|
|
 Previous Article | Table of Contents | Next Article 
Expression of Bomapin, a Novel Human Serpin, in Normal/Malignant
Hematopoiesis and in the Monocytic Cell Lines THP-1 and AML-193
Matthias Riewald,
Trinette Chuang,
Andreas Neubauer,
Hanno Riess, and
Raymond R. Schleef
From the Department of Vascular Biology, The Scripps Research
Institute, La Jolla, CA and Virchow Klinikum, Department of Hematology
and Oncology, Humboldt Universität, Berlin, Germany.
Our group recently cloned the cDNA-encoding bomapin, a member of the
serine protease inhibitor (serpin) superfamily, from a human bone
marrow cDNA library (J Biol Chem 270:2675, 1995). To
understand its expression within the hematopoietic compartment, RNA
extracted from bone marrow or peripheral blood from normal donors and
patients with leukemia was reverse transcribed and analyzed by
polymerase chain reaction (PCR). Bomapin PCR products were readily
detected in normal bone marrow, which was designated as a medium mRNA
level. In peripheral blood, bomapin expression was low or undetectable
in normal donors (n = 6) and patients with chronic lymphocytic
leukemia (n = 6). Blood from patients with chronic myeloid leukemia
(n = 6), chronic myelomonocytic leukemia (n = 6), acute myeloid
leukemia (n = 5), and acute lymphocytic leukemia (n = 5) exhibited
low to medium levels of bomapin expression. Furthermore, a high level
of bomapin expression was detected in one individual with acute
monocytic leukemia. These data suggest that bomapin expression may be
elevated in hematopoietic cells of monocytic lineage. Therefore, we
analyzed the expression of bomapin within cell lines that exhibited
characteristics of the monocytic lineage. Bomapin PCR products were
detected in the monocytic THP-1 and AML-193 cell lines but not in CRL
7607, CRL 7541, KG-1, or K562 cells. Induction of bomapin transcripts
was not detected in the latter series of cell lines following a 24-hour
treatment with phorbol myristate acetate (PMA, 10 8
mol/L) or tumor necrosis factor- (TNF-, 30 U/mL), whereas
treatment of THP-1 or AML-193 cells with these agents reduced the
intensity of the bomapin PCR products. Northern blotting confirmed
these results and showed that the expression of bomapin in THP-1 cells was downregulated over a 4-day period by PMA and, to a lesser extent,
TNF-. Immunoblotting was used to show the presence of a 40-kD
protein in THP-1 cytosol preparations. Bomapin antigen levels were
correspondingly reduced after treatment with PMA. Because PMA and
TNF- induce monocytic differentiation in THP-1 and AML-193 cells,
these data increase the possibility that bomapin may play a role in the
regulation of protease activities specifically in early stages of
cellular differentiation.
Blood, Vol. 91 No. 4 (February 15), 1998:
pp. 1256-1262
© 1998 by The American Society of Hematology.
 CiteULike  Connotea  Del.icio.us  Digg  Reddit  Technorati What's this?
This article has been cited by other articles:
|
|
|
|
 
M. Bots and J. P. Medema
Serpins in T cell immunity
J. Leukoc. Biol.,
November 1, 2008;
84(5):
1238 - 1247.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
M. C. Strik, B. A. Bladergroen, D. Wouters, W. Kisiel, J. H. Hooijberg, A. R. Verlaan, P. L. Hordijk, P. Schneider, C. E. Hack, and J. A. Kummer
Distribution of the Human Intracellular Serpin Protease Inhibitor 8 in Human Tissues
J. Histochem. Cytochem.,
November 1, 2002;
50(11):
1443 - 1454.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
J. E. Chipuk, L. V. Stewart, A. Ranieri, K. Song, and D. Danielpour
Identification and Characterization of A Novel Rat Ov-Serpin Family Member, Trespin
J. Biol. Chem.,
July 12, 2002;
277(29):
26412 - 26421.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
Z. Xia, R. R. Salzler, D. P. Kunz, M. R. Baer, L. Kazim, H. Baumann, and M. Wetzler
A Novel Serine-dependent Proteolytic Activity Is Responsible for Truncated Signal Transducer and Activator of Transcription Proteins in Acute Myeloid Leukemia Blasts
Cancer Res.,
February 1, 2001;
61(4):
1747 - 1753.
[Abstract]
[Full Text]
|
|
|
|
|
|
|
T. L. Chuang and R. R. Schleef
Identification of a Nuclear Targeting Domain in the Insertion between Helices C and D in Protease Inhibitor-10
J. Biol. Chem.,
April 16, 1999;
274(16):
11194 - 11198.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
R. R. Schleef and T. L. Chuang
Protease Inhibitor 10 Inhibits Tumor Necrosis Factor alpha -induced Cell Death. EVIDENCE FOR THE FORMATION OF INTRACELLULAR HIGH Mr PROTEASE INHIBITOR 10-CONTAINING COMPLEXES
J. Biol. Chem.,
August 18, 2000;
275(34):
26385 - 26389.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
