Редактирование: BMX

Cytoplasmic tyrosine-protein kinase BMX (EC 2.7.10.2) (Bone marrow tyrosine kinase gene in chromosome X protein) (Epithelial and endothelial tyrosine kinase) (ETK) (NTK38)

==Publications==

{{medline-entry
|title=Inducible Activation of [[FGFR2]] in Adult Mice Promotes Bone Formation After Bone Marrow Ablation.
|pubmed-url=https://pubmed.ncbi.nlm.nih.gov/28650109
|abstract=Apert syndrome is one of the most severe craniosynostoses, resulting from gain-of-function mutations in fibroblast growth factor receptor 2 ([[FGFR2]]). Previous studies have shown that gain-of-function mutations of [[FGFR2]] (S252W or P253R) cause skull malformation of human Apert syndrome by affecting both chondrogenesis and osteogenesis, underscoring the key role of [[FGFR2]] in bone development. However, the effects of [[FGFR2]] on bone formation at the adult stage have not been fully investigated. To investigate the role of [[FGFR2]] in bone formation, we generated mice with tamoxifen-inducible expression of mutant [[FGFR2]] (P253R) at the adult stage. Mechanical bone marrow ablation ([[BMX]]) was performed in both wild-type and Fgfr2 mutant (MT) mice. Changes in newly formed trabecular bone were assessed by micro-computed tomography and bone histomorphometry. We found that MT mice exhibited increased trabecular bone formation and decreased bone resorption after [[BMX]] accompanied with a remarkable increase in bone marrow stromal cell recruitment and proliferation, osteoblast proliferation and differentiation, and enhanced Wnt/β-catenin activity. Furthermore, pharmacologically inhibiting Wnt/β-catenin signaling can partially reverse the increased trabecular bone formation and decreased bone resorption in MT mice after [[BMX]]. Our data demonstrate that gain-of-function mutation in [[FGFR2]] exerts a Wnt/β-catenin-dependent anabolic effect on trabecular bone by promoting bone formation and inhibiting bone resorption at the adult stage. © 2017 American Society for Bone and Mineral Research.
|mesh-terms=* Aging
* Animals
* Bone Marrow
* Bone Resorption
* Cancellous Bone
* Cell Differentiation
* Cell Proliferation
* Gain of Function Mutation
* Mesenchymal Stem Cells
* Mice, Inbred C57BL
* Mice, Transgenic
* Osteogenesis
* Phenotype
* Receptor, Fibroblast Growth Factor, Type 2
* Up-Regulation
* Wnt Signaling Pathway
|keywords=* BONE FORMATION
* BONE MARROW ABLATION
* FGFR2
* WNT/β-CATENIN
|full-text-url=https://sci-hub.do/10.1002/jbmr.3204
}}
{{medline-entry
|title=Enhanced activity of an angiotensin-(1-7) neuropeptidase in glucocorticoid-induced fetal programming.
|pubmed-url=https://pubmed.ncbi.nlm.nih.gov/24355101
|abstract=We previously identified angiotensin converting enzyme (ACE) and an endopeptidase activity that degraded angiotensin-(1-7) [Ang-(1-7)] to Ang-(1-5) and Ang-(1-4), respectively, in the cerebrospinal fluid (CSF) of 6-month old male sheep. The present study undertook a more comprehensive analysis of the CSF peptidase that converts Ang-(1-7) to Ang-(1-4) in control and in utero betamethasone-exposed sheep ([[BMX]]). Characterization of the Ang-(1-7) peptidase revealed that the thiol agents 4-aminophenylmercuric acetate (APMA) and p-chloromercuribenzoic acid (PCMB), as well as the metallo-chelators o-phenanthroline and EDTA essentially abolished the enzyme activity. Additional inhibitors for serine, aspartyl, and cysteine proteases, as well as selective inhibitors against the endopeptidases neprilysin, neurolysin, prolyl and thimet oligopeptidases did not attenuate enzymatic activity. Competition studies against the peptidase revealed similar IC50s for Ang-(1-7) (5μM) and Ang II (3μM), but lower values for Ala(1)-Ang-(1-7) and Ang-(2-7) of 1.8 and 2.0μM, respectively. In contrast, bradykinin exhibited a 6-fold higher IC50 (32μM) than Ang-(1-7) while neurotensin was a poor competitor. Mean arterial pressure (78±1 vs. 94±2mmHg, N=4-5, P<0.01) and Ang-(1-7) peptidase activity (14.2±1 vs 32±1.5fmol/min/ml CSF, N=5, P<0.01) were higher in the [[BMX]] group, and enzyme activity inversely correlated with Ang-(1-7) content in CSF. Lower Ang-(1-7) expression in brain is linked to baroreflex impairment in hypertension and aging, thus, increased activity of an Ang-(1-7) peptidase may contribute to lower CSF Ang-(1-7) levels, elevated blood pressure and impaired reflex function in this model of fetal programming. 
|mesh-terms=* Aging
* Angiotensin I
* Animals
* Baroreflex
* Edetic Acid
* Hypertension
* Male
* Peptide Fragments
* Peptidyl-Dipeptidase A
* Phenanthrolines
* Phenylmercuric Acetate
* Sheep
* Substrate Specificity
* p-Chloromercuribenzoic Acid
|keywords=* Ang-(1–7)
* Cerebrospinal fluid
* Peptidase
* Renin angiotensin system
|full-text-url=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4157337
}}