smaller in size than those on normal spread cells, but were able to move then to cell centers. These findings support the concept that GATA-1 platelets are macrothrombocytes because they are not able to detach normally from each other during separation from megakaryocyte proplatelets. The marked decrease in the number and abnormal distribution of GPIb/IX receptors may play a role in GATA-1 megathrombocyte formation.
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PMID:Platelet pathology in sex-linked GATA-1 dyserythropoietic macrothrombocytopenia II. Cytochemistry. 1776 53