Ribonucleases and host defense: identification, localization and gene expression in adherent monocytes in vitro
(1997) In Biochimica et Biophysica Acta 1358(3). p.60-255- Abstract
- Several ribonucleases of the RNase A family function as antibacterial, anti-parasitic and anti-viral agents. In this work, we have shown that mRNAs encoding five of the six known human ribonucleases of the RNase A family are expressed in cultured human monocytes, and that ribonucleases are released by adherent monocytes in culture. Using a polyclonal antiserum prepared against recombinant protein, we have detected one of these ribonucleases, RNase 4, in lysates of normal human peripheral blood monocytes, but not granulocytes or lymphocytes, by Western blotting. Subcellular localization by immunoelectron microscopy demonstrated the presence of RNase 4 in the cytoplasmic granules of isolated monocytes. Interestingly, mRNA encoding RNase 4... (More)
- Several ribonucleases of the RNase A family function as antibacterial, anti-parasitic and anti-viral agents. In this work, we have shown that mRNAs encoding five of the six known human ribonucleases of the RNase A family are expressed in cultured human monocytes, and that ribonucleases are released by adherent monocytes in culture. Using a polyclonal antiserum prepared against recombinant protein, we have detected one of these ribonucleases, RNase 4, in lysates of normal human peripheral blood monocytes, but not granulocytes or lymphocytes, by Western blotting. Subcellular localization by immunoelectron microscopy demonstrated the presence of RNase 4 in the cytoplasmic granules of isolated monocytes. Interestingly, mRNA encoding RNase 4 could not be detected in freshly isolated monocytes, emerging only after 16 h in culture, suggesting the possibility of de novo protein synthesis in association with monocyte differentiation. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1296408
- author
- Egesten, Arne LU ; Dyer, K D ; Batten, D ; Domachowske, J B and Rosenberg, H F
- organization
- publishing date
- 1997
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Biochimica et Biophysica Acta
- volume
- 1358
- issue
- 3
- pages
- 60 - 255
- publisher
- Elsevier
- external identifiers
-
- scopus:0030829121
- language
- English
- LU publication?
- yes
- id
- b06f1b5f-d8dd-48be-a7c1-c28515128d71 (old id 1296408)
- alternative location
- http://www.sciencedirect.com/science/article/pii/S0167488997000815
- http://www.ncbi.nlm.nih.gov/pubmed/9366257
- date added to LUP
- 2016-04-04 13:37:40
- date last changed
- 2022-01-30 00:40:29
@article{b06f1b5f-d8dd-48be-a7c1-c28515128d71,
abstract = {{Several ribonucleases of the RNase A family function as antibacterial, anti-parasitic and anti-viral agents. In this work, we have shown that mRNAs encoding five of the six known human ribonucleases of the RNase A family are expressed in cultured human monocytes, and that ribonucleases are released by adherent monocytes in culture. Using a polyclonal antiserum prepared against recombinant protein, we have detected one of these ribonucleases, RNase 4, in lysates of normal human peripheral blood monocytes, but not granulocytes or lymphocytes, by Western blotting. Subcellular localization by immunoelectron microscopy demonstrated the presence of RNase 4 in the cytoplasmic granules of isolated monocytes. Interestingly, mRNA encoding RNase 4 could not be detected in freshly isolated monocytes, emerging only after 16 h in culture, suggesting the possibility of de novo protein synthesis in association with monocyte differentiation.}},
author = {{Egesten, Arne and Dyer, K D and Batten, D and Domachowske, J B and Rosenberg, H F}},
language = {{eng}},
number = {{3}},
pages = {{60--255}},
publisher = {{Elsevier}},
series = {{Biochimica et Biophysica Acta}},
title = {{Ribonucleases and host defense: identification, localization and gene expression in adherent monocytes in vitro}},
url = {{http://www.sciencedirect.com/science/article/pii/S0167488997000815}},
volume = {{1358}},
year = {{1997}},
}