|
|
 Previous Article | Table of Contents | Next Article 
Blood, Vol. 92 No. 4 (August 15), 1998:
pp. 1199-1205
Multiple Forms of the SH2-Containing Inositol Phosphatase,
SHIP, Are Generated by C-Terminal Truncation
Jacqueline E. Damen,
Ling Liu,
Mark D. Ware,
Marina Ermolaeva,
Philip W. Majerus, and
Gerald Krystal
From the Terry Fox Laboratory, B.C. Cancer Agency, Vancouver, British
Columbia, Canada; and Washington University School of Medicine, St
Louis, MO.
The SH2-containing inositol phosphatase, SHIP, often
appears as multiple bands in anti-SHIP immunoblots. To characterize
these bands, antisera were generated against the N-terminal (anti-N), mid-region (anti-M), and C-terminal (anti-C) portions of SHIP. Immunoprecipitation and immunoblotting studies showed that 145-, 135-, 125-, and 110-kD bands were detected in lysates from the murine
hematopoietic cell line, DA-ER, with either anti-N or anti-M antisera,
whereas only the 145- and 135-kD bands were recognized by the anti-C
antiserum. This finding suggested that the smaller proteins might be
C-terminal truncations of the full-length SHIP. To confirm this and
determine if these proteins arose through alternate splicing or
posttranslational cleavage, a 5 -hemagglutin (HA)-tagged
full-length SHIP cDNA was expressed in these cells. We observed, via
Western analysis with anti-HA antibodies, the same 4 bands with either
anti-N or anti-M and only the 145- and 135-kD bands with anti-C
immunoprecipitation. After interleukin-3 stimulation of
HA-SHIP-expressing DA-ER cells, only the 145-kD form coprecipitated
with Shc, raising the possibility that different forms of SHIP may have
distinct intracellular sites. This was confirmed by subcellular
fractionation, which showed that only the 110-kD form is present in the
cytoskeleton of DA-ER cells. This 110-kD form possesses the same
PIP3 5-ptase activity as the 145-kD form and can be
generated from the latter in vitro by digestion with calpain. It is
therefore possible that the different forms of SHIP are generated in
vivo by calpain-mediated C-terminal truncations and perform distinct
functions within hematopoietic cells.
© 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:
|
|
|
|
 
S. J. Harris, R. V. Parry, J. Westwick, and S. G. Ward
Phosphoinositide Lipid Phosphatases: Natural Regulators of Phosphoinositide 3-Kinase Signaling in T Lymphocytes
J. Biol. Chem.,
February 1, 2008;
283(5):
2465 - 2469.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
C. van 't Veer, P. S. van den Pangaart, M. A. D. van Zoelen, M. de Kruif, R. S. Birjmohun, E. S. Stroes, A. F. de Vos, and T. van der Poll
Induction of IRAK-M Is Associated with Lipopolysaccharide Tolerance in a Human Endotoxemia Model
J. Immunol.,
November 15, 2007;
179(10):
7110 - 7120.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
K. Gimborn, E. Lessmann, S. Kuppig, G. Krystal, and M. Huber
SHIP Down-Regulates Fc{epsilon}R1-Induced Degranulation at Supraoptimal IgE or Antigen Levels
J. Immunol.,
January 1, 2005;
174(1):
507 - 516.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
Y. Wang, R. J. Keogh, M. G. Hunter, C. A. Mitchell, R. S. Frey, K. Javaid, A. B. Malik, S. Schurmans, S. Tridandapani, and C. B. Marsh
SHIP2 Is Recruited to the Cell Membrane upon Macrophage Colony-Stimulating Factor (M-CSF) Stimulation and Regulates M-CSF-Induced Signaling
J. Immunol.,
December 1, 2004;
173(11):
6820 - 6830.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
A. S. J. Marshall, J. A. Willment, H.-H. Lin, D. L. Williams, S. Gordon, and G. D. Brown
Identification and Characterization of a Novel Human Myeloid Inhibitory C-type Lectin-like Receptor (MICL) That Is Predominantly Expressed on Granulocytes and Monocytes
J. Biol. Chem.,
April 9, 2004;
279(15):
14792 - 14802.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
C. P. Baran, S. Tridandapani, C. D. Helgason, R. K. Humphries, G. Krystal, and C. B. Marsh
The Inositol 5'-Phosphatase SHIP-1 and the Src Kinase Lyn Negatively Regulate Macrophage Colony-stimulating Factor-induced Akt Activity
J. Biol. Chem.,
October 3, 2003;
278(40):
38628 - 38636.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
R. W. Freeburn, K. L. Wright, S. J. Burgess, E. Astoul, D. A. Cantrell, and S. G. Ward
Evidence That SHIP-1 Contributes to Phosphatidylinositol 3,4,5-Trisphosphate Metabolism in T Lymphocytes and Can Regulate Novel Phosphoinositide 3-Kinase Effectors
J. Immunol.,
November 15, 2002;
169(10):
5441 - 5450.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
M. Leitges, K. Gimborn, W. Elis, J. Kalesnikoff, M. R. Hughes, G. Krystal, and M. Huber
Protein Kinase C-{delta} Is a Negative Regulator of Antigen-Induced Mast Cell Degranulation
Mol. Cell. Biol.,
June 15, 2002;
22(12):
3970 - 3980.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
Z. Tu, J. M. Ninos, Z. Ma, J.-W. Wang, M. P. Lemos, C. Desponts, T. Ghansah, J. M. Howson, and W. G. Kerr
Embryonic and hematopoietic stem cells express a novel SH2-containing inositol 5'-phosphatase isoform that partners with the Grb2 adapter protein
Blood,
October 1, 2001;
98(7):
2028 - 2038.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
J. E. Damen, M. D. Ware, J. Kalesnikoff, M. R. Hughes, and G. Krystal
SHIP's C-terminus is essential for its hydrolysis of PIP3 and inhibition of mast cell degranulation
Blood,
March 1, 2001;
97(5):
1343 - 1351.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
D. C. Fong, A. Brauweiler, S. A. Minskoff, P. Bruhns, I. Tamir, I. Mellman, M. Daeron, and J. C. Cambier
Mutational Analysis Reveals Multiple Distinct Sites Within Fc{gamma} Receptor IIB That Function in Inhibitory Signaling
J. Immunol.,
October 15, 2000;
165(8):
4453 - 4462.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
M. J. Aman, S. F. Walk, M. E. March, H.-P. Su, D. J. Carver, and K. S. Ravichandran
Essential Role for the C-Terminal Noncatalytic Region of SHIP in Fcgamma RIIB1-Mediated Inhibitory Signaling
Mol. Cell. Biol.,
May 15, 2000;
20(10):
3576 - 3589.
[Abstract]
[Full Text]
|
|
|
|
|
|
|
L. R. Rohrschneider, J. F. Fuller, I. Wolf, Y. Liu, and D. M. Lucas
Structure, function, and biology of SHIP proteins
Genes & Dev.,
March 1, 2000;
14(5):
505 - 520.
[Full Text]
|
|
|
|
|
|
|
C. D. Helgason, C. P. Kalberer, J. E. Damen, S. M. Chappel, N. Pineault, G. Krystal, and R. K. Humphries
A Dual Role for Src Homology 2 Domain-containing Inositol-5-Phosphatase (SHIP) in Immunity: Aberrant Development and Enhanced Function of B Lymphocytes in SHIP-/- Mice
J. Exp. Med.,
February 28, 2000;
191(5):
781 - 794.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
M. Sattler, S. Verma, C. H. Byrne, G. Shrikhande, T. Winkler, P. A. Algate, L. R. Rohrschneider, and J. D. Griffin
BCR/ABL Directly Inhibits Expression of SHIP, an SH2-Containing Polyinositol-5-Phosphatase Involved in the Regulation of Hematopoiesis
Mol. Cell. Biol.,
November 1, 1999;
19(11):
7473 - 7480.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
D. M. Lucas and L. R. Rohrschneider
A Novel Spliced Form of SH2-Containing Inositol Phosphatase Is Expressed During Myeloid Development
Blood,
March 15, 1999;
93(6):
1922 - 1933.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
M. Huber, C. D. Helgason, J. E. Damen, L. Liu, R. K. Humphries, and G. Krystal
The src homology 2-containing inositol phosphatase (SHIP) is the gatekeeper of mast cell degranulation
PNAS,
September 15, 1998;
95(19):
11330 - 11335.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
M. E. March, D. M. Lucas, M. J. Aman, and K. S. Ravichandran
p135 Src Homology 2 Domain-containing Inositol 5'-Phosphatase (SHIPbeta ) Isoform Can Substitute for p145 SHIP in Fcgamma RIIB1-mediated Inhibitory Signaling in B Cells
J. Biol. Chem.,
September 22, 2000;
275(39):
29960 - 29967.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
D. Saint-Dic, S. C. Chang, G. S. Taylor, M. M. Provot, and T. S. Ross
Regulation of the Src Homology 2-containing Inositol 5-Phosphatase SHIP1 in HIP1/PDGFbeta R-transformed Cells
J. Biol. Chem.,
June 8, 2001;
276(24):
21192 - 21198.
[Abstract]
[Full Text]
[PDF]
|
|
|
| |
