Biomedical subjects

Erica M Hanson

Publications and source records attributed to Erica M Hanson.

4 recordsLinked to original sources

PubMed2005

Interleukin-13 (IL-13) pathway.

Interleukin-13 (IL-13), like IL-4, is a cytokine produced by T(H)2 type helper T cells in response to signaling through the T cell antigen receptor and by mast cells and basophils upon cross-linkage of the high-affinity receptor for immunoglobulin E (IgE). It is also produced by activated eosinophils. IL-13 induces many of the same responses as IL-4 and shares a receptor subunit with IL-4. IL-13 has been implicated in airway hypersensitivity and mucus hypersecretion, inflammatory bowel disease, and parasitic nematode expulsion.

Animals↗

PubMed2005

Interleukin-4 (IL-4) pathway.

Interleukin-4 (IL-4) is a cytokine produced by T(H)2 type helper T cells and by mast cells, basophils, and eosinophils. This cytokine can elicit many responses, some of which are associated with allergy and asthma. Studies with long-term cell lines and primary cells have revealed differences in the signaling between these two experimental systems. Understanding these differences is important because therapeutic strategies targeting IL-4 and its signaling pathways are currently being tested to treat allergy and asthma.

Animals↗

PubMed2003

Interleukin-4 and interleukin-13 signaling connections maps.

Cytokines are inflammatory mediators important in responding to pathogens and other foreign challenges. Interleukin-4 (IL-4) and IL-13 are two cytokines produced by T helper type 2 cells, mast cells, and basophils. In addition to their physiological roles, these cytokines are also implicated in pathological conditions such as asthma and allergy. IL-4 can stimulate two receptors, type I and type II, whereas IL-13 signaling is mediated only by the type II receptor (see the STKE Connections Maps). These cytokines activate the Janus kinase/signal transducer and activator of transcription (JAK/STAT) signaling cascades, which may contribute to allergic responses. In addition, stimulation of the phosphatidylinositol 3-kinase (PI3K) pathway through recruitment of members of the insulin receptor substrate family may contribute to survival and proliferation.

Amino Acid Motifs↗

PubMed2002

Regulation of the dephosphorylation of Stat6. Participation of Tyr-713 in the interleukin-4 receptor alpha, the tyrosine phosphatase SHP-1, and the proteasome.

Signal transducer and activator of transcription 6 (Stat6) plays an important role in interleukin (IL)-4-induced responses. To analyze the regulation of Stat6 phosphorylation, cells were cultured in the continuous presence of IL-4 or after a pulse and washout. In the continual presence of IL-4, Stat6 remained phosphorylated for an extended period. After IL-4 removal and inhibition of the Janus family kinase, tyrosine-phosphorylated Stat6 decayed at a rate dependent upon the length of IL-4 stimulation. The decay of tyrosine-phosphorylated Stat6 was similar in the presence or absence of either cycloheximide or actinomycin D. In the absence of functional Src homology-containing phosphatase-1 (SHP-1), the early loss of tyrosine-phosphorylated Stat6 was substantially reduced. Furthermore, the rate of loss of tyrosine-phosphorylated Stat6 in cells expressing a mutation of the human IL-4 receptor alpha in the immunoreceptor tyrosine-based inhibitory motif sequence (Y5F) was dramatically decreased compared with wild-type cells. The early rate of decay was similar in the presence or absence of MG132, an inhibitor of the proteasome, but the later rate of decay was decreased 5-fold. These results suggest that the loss of tyrosine phosphorylation of Stat6 is regulated by the action of SHP-1 and the proteasome but is not dependent on new protein synthesis.

Animals↗