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  • 1
    Online Resource
    Online Resource
    Human Monocytes and Neutrophils Store Transforming Growth Factor-α in a Subpopulation of Cytoplasmic Granules
    American Society of Hematology ; 1997
    In:  Blood Vol. 90, No. 3 ( 1997-08-01), p. 1255-1266
    Details
    In: Blood, American Society of Hematology, Vol. 90, No. 3 ( 1997-08-01), p. 1255-1266
    Abstract: Transforming growth factor-α (TGF-α) exerts several effects on target cells, such as neovascularization promotion and mitogenic signalling. Using immunoelectron microscopy, we show that monocytes and neutrophils, store TGF-α in cytoplasmic granules. In monocytes, TGF-α did not colocalize with components of peroxidase-positive granules or with albumin of secretory vesicles. Furthermore, no colocalization of TGF-α with components of azurophilic or specific granules or secretory vesicles was observed in neutrophils. Activated monocytes and tissue-macrophages contained much less TGF-α–positive granules, suggesting TGF-α release. Western blot analysis showed a protein of 10 kD in lysates of monocytes. TGF-α mRNA was detected in monocytoid cells from the bone marrow by in situ hybridization. This study shows for the first time that monocytes and neutrophils contain TGF-α in all stages of maturation and that TGF-α in monocytes is stored in a large population of peroxidase-negative granules suggesting a function for these granules. Monocytes and neutrophils are important effector cells in inflammatory reactions. The present finding that these cells contain TGF-α might explain complications such as fibrosis and neoplastic transformation, caused by chronic inflammation.
    Type of Medium: Online Resource
    ISSN: 1528-0020 , 0006-4971
    URL: Article
    DOI: 10.1182/blood.V90.3.1255.1255_1255_1266
    RVK:
    XA 33000
    RVK:
    XA 10000
    Language: English
    Publisher: American Society of Hematology
    Publication Date: 1997
    detail.hit.zdb_id: 1468538-3
    detail.hit.zdb_id: 80069-7
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  • 2
    Online Resource
    Online Resource
    Specific Granules of Human Eosinophils Have Lysosomal Characteristics: Presence of Lysosome-Associated Membrane Proteins and Acidification upon Cellular Activation
    Elsevier BV ; 2002
    In:  Biochemical and Biophysical Research Communications Vol. 291, No. 4 ( 2002-03), p. 844-854
    Details
    In: Biochemical and Biophysical Research Communications, Elsevier BV, Vol. 291, No. 4 ( 2002-03), p. 844-854
    Type of Medium: Online Resource
    ISSN: 0006-291X
    URL: Article
    DOI: 10.1006/bbrc.2002.6512
    RVK:
    WA 15000
    Language: English
    Publisher: Elsevier BV
    Publication Date: 2002
    detail.hit.zdb_id: 1461396-7
    SSG: 12
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  • 3
    Online Resource
    Online Resource
    The bactericidal/permeability‐increasing protein (BPI) is membrane‐associated in azurophil granules of human neutrophils, and relocation occurs upon cellular activation
    Wiley ; 2000
    In:  APMIS Vol. 108, No. 3 ( 2000-01), p. 201-208
    Details
    In: APMIS, Wiley, Vol. 108, No. 3 ( 2000-01), p. 201-208
    Abstract: Neutrophilic granulocytes contain the 55 kDa bactericidal/permeability‐increasing protein (BPI). BPI binds to lipopolysaccharides (LPS), and exerts bacteriostatic and bactericidal effects against a wide variety of Gram‐negative bacterial species. We have investigated the subcellular location of BPI in immature and mature neutrophils using cryotechnique for immunoelectron microscopy. BPI was found to colocate with myeloperoxidase (MPO), a marker for azurophil granules, and it also showed the same pattern of distribution as CD63, a transmembrane‐anchored protein. This suggests that BPI is membrane‐associated in the azurophil granules in neutrophils. Its presence in azurophil granules was further confirmed by the finding of BPI in the azurophil granules of neutrophil promyelocytes of the bone marrow. Induction of selective release of azurophilic granules by the Na‐ionophore monensin resulted in fusion of endosomes with azurophil granules, leading to the formation of large vacuoles containing MPO, CD63, and BPI. After phagocytosis of serum‐treated zymosan (STZ), BPI was detected in phagosomes, both in association with membranes as well as in the lumen, suggesting the release of BPI into activated compartments. The results show that BPI is present in azurophil granules, is probably primarily membrane‐associated, and is relocated after activation, following the same route as MPO and CD63.
    Type of Medium: Online Resource
    ISSN: 0903-4641 , 1600-0463
    URL: Article
    DOI: 10.1034/j.1600-0463.2000.d01-45.x
    RVK:
    XA 13160
    Language: English
    Publisher: Wiley
    Publication Date: 2000
    detail.hit.zdb_id: 2098213-6
    SSG: 12
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  • 4
    Online Resource
    Online Resource
    The Bactericidal/Permeability-Increasing Protein (BPI) Is Present in Specific Granules of Human Eosinophils
    American Society of Hematology ; 1998
    In:  Blood Vol. 91, No. 12 ( 1998-06-15), p. 4770-4775
    Details
    In: Blood, American Society of Hematology, Vol. 91, No. 12 ( 1998-06-15), p. 4770-4775
    Abstract: Eosinophils participate in the inflammatory response seen in allergy and parasitic infestation, but a role in host defense against bacterial infection is not settled. The bactericidal/permeability-increasing protein (BPI) has been demonstrated in neutrophils and it exerts bacteriostatic and bactericidal effects against a wide variety of Gram-negative bacterial species. Using the Western blot technique, a 55-kD band, corresponding to BPI, was detected in lysates from both neutrophils and eosinophils. The localization of BPI in immature and mature eosinophils was investigated using immunoelectron microscopy. BPI was found in immature and mature specific granules of eosinophils and was detected in phagosomes as well, indicating release of the protein from the granules into the phagosomes. Using a specific enzyme-linked immunosorbent assay, eosinophils were shown to contain 179 ng of BPI/5 × 106 eosinophils compared with 710 ng BPI/5 × 106 neutrophils. The presence of BPI in eosinophils suggests a role for these cells in host defense against Gram-negative bacterial invasion or may suggest a role for BPI against parasitic infestation.
    Type of Medium: Online Resource
    ISSN: 1528-0020 , 0006-4971
    URL: Article
    DOI: 10.1182/blood.V91.12.4770
    RVK:
    XA 33000
    RVK:
    XA 10000
    Language: English
    Publisher: American Society of Hematology
    Publication Date: 1998
    detail.hit.zdb_id: 1468538-3
    detail.hit.zdb_id: 80069-7
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  • 5
    Online Resource
    Online Resource
    Localization of Granule Proteins in Human Eosinophil Bone Marrow Progenitors
    S. Karger AG ; 1997
    In:  International Archives of Allergy and Immunology Vol. 114, No. 2 ( 1997), p. 130-138
    Details
    In: International Archives of Allergy and Immunology, S. Karger AG, Vol. 114, No. 2 ( 1997), p. 130-138
    Type of Medium: Online Resource
    ISSN: 1018-2438 , 1423-0097
    URL: Article
    DOI: 10.1159/000237657
    RVK:
    XA 49650
    Language: English
    Publisher: S. Karger AG
    Publication Date: 1997
    detail.hit.zdb_id: 1482722-0
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  • 6
    Online Resource
    Online Resource
    Eosinophil Granulocyte Interaction with Serum-Opsonized Particles: Binding and Degranulation Are Enhanced by Tumor Necrosis Factor Alpha
    S. Karger AG ; 1998
    In:  International Archives of Allergy and Immunology Vol. 115, No. 2 ( 1998), p. 121-128
    Details
    In: International Archives of Allergy and Immunology, S. Karger AG, Vol. 115, No. 2 ( 1998), p. 121-128
    Abstract: Eosinophils participate in the inflammatory response seen in allergy and helminthic infestation. Their release of granule-bound cationic proteins may play a role in these diseases. Therefore, we investigated mechanisms involved in the release of eosinophil cationic protein (ECP). Serum-opsonized zymosan was phagocytosed by eosinophils, and ECP was released into the phagosomes as judged by immunoelectron microscopy. Degranulation to the external milieu was induced by serum-opsonized, non-phagocytosable Sephadex beads (SOS), and ECP release was determined by use of an enzyme-linked immunosorbent assay. CD11b, CD18, and CD32 monoclonal antibodies inhibited degranulation, demonstrating dependence on complement receptor type 3 (CR3), and the low-affinity Fc receptor for IgG. Tumor necrosis factor-α (TNF-α) and interleukin (IL)-5 both rapidly enhanced the binding of eosinophils to serum-opsonized zymosan, and also the release of ECP upon interaction with SOS. The cytokine-induced increase in ECP release was inhibited by the phospholipase A 〈 sub 〉 2 〈 /sub 〉 (PLA 〈 sub 〉 2 〈 /sub 〉 ) inhibitor mepacrine, indicating an involvement of PLA 〈 sub 〉 2 〈 /sub 〉 in the enhanced response but not in baseline degranulation. Autocrine stimulation by the platelet-activating factor (PAF) is unlikely since the PAF receptor antagonist WEB 2086 did not inhibit the enhanced response. In conclusion, the main signals for eosinophil degranulation on serum-opsonized particles are mediated by CR3 and receptors for immunoglobulins. As for IL-5, TNF-α changes eosinophil phenotype from a resting to an activated state.
    Type of Medium: Online Resource
    ISSN: 1018-2438 , 1423-0097
    URL: Article
    DOI: 10.1159/000023891
    RVK:
    XA 49650
    Language: English
    Publisher: S. Karger AG
    Publication Date: 1998
    detail.hit.zdb_id: 1482722-0
    Location Call Number Limitation Availability
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    Online Resource
  • 7
    Online Resource
    Online Resource
    Human Monocytes and Neutrophils Store Transforming Growth Factor-α in a Subpopulation of Cytoplasmic Granules
    American Society of Hematology ; 1997
    In:  Blood Vol. 90, No. 3 ( 1997-08-01), p. 1255-1266
    Details
    In: Blood, American Society of Hematology, Vol. 90, No. 3 ( 1997-08-01), p. 1255-1266
    Abstract: Transforming growth factor-α (TGF-α) exerts several effects on target cells, such as neovascularization promotion and mitogenic signalling. Using immunoelectron microscopy, we show that monocytes and neutrophils, store TGF-α in cytoplasmic granules. In monocytes, TGF-α did not colocalize with components of peroxidase-positive granules or with albumin of secretory vesicles. Furthermore, no colocalization of TGF-α with components of azurophilic or specific granules or secretory vesicles was observed in neutrophils. Activated monocytes and tissue-macrophages contained much less TGF-α–positive granules, suggesting TGF-α release. Western blot analysis showed a protein of 10 kD in lysates of monocytes. TGF-α mRNA was detected in monocytoid cells from the bone marrow by in situ hybridization. This study shows for the first time that monocytes and neutrophils contain TGF-α in all stages of maturation and that TGF-α in monocytes is stored in a large population of peroxidase-negative granules suggesting a function for these granules. Monocytes and neutrophils are important effector cells in inflammatory reactions. The present finding that these cells contain TGF-α might explain complications such as fibrosis and neoplastic transformation, caused by chronic inflammation.
    Type of Medium: Online Resource
    ISSN: 1528-0020 , 0006-4971
    URL: Article
    DOI: 10.1182/blood.V90.3.1255
    RVK:
    XA 33000
    RVK:
    XA 10000
    Language: English
    Publisher: American Society of Hematology
    Publication Date: 1997
    detail.hit.zdb_id: 1468538-3
    detail.hit.zdb_id: 80069-7
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Online Resource
  • 8
    Online Resource
    Online Resource
    The Bactericidal/Permeability-Increasing Protein (BPI) Is Present in Specific Granules of Human Eosinophils
    American Society of Hematology ; 1998
    In:  Blood Vol. 91, No. 12 ( 1998-06-15), p. 4770-4775
    Details
    In: Blood, American Society of Hematology, Vol. 91, No. 12 ( 1998-06-15), p. 4770-4775
    Abstract: Eosinophils participate in the inflammatory response seen in allergy and parasitic infestation, but a role in host defense against bacterial infection is not settled. The bactericidal/permeability-increasing protein (BPI) has been demonstrated in neutrophils and it exerts bacteriostatic and bactericidal effects against a wide variety of Gram-negative bacterial species. Using the Western blot technique, a 55-kD band, corresponding to BPI, was detected in lysates from both neutrophils and eosinophils. The localization of BPI in immature and mature eosinophils was investigated using immunoelectron microscopy. BPI was found in immature and mature specific granules of eosinophils and was detected in phagosomes as well, indicating release of the protein from the granules into the phagosomes. Using a specific enzyme-linked immunosorbent assay, eosinophils were shown to contain 179 ng of BPI/5 × 106 eosinophils compared with 710 ng BPI/5 × 106 neutrophils. The presence of BPI in eosinophils suggests a role for these cells in host defense against Gram-negative bacterial invasion or may suggest a role for BPI against parasitic infestation.
    Type of Medium: Online Resource
    ISSN: 1528-0020 , 0006-4971
    URL: Article
    DOI: 10.1182/blood.V91.12.4770.412k33_4770_4775
    RVK:
    XA 33000
    RVK:
    XA 10000
    Language: English
    Publisher: American Society of Hematology
    Publication Date: 1998
    detail.hit.zdb_id: 1468538-3
    detail.hit.zdb_id: 80069-7
    Location Call Number Limitation Availability
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    Online Resource
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