Identification of the major tyrosine phosphorylated protein of capacitated hamster spermatozoa as a homologue of mammalian sperm a kinase anchoring protein

2002 ◽  
Vol 61 (2) ◽  
pp. 258-270 ◽  
Author(s):  
Kula Nand Jha ◽  
S. Shivaji
Keyword(s):  
Phosphorylated Protein ◽  
Mammalian Sperm ◽  
Anchoring Protein ◽  
Tyrosine Phosphorylated Protein

scholarly journals pp75: A novel tyrosine-phosphorylated protein that heralds differentiation of HL-60 cells

1991 ◽  
Vol 266 (18) ◽  
pp. 11890-11895
Author(s):  
I. Bushkin ◽  
J. Roth ◽  
D. Heffetz ◽  
Y. Zick
Keyword(s):  
Phosphorylated Protein ◽  
Tyrosine Phosphorylated Protein

Chronic stress affects tyrosine phosphorylated protein expression and secretion of male rat epididymis

Andrologia ◽  
2021 ◽  
Author(s):  
Supatcharee Arun ◽  
Arada Chaiyamoon ◽  
Natthapol Lapyuneyong ◽  
Sudtida Bunsueb ◽  
Alexander Tsang‐Hsien Wu ◽  
...  
Keyword(s):  
Protein Expression ◽  
Chronic Stress ◽  
Male Rat ◽  
Phosphorylated Protein ◽  
Rat Epididymis ◽  
Tyrosine Phosphorylated Protein

scholarly journals Erythropoietin induces the association of phosphatidylinositol 3'-kinase with a tyrosine-phosphorylated protein complex containing the erythropoietin receptor

1993 ◽  
Vol 216 (3) ◽  
pp. 821-828 ◽  
Author(s):  
Patrick MAYEUX ◽  
Isabelle DUSANTER-FOURT ◽  
Odile MULLER ◽  
Philippe MAUDUIT ◽  
Michele SABBAH ◽  
...  
Keyword(s):  
Protein Complex ◽  
Erythropoietin Receptor ◽  
Phosphatidylinositol 3 Kinase ◽  
Phosphorylated Protein ◽  
Tyrosine Phosphorylated Protein ◽  
Phosphatidylinositol 3

Crkl is constitutively tyrosine phosphorylated in platelets from chronic myelogenous leukemia patients and inducibly phosphorylated in normal platelets stimulated by thrombopoietin

Blood ◽  
1996 ◽  
Vol 88 (11) ◽  
pp. 4304-4313 ◽  
Author(s):  
A Oda ◽  
Y Miyakawa ◽  
BJ Druker ◽  
A Ishida ◽  
K Ozaki ◽  
...  
Keyword(s):  
Platelet Aggregation ◽  
Tyrosine Phosphorylation ◽  
Molecular Mechanisms ◽  
Genetically Engineered ◽  
Myelogenous Leukemia ◽  
Insoluble Residue ◽  
Consistent Difference ◽  
Clot Retraction ◽  
Phosphorylated Protein ◽  
Tyrosine Phosphorylated Protein

Abstract Platelet functions such as aggregation and clot retraction are often abnormal in chronic mylogenous leukemia (CML) patients. However, the molecular mechanisms of these altered functions are unknown. As expression of the p210bcr-abl oncogene product, a constitutively active tyrosine kinase, is known to have an essential role in the pathogenesis of CML and tyrosine phosphorylation is intimately involved in various aspects of platelet activation, we examined the pattern of protein tyrosine phosphorylation in platelets from 15 CML patients by immunoblotting with a monoclonal antiphosphotyrosine antibody (4G10). Before and after stimulation with thrombin, the only consistent difference between normal and CML platelets was the presence of a tyrosine phosphorylated protein with a relative molecular weight of 39 kD. This tyrosine phosphorylated protein was identified as crid, an SH2, SH3 containing adapter protein. Thus, as previously demonstrated for neutrophils from CML patients, tyrosine phosphorylation of p39crkl persists in mature platelets. No tyrosine phosphorylation of crid was detected following stimulation with thrombin in normal platelets. However, crkl became incorporated into the Triton X-100 insoluble residue following thrombin stimulation in a manner dependent on platelet aggregation. Further, we found that crkl is an endogenous substrate for calpain, a protease that may be involved in postaggregation signaling processes. This suggests that crkl may be involved in the reorganization of the cytoskeleton during normal platelet aggregation and its tyrosine phosphorylation in CML platelets may contribute to the abnormal platelet function in CML patients. Finally, we found that thrombopoietin induces tyrosine phosphorylation of crk1 in normal platelets and FDCP cells genetically engineered to express human c-Mpl. This suggests that crk1 can be phosphorylated by a kinase other than p210bcr-abl and that crk1 may have a role in signaling by thrombopoietin.

Localization of a 215-kDa tyrosine-phosphorylated protein that cross-reacts with tensin antibodies

1992 ◽  
Vol 203 (1) ◽  
pp. 39-46 ◽  
Author(s):  
Susanne M. Bockholt ◽  
Carol A. Otey ◽  
John R. Glenney ◽  
Keith Burridge
Keyword(s):  
Phosphorylated Protein ◽  
Tyrosine Phosphorylated Protein

An avian cDNA encoding a tyrosine-phosphorylated protein with PDZ, coiled-coil, and SAM domains

Gene ◽  
1998 ◽  
Vol 219 (1-2) ◽  
pp. 111-123 ◽  
Author(s):  
Kwang Sun Suh ◽  
Yuan-Tsang Ting ◽  
John G. Burr
Keyword(s):  
Coiled Coil ◽  
Phosphorylated Protein ◽  
Tyrosine Phosphorylated Protein

scholarly journals Erythropoietin stimulates the tyrosine phosphorylation of Shc and its association with Grb2 and a 145-Kd tyrosine phosphorylated protein

Blood ◽  
1993 ◽  
Vol 82 (8) ◽  
pp. 2296-2303 ◽  
Author(s):  
JE Damen ◽  
L Liu ◽  
RL Cutler ◽  
G Krystal
Keyword(s):  
Growth Factor ◽  
Tyrosine Kinase ◽  
Tyrosine Phosphorylation ◽  
Consensus Sequence ◽  
Erythropoietin Receptor ◽  
Phosphorylated Protein ◽  
Molecular Masses ◽  
Epidermal Growth ◽  
Tyrosine Phosphorylated Protein

Although the erythropoietin receptor (EpR) lacks a tyrosine kinase consensus sequence within its proline-rich intracellular domain, addition of its ligand to Ep-responsive cells stimulates the rapid and transient tyrosine phosphorylation of a number of cellular proteins. The characterization of these phosphorylatable substrates, which include 5 major phosphoproteins with molecular masses of approximately 145, 130, 97, 72, and 56 Kd is an essential step in understanding the signal transduction pathways used by Ep. Recently, we and others have shown that the major 72-Kd tyrosine phosphorylated protein is the EpR itself. We now report, using both murine DA-3 and human MO7E cell lines engineered to express high levels of biologically responsive EpRs (and designated DA-ER and MO7-ER, respectively), that the major 56-Kd tyrosine phosphorylated protein is the recently identified SH2- containing protein, p52shc. Interestingly, in Ep-stimulated cells, anti- Shc antibodies coprecipitate the major 145-Kd tyrosine phosphorylated protein in both DA-ER and MO7-ER cells. Tyrosine phosphorylation of both proteins is detectable within 30 seconds of incubation with Ep at 37 degrees C, reaches a maximum between 2 and 5 minutes, and declines by 30 minutes. In addition, tyrosine phosphorylated Shc appears capable of associating with the activated EpR, but this could only be shown in MO7-ER cells. Lastly, as has been shown previously with the tyrosine kinase containing receptors for epidermal growth factor, platelet derived growth factor, and insulin, activation of the EpR leads to the association of p52shc with the 25-Kd polypeptide, Grb2. Taken together, our data suggest that the previously reported increases in rasGTP observed with Ep result, in part, from the tyrosine phosphorylation of Shc and its association with Grb2 and/or a tyrosine phosphorylated 145- Kd protein.

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