Friday, September 27, 2013

FOR POWER, WATCH THE COMPANY YOU KEEP! IBRUTINIB, A WONDER DRUG.

 IBRUTINIB, A WONDER DRUG.
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If there is a wonder drug, nothing comes close to Ibrutinib!  This drug could be a wonder drug for sure because it affect not only powerful genes that cause malformations when they are mutated (a clear power of the gene) but also involve all mighty "wild genes" (those  having multiple interactions).
Malformations involved  by the Bruton (BTK) gene are particularly wide going from Agammaglobulinemia which kill children with multiple infections, to the Sturge-Weber syndrome which lead to mental Retardation and seizures, to the Albright syndrome!  Even bone dysmorphy is in the wing.

wild genes involved include the Gerb2 through the GAB1, the LYN, PTPN1 etc...
The mere involvement of the Adenyl Cyclase remind us of some of the undesirable effect of powerful infection such as E.coli, Mycobacterium, and the Whooping cough!  All these various pathways are affected broadening the impact of Ibrutinib to all white blood cell neoplastic process!

By affecting the GNAQ, Bruton's Inhibitor  could work in Uveal Melanoma theoritically

And through inhibition of the GPCR family (S1PR1) Bruton inhibitor could act in Angiosarcoma and harmartomatous syndromes. Remember RIC8A and the Gs -ALPHA are affected!

Investors, if you have not jump on the wagon, it is not too late!  Ibrutinib is a wild one with unlimited potential!  IBRUTINIB IS POWERFUL BECAUSE OF THE GENE COMPANY IT KEEPS!
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the CRBCM has not invested in any drug to this point! But the science is behind this drug!
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WIKIPEDIA comes to the Rescue with scientific comments!


In preclinical studies on chronic lymphocytic leukemia (CLL) cells, ibrutinib has been reported to promote apoptosis, inhibit proliferation, and also prevent CLL cells from responding to survival stimuli provided by the microenvironment.[11] In this study, treatment of activated CLL cells with ibrutinib resulted in inhibition of Btk tyrosine phosphorylation and also effectively abrogated downstream survival pathways activated by this kinase including ERK1/2, PI3K, and NF-κB. Additionally, ibrutinib inhibited proliferation of CLL cells in vitro, effectively blocking survival signals provided externally to CLL cells from the microenvironment including soluble factors (CD40L, BAFF, IL-6, IL-4, and TNF-α), fibronectin engagement and stromal cell contact.
In early clinical studies, the activity of ibrutinib has been described to include a rapid reduction in lymphadenopathy accompanied by a transient lymphocytosis, suggesting that the drug might have direct effects on cell homing or migration to factors in tissue microenvironments.[12]
Ibrutinib has been reported to reduce CLL cell chemotaxis towards the chemokines CXCL12 and CXCL13, and inhibit cellular adhesion following stimulation at the B cell receptor.[13][14] Together, these data are consistent with a mechanistic model whereby ibrutinib blocks BCR signaling, which drives cells into apoptosis and/or disrupts cell migration and adherence to protective tumor microenvironments.

1.S1PR1 is one of the main responsible of vascular growth and development, at least during embryogenesis.[9] In vascular endothelial cells the binding of S1P to S1PR1 induces migration, proliferation, cell survival and morphogenesis into capillary-like structures.[10] Moreover, the binding of S1P to S1PR1 is implicated in the formation of cell-cell adherens junctions, therefore inhibiting paracellular permeability of solutes and macromolecules.[11][12] It was also shown in vivo that S1P synergizes with angiogenic factors such as FGF-2 and VEGF in inducing angiogenesis and vascular maturation through S1PR1.[12][13] showed that S1PR1-KO mice died during development due to a defect in vascular stabilization, suggesting that this receptor is essential for vascular development. In conclusion, several evidences confirm that S1P via S1PR1 is a potent regulator of vascular growth and development, at least during embryogenesis.[9]

2.RGS16.  It inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits.

3.GNAQ1 activity is terminated by:

Activation of GNAQ1 is terminated by a GTPase intrinsic to the G-alpha subunit. G-alpha-q is the alpha subunit of one of the heterotrimeric GTP-binding proteins that mediates stimulation of phospholipase C-beta (MIM 600230).[supplied by OMIM][2]
4. Bruton's tyrosine kinase (abbreviated Btk or BTK) is a type of kinase enzyme implicated in the primary immunodeficiency disease X-linked agammaglobulinemia (Bruton's agammaglobulinemia). Its exact mechanism of action remains unknown, but it plays a crucial role in B cell maturation as well as mast cell activation through the high-affinity IgE receptor. Patients with XLA have normal pre-B cell populations in their bone marrow but these cells fail to mature and enter the circulation. The Btk gene is located on the X chromosome.[1] At least 400 mutations of the Btk gene have been identified.WIKIPEDIA


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