Origin of megakaryocyte granules from Golgi vesicles

Jones, Oliver P.

doi:10.1002/ar.1091380204

Cited by 44 publications

(11 citation statements)

References 20 publications

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“…This is most easily explained on the basis of an influx of labeled cells from a group of precursors which is not recognized to belong to the megacaryocytic series ( 1,6,9,11). The figures given here for the size of this group are a lower limit, since a fraction of the cells registered in Group 2 may in fact be closer functionally to Group 3.…”

Section: Resultsmentioning

confidence: 99%

Kinetics of Megacaryocyte Proliferation.

Feinendegen

Odartchenko

Cottier

et al. 1962

Experimental Biology and Medicine

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177proteins found (approximately 3 mgjml serum) constitute a small percentage of total serum proteins. Nevertheless, they may have significant quantitative importance if, as indicated by immunoelectrophoresis, their serum protein distribution is considered.Summary. Liver antigens were demonstrated in the sera of rats with hepatic damage induced by single injections of carbon tetrachloride, chloroform, phosphorus and tannic acid, and with carbon tetrachloride cirrhosis by the Ouchterlony and immunoelectrophoresis methods, using rabbit anti-rat liver serum absorbed with normal rat serum proteins. In carbon tetrachloride poisoned rats, hepatic antigens in the sera began to rise within a few hours after injection, reached a peak at 12-24 hours, remained there for 2 days and then declined, to disappear in approximately one week. The highest titers indicated the presence of about 3 mg liver proteins per ml serum. The minimum amount of antigens detectable by the method employed was 25 pg hepatic proteins per ml serum. These liver antigens in the sera have electrophoretic mobilities of gamma, beta and alpha globulins, as shown by immunoelectrophoresis. Their influence on serum protein levels after acute liver injury is discussed. In rats with carbon tetrachloride cirrhosis, leakage of hepatic antigens into the blood was demonstrated only in the 2-3-day period following a maintenance injection, indicating that this phenomenon is related to the acute hepatic injury.We gratefully acknowledge the technical assistance of Mr. B. Oporto and Mrs. A. Eisemann de Weinlaub.

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Section: Resultsmentioning

confidence: 99%

Kinetics of Megacaryocyte Proliferation.

Feinendegen

Odartchenko

Cottier

et al. 1962

Experimental Biology and Medicine

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“…Utilization of [ 35S]sulfate by ovarian intersititial cells has not been reported previously . The func- FIGURE 13 Schwann cell surrounding a myelinated axon in the intercostal nerve of a rat killed 30 tion of these cells is the production of steroid hormones, particularly estrogens (10,41,49) . Sulfate is known to play a role in the biosynthesis and metabolism of steroids (52), although the precise role of the sulfated steroid intermediates is still uncertain (51) .…”

Section: Discussionmentioning

confidence: 99%

The Role of the Golgi Complex in Sulfate Metabolism

Young

1973

The Journal of Cell Biology

200

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This investigation was designed to determine if sulfate metabolism is the function of a particular cell organelle, or whether the site of sulfation varies, depending upon the type of cell and the class of sulfated compound . Rats and mice were injected intravenously with inorganic sulfate labeled with I'S (H 235 SO 4), and were then killed by vascular perfusion of fixative 5-30 min later . Several tissues were prepared for electron microscope autoradiography . 14 different types of specialized cells which incorporated the labeled sulfate were analyzed . In every case, the sulfate was initially detected in the smooth membranes and vesicles of the Golgi complex. Available evidence indicates that these cells were engaged in the synthesis of several different sulfated compounds, including mucopolysaccharides, glycoproteins, lipids, and steroids . These results lead to the generalization that the enzymes required for the transfer of inorganic sulfate to a variety of acceptor molecules are located in the Golgi complex .

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“…3 Serotonin causes vasoconstriction and assists in the binding of adhesive proteins to their platelet receptors. 3 Biogenesis Like a-granules, dense granules originate from the Golgi complex 9,10 and are transported to the periphery of megakaryocytes via microtubules and actin filaments, which effect proplatelet formation and elongation. Along this path, a dense granule engages with a multivesicular body (MVB), the key storage and sorting compartment involved in the biogenesis of both a-and dense granules.…”

Section: Contents and Functionmentioning

confidence: 99%

Molecular Defects that Affect Platelet Dense Granules

Gunay‐Aygun

Huizing

Gahl

2004

Semin Thromb Hemost

112

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Platelet dense granules form using mechanisms shared by melanosomes in melanocytes and by subsets of lysosomes in more generalized cells. Consequently, disorders of platelet dense granules can reveal how organelles form and move within cells. Models for the study of new vesicle formation include isolated delta-storage pool deficiency, combined alphadelta-storage pool deficiency, Hermansky-Pudlak syndrome (HPS), Chediak-Higashi syndrome, Griscelli syndrome, thrombocytopenia absent radii syndrome, and Wiskott-Aldrich syndrome. The molecular bases of dense granule deficiency are known for the seven subtypes of HPS, as well as for Chediak-Higashi syndrome, Griscelli syndrome, and Wiskott-Aldrich syndrome. The gene products involved in these disorders help elucidate the generalized process of the formation of vesicles from extant membranes such as the Golgi.

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Origin of megakaryocyte granules from Golgi vesicles

Cited by 44 publications

References 20 publications

Kinetics of Megacaryocyte Proliferation.

Kinetics of Megacaryocyte Proliferation.

The Role of the Golgi Complex in Sulfate Metabolism

Molecular Defects that Affect Platelet Dense Granules

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