Tyrosine phosphorylation of an interleukin 2 receptor-like protein in cells transformed by human T cell leukemia virus type I.

Ogawa, Ryoichi; Sugamura, Kazuo; Watanabe, Y.

doi:10.1084/jem.165.4.959

Cited by 8 publications

(3 citation statements)

References 22 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Wealso analyzed ecto-kinase activity in several other cell lines, such as HeLa cell and an HTLV-transformed human T cell line, TL-Su. They have been reported to possess EGF receptor or Ptyr-containing proteins on the cell surface (15,20). The ecto-kinase activity in these cells was weak, and practically no EGFreceptor or Ptyr-containing proteins were detected by immunoprecipitation with anti-EGF receptor-or anti-Ptyr monoclonal antibodies (unpublished result).…”

Section: Resultsmentioning

confidence: 99%

Evoidence that the Tyrosine Kinase Domain of a Small Fraction of Epidermal Growth Factor Receptor Molecules is Exposed on the Outer Surface of A431 Cells.

Ihara

Maeda-Takekoshi

Takekoshi

et al. 1991

Cell Struct. Funct.

View full text Add to dashboard Cite

ABSTRACT. Intact A431 cells were labeled with [f-32P]ATP. The major phosphorylation product of the ectokinase activity of A431 cells had the molecular mass of 170 kd and was identified as EGF receptor by specific immunoprecipitation. This phosphorylation was not stimulated by EGFadded to the reaction buffer, but replacement of MgCl2 by MnChin the buffer remarkably stimulated phosphorylation. An exogenous protein substrate, a-casein, was also phosphorylated by intact A431 cells. The analyses for phospho-amino acids of both EGF receptor and a-casein revealed that phosphorylation occurred mainly at phosphotyrosine residues. Tryptic phospho-peptides of the EGF receptor of intact A431 cells labeled with [f-32P]ATP were fractionated by HPLC. The elution patterns were essentially the same as that of the autophosphorylated EGFreceptor, indicating that the phosphorylation sites of EGFreceptor labeled in vivo with [f-32P]ATP are located in three tyrosine residues in the carboxyl terminus. These results indicate that the carboxyl-terminal tyrosine kinase domain of a small fraction of the EGFreceptor molecules of an A431cell is exposed on the outer surface of the cells.Since the discovery of phosphotyrosine in Polioma virus T-antigen, many regulatory proteins have been found to have tyrosine kinase activity. Most of tyrosine kinases found to date are classified into two categories: (i ) oncogene products of several distinct groups of retroviruses like pp60v src, and (ii) receptors for growth factors like the epidermal growth factor (EGF) receptor (6), the platelet-derived growth factor receptor (5), and the insulin receptor (8, 9). The src-type tyrosine kinases are located on the inner side of the plasma membrane, but receptor-type tyrosine kinases contain two functional domainslinked by a transmembraneregion. The extracellular domain possesses a ligand-binding site, and the intracellular portion includes a tyrosine kinase domain at the carboxyl terminus. Protein-kinase activity has also been demonstrated on the external surface of intact cells of a variety of cell lines (4). In HeLa cells, such a surface kinase (ecto-kinase) was detected, but it phosphorylates its substrates in serine and threoninf residues (10, ll). These findings indicate that protein-

show abstract

Section: Resultsmentioning

confidence: 99%

Evoidence that the Tyrosine Kinase Domain of a Small Fraction of Epidermal Growth Factor Receptor Molecules is Exposed on the Outer Surface of A431 Cells.

Ihara

Maeda-Takekoshi

Takekoshi

et al. 1991

Cell Struct. Funct.

View full text Add to dashboard Cite

show abstract

“…In these cases, the cytoplasmic portion of the receptor molecules has a tyrosine kinase domain, and their tyrosine phosphorylation, which is associated with cell growth, was directed by the receptors themselves . We have previously detected at least three classes of phosphotyrosine proteins with molecular masses of 70, 64, and 45 kD that were detectable with antiphosphotyrosine antibody and anti-IL-2Rp55 mAb, suggesting that these phosphoproteins could associate with IL-2Rp55, although the relationship between the proteins and IL-2Rp75 has not been clarified yet (10) . A recent report using antiphosphotyrosine antibody further suggested that IL-2 induces tyrosine phosphorylation of some cellular proteins ; however, whether they include IL-2R components is unknown (11) .…”

Section: Discussionmentioning

confidence: 99%

Interleukin 2 (IL-2)-induced tyrosine phosphorylation of IL-2 receptor p75.

Asao

Takeshita

Nakamura

et al. 1990

The Journal of Experimental Medicine

Self Cite

View full text Add to dashboard Cite

Expansion ofT lymphocytes after exposure to antigens results from clonal growth of the T cells specific for the antigens . Proliferation of these T cells is initiated by the interaction of IL-2 and its receptor (IL-2R), which are transiently secreted as a growth factor lymphokine and expressed on the cell surface as an acceptor of the growth factor, respectively. There exist at least two classes of IL-2R, which differ in their affinity to IL-2. The high affinity receptor is responsible for conferring signals mediating various functions in T, B, and non-T non-B cells such as internalization of IL-2R, activation of gene expression and culminating in cell growth (reviewed in reference 1) . The chemical crosslinking analysis with 125 1-labeled IL-2 revealed that the high affinity IL-2R is a complex-of at least two distinct subunits, p55 and p75 (2-6) . The p55 molecule alone having failed to mediate growth signals (7, 8), much attention focuses on the structure and function of p75 that is thought to be involved in transducing signals .Several of the growth factor receptors are known to possess tyrosine kinase domains, and the tyrosine phosphorylation of receptor molecules has been considered to be involved in the pathway of growth signals as one of the earliest detectable responses to ligand bindings (reviewed in reference 9) . We previously detected the phosphotyrosine proteins in the immunocomplex purified with anti-IL-2Rp55 (10), and a recent report also demonstrated IL-2-induced tyrosine phosphorylation of several proteins with antiphosphotyrosine antibody (11), although the molecular nature of these phosphotyrosine proteins has not been clarified . We have recently established two independent mAbs specific for human IL-2Rp75, which enabled us to characterize the IL-2Rp75 molecule (12, 13) . The present study uses one of these mAbs to demonstrate the IL-2-induced tyrosine phosphorylation of IL-2Rp75 and association of IL-2Rp75 with tyrosine kinase activity.

show abstract

“…Se puede manifestar de tres formas diferentes: una forma asintomática aleucémica (AL), caracterizada por un número normal de linfocitos B en la circulación sanguínea; una forma de linfocitosis permanente (LP), que posee un aumento sostenido del número absoluto de linfocitos B en la sangre y por último una presentación linfoproliferativa tumoral en forma de linfosarcoma o linfoma maligno con la presencia de masas sóli-das tumorales, infiltrando diferentes órganos y tejidos (Burny et al, 1987;Ogawa et al, 1987).…”

Section: Introductionunclassified

Polymorphisms of BoLA-DRB3 gene and its association with resistance / susceptibility to Leucosis in Holstein cattle from La Pampa

Baltian¹,

Follmer²,

Peratta³

et al. 2016

cienvet

View full text Add to dashboard Cite

Polimorfismos del exón 2 del gen BoLA-DRB3 asociados con resistencia / susceptibilidad a leucosis en ganado Holstein de La Pampa ResumenLa leucosis bovina enzoótica es una enfermedad del ganado bovino adulto causada por el retrovirus de la leucemia bovina. Se puede manifestar como: una forma asintomática aleucémica, con un número normal de linfocitos B en sangre; una forma de linfocitosis permanente, con aumento del número de linfocitos B y como una presentación linfoproliferativa tumoral en forma de linfosarcoma. Los alelos de los genes del Complejo Principal de Histocompatibilidad Bovino (BoLA) han sido asociados con resistencia y susceptibilidad a enfermedades infecciosas. El objetivo general del presente estudio consistió en asociar los polimorfismos del exón 2 del gen BoLA-DRB3.2, definidos mediante la técnica de Reacción en Cadena de la Polimerasa y la técnica de Polimorfismos de la Longitud de los Fragmentos de Restricción (PCR-RFLP), con resistencia/susceptibilidad a leucosis en vacas Holstein de La Pampa. Se basó en un diseño caso/control, para lo cual se tomó muestra de sangre a 150 animales en 3 oportunidades con intervalos de tres meses cada una. Los animales fueron incluidos en el grupo caso cuando dieron positivos en la prueba de inmunodeficiencia en agar (DIDA) y cuyo recuento linfocitario en sangre fue ≥ 10.000 linfocitos/µl y el grupo control estuvo constituido con animales negativos en DIDA y que tenían < 10.000 linfocitos/µl de sangre. Los tests Exacto de Fisher y Odds Ratio (OR) de Woolf-Haldane se utilizaron para estudiar la asociación entre recuento de linfocitos y resultados del DIDA con las variantes alélicas. En 82 animales genotipados por PCR-RFLP el alelo DRB3.2*22 evidenció un OR= 5,332 (p= 0,0138) y el alelo DRB3.2*11 mostró un OR= 0,11 (p=0,001) siendo más

show abstract

Tyrosine phosphorylation of an interleukin 2 receptor-like protein in cells transformed by human T cell leukemia virus type I.

Cited by 8 publications

References 22 publications

Evoidence that the Tyrosine Kinase Domain of a Small Fraction of Epidermal Growth Factor Receptor Molecules is Exposed on the Outer Surface of A431 Cells.

Evoidence that the Tyrosine Kinase Domain of a Small Fraction of Epidermal Growth Factor Receptor Molecules is Exposed on the Outer Surface of A431 Cells.

Interleukin 2 (IL-2)-induced tyrosine phosphorylation of IL-2 receptor p75.

Polymorphisms of BoLA-DRB3 gene and its association with resistance / susceptibility to Leucosis in Holstein cattle from La Pampa

Contact Info

Product

Resources

About