Inhibition in Proper Ser and In Plcγ2 Synthesis Are the Main for Causing Osteoarthritis, Diabetes, and C-Lymphocytic Leukemia Diseases

Proper S6K /BTK and PLCγ2 synthesis (which regulated by Ser phosphorylation pathway) are main regulations for thromboxane-A “TXA2” synthesis, and necessary for B-cell maturations and T-cells modulations and functions. The main reasons for causing Osteoarthritis “OA” and diabetes diseases (that are linked together) are the deficiency of Ser amino acids and decreasing of Ser phosphorylation signalling pathway which necessary for proper S6K productions, where normally the Ser phosphorylation signalling pathway is the basis of Ser /Thr phosphorylation signalling and is necessary for proper Akt, S6K1 synthesis and necessary for RORs and IFNs synthesis and also necessary for running proper BTK for PLCγ2 productions , where S6K is main regulator for ATPase and for proper PLCγ1 and for PLCγ2 synthesis which necessary for bone growth and for modulating immune efficiency. Osteoarthritis “OA” is characterized by a sharp expression in Gamma-Phospholipase C-1 “PLCγ1”, with decreasing “or inhibition” in PLCγ2 “PLC beta” productions due to inhibition or mutation in S6K and then in BTK. The increasing in PLCγ1 with Deficiency in Ser amino acids will lead to deficiency in Ser phosphorylation signalling, and decreasing in synthase activity that will reflect down regulations in BTK pathways and lead to inhibition in PLCγ2 productions which will reflect diabetes (inhibition in Estrogen with the production of Androgen instead of estrogen) and can reflect Osteoarthritis “OA” prognosis depend on the percentage of Deficiency or inhibition in basic amino acids and its basic necessary signaling pathways. The proper S6K are so necessary for reactivating both PLCγ1&2, where phospholipase Cγ2 (PLCγ2) is activated from a variety of cell surface receptors such as SyK “S6K”. The B-cells are promoted by the function and activities of both PLCγ1&2, but the deficiency in Ser amino acids will reflect decreasing in Ser phosphorylation pathways and then decreasing in Estrogen synthesis, with increasing in Androgen synthesis which lead to decreasing in PLCs isoforms production and lead to pathogenic diabetes problem. So T2DM is strongly connected with OA diseases are linked together that deficiency in Ser amino acids and their phosphorylation can cause both diseases, and any early step from any of those two or more similar diseases can lead to the other. Pathogenic type 2 diabetes associated with progressive beta-cell impairment due to the mutations in the production of S6K1 and inhibition in the PLCγ2 which due to inhibition or decreasing in Ser phosphorylation signaling during mTOR Ser/Thr phosphorylation pathways that can reflect Inhibition in The releasing of PS/T-Thymine Kinases and PS/T-Cytosine kinases chains (mTORC1) which are depending on availability of hydrophobic amino acids synthesis including Ser and Tyr which can be modified by synthetase enzymes for creating active gamma-subunits (upon synthetase effects) that can be modified by synthase effect for Beta-subunit synthesis “PLCγ2” then will be modified by phospholipase effects for alpha subunits productions.The releasing of PS/T-Thymine -Kinase and PS/T-Cytosine -kinase chains (mTORC1) from the phosphorylations of Ser amino acids is so necessary steps for normal proper S6K productions, which necessary for IFN-Gamma and for PLCγ1 productions, and therefore necessary for normal PLCγ2 synthesis upon “BTK activity” which is necessary for B-cell maturations , for T-cells modulations, for modulating anti-inflammatory steps and procedures, for thromboxane-A synthesis, and for bone growth and modulation.Inhibition in PS/T-Thymine -Kinase and PS/T-Cytosine -kinase chains (mTORC1) productions will be the main reason for inhibition the beta subunits productions that can be the reason of decreasing in the hyperpolarization and then electrical activity will lead to decreasing in the abolition of Ça+ . Deficiency in conversion of glutarate to glutamate and decreasing in proline biosynthesis can affect on cartilage synthesis and bone growth due to decreasing in stimulating mitochondrial OPA1 oxidations.It’s imp to note that Tyrosine phosphatase PTPs are important regulator of chondrogenic patterning and are critical regulators of tyrosine phosphorylation that it’s activity depends on Tyr, Ser synthesis (hydrophobic acids) and on JAK state signaling activities. And so, the proline-rich tyrosine kinases regulate proper PLCs isoforms which compete for binding site at the very C terminus of fibroblast growth factor for osteorogenitor embryonic development , and bone formations. Synthetase is the main regulator for PLCγ1 activities followed by synthase effects which is the main regulator for beta-subunits “PLCγ2” productions which is able to “upregulate phospholipase abtivity” for alpha subunits (PLC-alpha) productions for reactivating fibroblast growth factor receptor (FGFR2), for reactivating both IgM and IgD, and for TLR4 productions for osteoblast processes. Where, PLCγ1 competes for a binding site at the very C terminus of FGFR2 for embryonic development and bones growth, where, PLCs isoforms are involved in multiple stages in TLR4, interferon, and in anti-inflammatory steps. And also, PLCγ1 recruit to CSF-1 is following imp stages for producing PLCγ2 which is necessary for activating anti-inflammatory where, IFN-γ activates PLC-γ2 via an upstream of tyrosine kinase. PLCγ1 recruited to CSF-1 for two pathways activities 1st / re-activating IFNs productions which regulate MHC class1 and class two for modulating cell-surface protein activities , 2nd / activating PLCγ2 for modulating T-cells , where PLCγ1 involved in the production of TRIM22 for mediating antiviral activities and anti-inflammatory processes through reactivating IFNs productions for PLCγ2 synthesis. PLCγ2 are so imp in anti-inflammatory processes and can be considered as having the main roles for thromboxane-A synthesis. Inhibitions or mutations in S6K, in BTK and then in PLCγ2 productions will cause an inherent or inhibition in CXCL12 then followed by inherent or inhibition in CXCR4 then reflect inherent or inhibition in the regulation of B-cell growth through mutations in IgM and in IgD. Proline amino acids is necessary for reactivate OPA1 anabolic oxidations (started by synthetase, then synthase, then phospholipase for producing gamma “PLCγ1” , then beta “PLCγ2” , and then alpha “PLC-a” subunits respectively) for cartilage synthesis which promote PLCγ2 synthesis necessary for bone growth including antigen and thromboxane-A synthesis.

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