Human megakaryocytes express clusterin and package it without apolipoprotein A-1 into alpha-granules
| Autor: | André-Pierre Sapino, Dieter E. Jenne, Hans Morgenstern, Jürg Tschopp, Silvie Hertig, Klaus T. Preissner, Lars E. French |
|---|---|
| Rok vydání: | 1993 |
| Předmět: |
chemistry.chemical_classification
Apolipoprotein B biology Clusterin Immunology Cell Biology Hematology Immunogold labelling Biochemistry Molecular biology Lipoprotein particle eye diseases medicine.anatomical_structure Thrombin Megakaryocyte chemistry biology.protein medicine Platelet sense organs Glycoprotein medicine.drug |
| Zdroj: | Blood. 82:118-125 |
| ISSN: | 1528-0020 0006-4971 |
| DOI: | 10.1182/blood.v82.1.118.bloodjournal821118 |
| Popis: | Clusterin, a 70-Kd disulfide-linked two-chain plasma glycoprotein circulates in blood as a high-density lipoprotein particle and is highly induced after tissue injury and tissue remodeling. In this study, peripheral blood leukocytes were assayed for clusterin expression. The protein was predominantly detectable in human platelets by immune cytochemistry. The content of clusterin was determined and amounts to 2.5 +/- 1.3 micrograms/10(9) platelets, thus representing about 2% of the blood pool. Clusterin purified from human platelets had the same molecular weight as plasma clusterin under nonreducing conditions and was composed of two disulfide-linked nonidentical subunits of the same size. Both preparations were sensitive to reduction yielding the two subunits of 35 Kd. In contrast to plasma clusterin, the platelet form was not complexed to apolipoprotein A-I. By immunogold labeling, alpha-granule localization of clusterin was observed. Complete release of platelet clusterin occurred at optimal doses of A23187, phorbol myristate acetate (PMA), and thrombin. Because clusterin mRNA was detected by hybridization in situ in bone marrow- derived megakaryocytes, platelet clusterin is most likely produced and packaged into alpha-granules during megakaryocyte development. |
| Databáze: | OpenAIRE |
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