Muscle transcriptome analysis identifies genes involved in ciliogenesis and the molecular cascade associated with intramuscular fat content in Large White heavy pigs
the content of intramuscular fat (IMF) is a complex trait that affects the sensory and technological features of the product determines the quality of meat and pork. Thus, we aimed to analyze through RNA-semimembranosus muscle transcriptome sequencing of Italian white large pig to study gene networks associated with the deposition of the IMF. Two groups of samples used; each consisting of six pigs is not associated with extreme and divergent IMF content (0.67 ± 0.09% in the low IMF vs. 6.81 ± 1.17% in the group of high IMF) selected from 950 individuals of the original race.
Paired-end RNA sequences were aligned with Sus scrofa 11.1 assembling genomes and gene number was analyzed by using WGCNA and DeSeq2 in the neighborhood R. Interestingly, among the 58 genes differentially expressed (degs), some associated with primary ciliary organelles (such Lebercilin 5 gene), in addition to genes involved in the regulation of cell differentiation, in the control of RNA-processing, and G-protein and ERK signaling pathway. Together with genes associated with cilia, we also found in pigs IMF high over-expression of Fibroblast Growth Factor 2 (FGF2) gene, which in other animal species found to be a regulator of ciliogenesis.
WGCNA module four genes would produce significant results of analyzes related to the deposition of the IMF: grey60 (P = 0.003), darkturquoise (P = 0.022), skyblue1 (P = 0.022), and lavenderblush3 (P = 0.030). Genes in a significant module confirmed the . Among the complex molecular affecting fat depot muscle, genes involved in cilia primer may have an important role, and reprogramming transcription observed in pigs IMF height can be associated with a cascade related molecules FGF and ciliogenesis, which in the literature has been associated with the differentiation of precursor fibro-adipogenic.
Muscle transcriptome analysis identifies genes involved in ciliogenesis and the molecular cascade associated with intramuscular fat content in Large White heavy pigs
differential response to kinase inhibition in triple negative breast cancer cells FGFR2-addiction: phosphoproteomics quantitative studies.
Fibroblast Growth Factor (FGF) signaling depends frequently activated in cancer by different mechanisms. However, the downstream signal transduction pathways involved are poorly characterized. Here differential quantitative approach phosphoproteomics, SILAC, applied to identify phosphorylation events FGF-arranged in two tumor cell lines triple negative breast, MFM223 and SUM52, that exhibit enhanced expression of FGF receptor 2 (FGFR2) and depending on the advanced FGFR2 signaling for cell survival.
Gene Ontology Comparative proteome analysis revealed that cells enriched SUM52 proteins associated with cell metabolism and cell MFM223 enriched proteins associated with cell adhesion and migration. FGFR2 inhibition by SU5402 impact of a significant fraction of phosphoproteome observed from these cells. This study extends the known landscape of FGF signaling and identify many new targets for functional investigations.
Description: A polyclonal antibody against FGF9. Recognizes FGF9 from Human, Mouse, Rat. This antibody is Unconjugated. Tested in the following application: WB, ELISA;WB:1/500-1/2000.ELISA:1/20000
Description: A polyclonal antibody against FGF9. Recognizes FGF9 from Human. This antibody is Unconjugated. Tested in the following application: ELISA, IHC; Recommended dilution: IHC:1:20-1:200
Description: A polyclonal antibody against FGF9. Recognizes FGF9 from Human, Mouse, Rat. This antibody is Unconjugated. Tested in the following application: ELISA, IHC;ELISA:1:1000-1:2000, IHC:1:15-1:50
Description: A polyclonal antibody against FGF9. Recognizes FGF9 from Human, Mouse, Rat. This antibody is Unconjugated. Tested in the following application: ELISA, WB, IHC;ELISA:1:2000-1:5000, WB:1:500-1:2000, IHC:1:50-1:200
Description: Plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation and cell migration. May have a role in glial cell growth and differentiation during development, gliosis during repair and regeneration of brain tissue after damage, differentiation and survival of neuronal cells, and growth stimulation of glial tumors.
Description: Plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation and cell migration. May have a role in glial cell growth and differentiation during development, gliosis during repair and regeneration of brain tissue after damage, differentiation and survival of neuronal cells, and growth stimulation of glial tumors.
Description: FGF 9, Fibroblast growth factor 9, is a protein that in humans is encoded by the FGF9 gene. The protein encoded by this gene is a member of the fibroblast growth factor(FGF) family. The FGF 9 gene contains 3 exons. By radioactive chromosomal in situ hybridization, the FGF 9 gene is mapped to chromosome 13q11-q12. This protein was isolated as a secreted factor that exhibits a growth-stimulating effect on cultured glial cells. In nervous system, this protein is produced mainly by neurons and may be important for glial cell development. Expression of the mouse homolog of this gene was found to be dependent on Sonic hedgehog(Shh) signaling.
Description: FGF 9, Fibroblast growth factor 9, is a protein that in humans is encoded by the FGF9 gene. The protein encoded by this gene is a member of the fibroblast growth factor (FGF) family. The FGF 9 gene contains 3 exons. By radioactive chromosomal in situ hybridization, the FGF 9 gene is mapped to chromosome 13q11-q12. This protein was isolated as a secreted factor that exhibits a growth-stimulating effect on cultured glial cells. In nervous system, this protein is produced mainly by neurons and may be important for glial cell development. Expression of the mouse homolog of this gene was found to be dependent on Sonic hedgehog (Shh) signaling.
Description: FGF-9 is an autocrine and paracrine prostatic growth factor expressed by prostatic stromal cells. FGF-9 induces osteoblast proliferation and new bone formation in a bone organ assay. FGF-9 is produced by many prostate cancer cells and contributes to prostate cancer-induced new bone formation. It also may participate in the osteoblastic progression of prostate cancer in bone. It is also an autocrine and/or paracrine neurotrophic factor that promotes the survival of motoneurons and upregulates choline acetyl-transferase activity. FGF-9 enhances survival of AChE-positive neurons and increases their mean soma size. It also up-regulates their choline acetyltransferase activity as potently as NGF and the effect is greater than that elicited by bFGF, CNTF, or GDNF. FGF-9 acts as a survival factor for neurons but does not promote neurite outgrowth. FGF-9 has been shown to mediate its effects by binding to FGF receptors. It efficiently activates the FGFR2c splice form of FGFR2 and the FGFR3b and FGFR3c splice isoforms of FGFR3.
Description: FGF-9 is an autocrine and paracrine prostatic growth factor expressed by prostatic stromal cells. FGF-9 induces osteoblast proliferation and new bone formation in a bone organ assay. FGF-9 is produced by many prostate cancer cells and contributes to prostate cancer-induced new bone formation. It also may participate in the osteoblastic progression of prostate cancer in bone. It is also an autocrine and/or paracrine neurotrophic factor that promotes the survival of motoneurons and upregulates choline acetyl-transferase activity. FGF-9 enhances survival of AChE-positive neurons and increases their mean soma size. It also up-regulates their choline acetyltransferase activity as potently as NGF and the effect is greater than that elicited by bFGF, CNTF, or GDNF. FGF-9 acts as a survival factor for neurons but does not promote neurite outgrowth. FGF-9 has been shown to mediate its effects by binding to FGF receptors. It efficiently activates the FGFR2c splice form of FGFR2 and the FGFR3b and FGFR3c splice isoforms of FGFR3.
Description: Fibroblast growth factor 9 is also known as FGF9, GAF, HBFG-9, SYNS3, and is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF9 is also a mitogen for oligodendrocyte type 2 astrocyte progenitor cells, smooth muscle cells, pheochromocytoma PC12 cells, and BALB/3T3 fibroblasts. However, unlike FGF acidic and basic, FGF9 has no effect on human umbilical vein endothelial cells, and it has been demonstrated that FGF9 binds preferentially to the IIIc form of FGFR3. Although no typical signal sequence was found in FGF9, it is secreted efficiently after synthesis not in a conventional manner. In nervous system, FGF9 is produced mainly by neurons and may plays an important role in CNS development. FGF9 has been shown to interact with Fibroblast growth factor receptor 3.
Description: A polyclonal antibody raised in Rabbit that recognizes and binds to Human FGF9 . This antibody is tested and proven to work in the following applications:
FGF signaling pathway is found to be flexible in architecture as both shared and divergent, in response to the FGFR2 kinase inhibitory activity in canonical RAF / MAPK / ERK / RSK and PI3K / AKT / PDK / mTOR / S6K pathways identified. Inhibition of the negative feedback path dependent phosphorylation observed, defining the FGFR2 inhibitory mechanisms of intrinsic resistance. These findings have implications for FGFR inhibitor therapy applications because they identify both common and different responses in cells of the same genetic lesion hides and pathways of drug resistance.
Felicia
