Prolactin (PRL) is a secreted neuroendocrine pituitary hormone that acts primarily on the mammary gland to promote lactation, but has pleiotropic effects in both males and females. Non-glycosylated prolactin is produced by the pituitary and packaged in storage granules before secretion, while glycosylated prolactin is reported to be constitutively secreted, have lower biological potency, and be removed from the circulation more quickly. Prolactin is synthesized mainly by the anterior pituitary in all mammals, where secretion is under tonic inhibition by hypothalamic dopamine. In humans, prolactin is also produced peripherally. Prolactin expression is low during early human pregnancy, but increases in late pregnancy. The prolactin receptor (PRLR) is a transmembrane type I glycoprotein that belongs to the cytokine hematopoietic receptor family. prolactin molecule is thought to bind two receptor molecules. In addition to its lactogenic activity, peripherally produced prolactin plays roles in breast and prostate cancer development, regulation of reproductive function, and immunoregulation.
This gene encodes a protein that is instrumental in patterning the early embryo. It has been implicated as the key inductive signal in patterning of the ventral neural tube, the anterior-posterior limb axis, and the ventral somites. Of three human proteins showing sequence and functional similarity to the sonic hedgehog protein of Drosophila, this protein is the most similar. The protein is made as a precursor that is autocatalytically cleaved; the N-terminal portion is soluble and contains the signalling activity while the C-terminal portion is involved in precursor processing. More importantly, the C-terminal product covalently attaches a cholesterol moiety to the N-terminal product, restricting the N-terminal product to the cell surface and preventing it from freely diffusing throughout the developing embryo.
SH2-containing inositol phosphatase 1 (SHIP1) is a hematopoietic phosphatase that hydrolyzes phosphatidylinositol-3,4,5-triphosphate to phosphatidylinositol-3,4-bisphosphate. SHIP1 is a cytosolic phosphatase with an SH2 domain in its amino terminus and two NPXY Shc binding motifs in its carboxy terminus. Upon receptor cross-linking, SHIP is first recruited to the membrane junction through binding of its SH2 domain to the phospho-tyrosine in the ITIM motif, followed by tyrosine phosphorylation on the NPXY motif. The membrane relocalization and phosphorylation on the NPXY motif is essential for the regulatory function of SHIP1. Its effect on calcium flux, cell survival, growth, cell cycle arrest, and apoptosis is mediated through the PI3K and Akt pathways. Tyr1021 is located in one of the NPXY motifs in SHIP1, and its phosphorylation is important for SHIP1 function.
SH2-containing inositol phosphatase 1 (SHIP1) is a hematopoietic phosphatase that hydrolyzes phosphatidylinositol-3,4,5-triphosphate to phosphatidylinositol-3,4-bisphosphate. SHIP1 is a cytosolic phosphatase with an SH2 domain in its amino terminus and two NPXY Shc binding motifs in its carboxy terminus. Upon receptor cross-linking, SHIP is first recruited to the membrane junction through binding of its SH2 domain to the phospho-tyrosine in the ITIM motif, followed by tyrosine phosphorylation on the NPXY motif. The membrane relocalization and phosphorylation on the NPXY motif is essential for the regulatory function of SHIP1. Its effect on calcium flux, cell survival, growth, cell cycle arrest, and apoptosis is mediated through the PI3K and Akt pathways. Tyr1021 is located in one of the NPXY motifs in SHIP1, and its phosphorylation is important for SHIP1 function.SHIP2, a homolog of SHIP1, is highly expressed in heart, skeletal muscle and placenta.SHIP2 negatively regulates insulin signaling and polymorphisms in SHIP2 have been linked to hyperglycemia. Recent studies also suggest SHIP2 as a therapeutic target for the treatment of both obesity and type 2 diabetes. Tyr1135 is phosphorylated in human cancer cells.
The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. N-terminal part of this PTP contains two tandem Src homolog (SH2) domains, which act as protein phospho-tyrosine binding domains, and mediate the interaction of this PTP with its substrates. This PTP is expressed primarily in hematopoietic cells, and functions as an important regulator of multiple signaling pathways in hematopoietic cells. This PTP has been shown to interact with, and dephosphorylate a wide spectrum of phospho-proteins involved in hematopoietic cell signaling. Multiple alternatively spliced variants of this gene, which encode distinct isoforms, have been reported.
The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP contains two tandem Src homology-2 domains, which function as phospho-tyrosine binding domains and mediate the interaction of this PTP with its substrates. This PTP is widely expressed in most tissues and plays a regulatory role in various cell signaling events that are important for a diversity of cell functions, such as mitogenic activation, metabolic control, transcription regulation, and cell migration. Mutations in this gene are a cause of Noonan syndrome as well as acute myeloid leukemia.
Acts as a negative regulator of the Toll-like and IL-1R receptor signaling pathways. Attenuates the recruitment of receptor-proximal signaling components to the TLR4 receptor, probably through an TIR-TIR domain interaction with TLR4. Through its extracellular domain interferes with the heterodimerization of Il1R1 and IL1RAP.
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