314 Results for: "peptide synthesis"

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Glucose-6-Phosphate 1-Dehydrogenase (G6PD) is a cytosolic enzyme that belongs to the glucose-6-phosphate dehydrogenase family. G6PD participates in the pentose phosphate pathway that supplies reducing energy to cells by maintaining the level of the co-enzyme nicotinamide adenine dinucleotide phosphate (NADPH). G6PD produces pentose sugars for nucleic acid synthesis and main producer of NADPH reducing power. NADPH in turn maintains the level of glutathione in these cells that helps protect the red blood cells against oxidative damage. It is notable in humans that G6PD is remarkable for its genetic diversity. G6PD deficiency may cause neonatal jaundice, acute hemolysis, or severe chronic non-spherocytic hemolytic anemia.

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Cluster of Differentiation 74 (CD74) is also known as HLA class II histocompatibility antigen gamma chain (HLADG), DHLAG, Ia-GAMMA, invariant chain (Abbreviated Ii). CD74 / HLADG is a polypeptide involved in the formation and transport of MHC class II protein. The cell surface form of the invariant chain is known as CD74. CD74 is upregulated in several cancers and is also expressed by non-immune cells during inflammation. CD74 plays a critical role in MHC class II antigen processing by stabilizing peptide-free class II alpha / beta heterodimers in a complex soon after their synthesis and directing transport of the complex from the endoplasmic reticulum to the endosomal / lysosomal system where the antigen processing and binding of antigenic peptides to MHC class II takes place. CD74 / DHLAG also serves as cell surface receptor for the cytokine MIF.

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Interleukin-10 (IL-10) is a cytokine produced by activated Th2 cells, B cells, keratinocytes and monocytes/macrophages. In vitro murine and human IL-10 inhibits cytokine synthesis by Th1 cells, natural killer cells and monocytes/macrophages. Several studies have suggested the potential application of IL-10 as an anti-inflammatory agent in the treatment of septic shock and as an immunosuppressive agent in certain T cell mediated autoimmune diseases.

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Interleukin-10 (IL-10) is a cytokine produced by activated Th2 cells, B cells, keratinocytes and monocytes/macrophages. In vitro murine and human IL-10 inhibits cytokine synthesis by Th1 cells, natural killer cells and monocytes/macrophages. Several studies have suggested the potential application of IL-10 as an anti-inflammatory agent in the treatment of septic shock and as an immunosuppressive agent in certain T cell mediated autoimmune diseases.

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N-alpha-acetylation is one of the most common protein modifications that occurs during protein synthesis and involves the transfer of an acetyl group from acetyl-coenzyme A to the protein alpha-amino group. ARD1A, together with NATH (NARG1; MIM 608000), is part of a major N-alpha-acetyltransferase complex responsible for alpha-acetylation of proteins and peptides.N-alpha-acetylation is one of the most common protein modifications that occurs during protein synthesis and involves the transfer of an acetyl group from acetyl-coenzyme A to the protein alpha-amino group. ARD1A, together with NATH (NARG1; MIM 608000), is part of a major N-alpha-acetyltransferase complex responsible for alpha-acetylation of proteins and peptides (Sanchez-Puig and Fersht, 2006 [PubMed 16823041]).

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Low Molecular Weight Phosphotyrosine Protein Phosphatase (LMW-PTP) is a member of the low molecular weight phosphotyrosine protein phosphatase family. LMW-PTP serves as an acid phosphatase and a protein tyrosine phosphatase (PTPase) by hydrolyzing protein tyrosine phosphate to protein tyrosine and orthophosphate. LMW-PTP can be detected in all human tissues, including adipocytes. LMW-PTP is a cytosolic enzyme that regulate cell proliferation and growth of leiomyomas during dephosphorylation of the PDGF receptor. In addition, LMW-PTP plays an important role in the regulation of physiological functions, such as stress resistance and synthesis of the polysaccharide capsule.

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CD Antigen CD27 is also known as Tumor necrosis factor receptor superfamily member 7 (TNFRSF7), which belongs to TNF-receptor superfamily. CD27 / TNFRSF7 is found in most T-lymphocytes. CD27 / TNFRSF7 is required for generation and long-term maintenance of T cell immunity. It binds to ligand CD70, and plays a key role in regulating B-cell activation and immunoglobulin synthesis. This receptor transduces signals that lead to the activation of NF-κB and MAPK8/JNK. CD27 has been shown to interact with SIVA1, TRAF2 and TRAF3.

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CD27 antigen is also known as CD27L receptor, T-cell activation antigen CD27, Tumor necrosis factor receptor superfamily member 7, T14 and TNFRSF7. In humans, it is encoded by the CD27 gene. CD27 is a single-pass type I membrane protein with 3 TNFR-Cys repeats. It is a member of the TNF-receptor superfamily and is required for generation and long-term maintenance of T cell immunity. It binds to ligand CD70, and plays a key role in regulating B-cell activation and immunoglobulin synthesis. It plays a role in survival of activated T-cells and apoptosis through association with SIVA1.

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Ubiquitin-Conjugating Enzyme Variant 1a (UBE2V1) is a member of the Ubiquitin-conjugating (E2) enzyme family. The E2 catalytic core domain of UBE2V1 lacks an active site cysteine residue, rendering it catalytically inactive on its own. However, in the cytoplasm UBE2V1 is able to form a catalytically active complex with UBE2N/Ubc13, which mediates the synthesis Lys63-linked Ubiquitin chains and is required for NF-kappa B activation. UBE2V1 is required for UBE2N (Ubc13)/UBE2V1 Complex-dependent Lys63-linked Ubiquitin chain formation. More specifically, UBE2V1 orients the Ubiquitin molecule to favor linkage at Lys63 via a non-covalent interaction with the Ubiquitin molecule. The UBE2V1-UBE2N heterodimer catalyses the synthesis of non-canonical poly-ubiquitin chains that are linked through Lys63. This type of poly-ubiquitination activates IKK and does not seem to involve protein degradation by the proteasome. UBE2V1 plays a role in the activation of NF-kappa-B mediated by IL1B, TNF, TRAF6, and TRAF2. It mediates transcriptional activation of target genes. UBE2V1 also controls the progress through the cell cycle and differentiation, the error-free DNA repair pathway and contributes to the survival of cells after DNA damage.

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Tyrosine Hydroxylase (TH) is the rate-limiting enzyme in the synthesis of the catecholamines Dopamine and Norepinephrine. TH antibodies can therefore be used as markers for dopaminergic and noradrenergic neurons. We raised this polyclonal antibody against a peptide representing the sequence around Ser40 in rat TH. This antibody is suitable for most immunochemical applications in a variety of mammalian and some non-mammalian species.

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Apoptosis-Inducing Factor 1, Mitochondrial (AIFM1) is a flavoprotein essential for nuclear disassembly in apoptotic cells that is found in the mitochondrial intermembrane space in healthy cells. During apoptosis, it is translocated from the mitochondria to the nucleus to function as a proapoptotic factor in a caspase-independent pathway, while in normal mitochondria, it functions as an antiapoptotic factor via its oxidoreductase activity. The soluble form (AIFsol) found in the nucleus induces parthanatos i.e., caspase-independent fragmentation of chromosomal DNA. AIFM1 interacts with EIF3G, and thereby inhibits the EIF3 machinery and protein synthesis, and activates casapse-7 to amplify apoptosis. It binds to DNA in a sequence-independent manner and plays a critical role in caspase-independent, pyknotic cell death in hydrogen peroxide-exposed cells.

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CD27 (TNFRSF7) is a member of the TNF-receptor superfamily limited to cells of the lymphoid lineage and exists as both a dimeric glycoprotein on the cell surface and as a soluble protein in serum. As a T and B cell co-stimulatory molecule, the activity of CD27 is governed by its TNF-like ligand CD70 on lymphocytes and dendritic cells. The CD27-CD70 interaction is required for Th1 generation responses to differentiation signals and long-term maintenance of T cell immunity, and meanwhile, plays a key role in regulating B cell differentiation, activation and immunoglobulin synthesis. The CD27 receptor transduces signals and subsequently leads to the activation of NF-kappaB and MAPK8/JNK, mediated by the adaptor proteins TRAF2 and TRAF5. In addition, the proapoptotic protein SIVA is capable of binding the cytoplasmic tail of CD27 and exerts action in the process of apoptosis.

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Human epidermal growth factor receptor 2 (HER2) is a type of membrane glycoprotein, and belongs to the epidermal growth factor (EGF) receptor family. HER2 plays a key role in development, cell proliferation and differentiation. HER2 has been reported to associate with malignancy and a poor prognosis in numerous carcinomas, including breast, prostate, ovarian, lung cancers and so on. HER2 is activated by dimerization and not activated by EGF, TGF-alpha and amphiregulin. Interaction with PTK6 increases its intrinsic kinase activity.It is heterodimer with EGFR, ERBB3 and ERBB4. HER2 associates with the 5'-TCAAATTC-3' sequence in the PTGS2/COX-2 promoter and activates its transcription. It implicated in transcriptional activation of CDKN1A and the function of the protein involves STAT3 and SRC. And also it involved in the transcription of rRNA genes by RNA Pol I and enhances protein synthesis and cell growth.

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Tryptophan 2,3-dioxygenase (TDO) is a heme-containing dioxygenase catalyzing the addition of molecular oxygen across the 2,3-double bond of the indole ring of tryptophan to form N-formylkynurenine (NFK). In Anopheles gambiae, TDO is the only enzyme able to catalyze the first and rate-limiting step in L-Trp catabolism through the kynurenine pathway. Tryptophan is an essential amino acid for protein synthesis and also the precursor for production of a number of neurotransmitters, such as serotonin and melatonin; in mosquitoes, the kynurenine pathway is essential for eye pigmentation. Conceivably, the tryptophan-using pathways should be regulated in a coordinated manner in mosquitoes as well as in other species and TDO activation/inactivation processes could play an essential role in these phenomena.

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Peroxisomes are essential organelles that participate in multiple important metabolic processes, including the beta -oxidation of fatty acids, plasmalogen synthesis, and the metabolism of reactive oxygen species (ROS). Peroxiredoxins is overexpressed in breast cancer tissues to a great extent suggesting that they has a proliferative effect and may be related to cancer development or progression. Peroxiredoxin 5 (PRDX5) is a thioredoxin peroxidase that belongs to the atypical 2-Cys class of the TSA/ahpC family of peroxiredoxins. PRDX5 is a widely expressed mitochondrial antioxidant enzyme that reduces hydrogen peroxide, alkyl hydroperoxides, and peroxynitrite. In human cells, this enzyme is present in the cytosol, mitochondria, peroxisomes, and nucleus.

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LIF has the capacity to induce terminal differentiation in leukemic cells. Its activities also include the induction of hematopoietic differentiation in normal and myeloid leukaemia cells, the induction of neuronal cell differentiation and the stimulation of acute-phase protein synthesis in hepatocytes. LIF activates JAK & STAT signalling in human embryonic stem (ES) cells, but this pathway does not maintain pluripotency in these cells, which instead rely on FGF2-mediated ERK signalling. By contrast, mouse ES cells can be maintained by LIF-mediated JAK & STAT signalling. LIF binds to a high affinity heterodimeric receptor complex consisting of two proteins: LIF-R alpha that binds LIF with low affinity and the 130kDa (gp130) subunit that by itself does not bind LIF, but is required for high affinity binding of LIF.

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Mouse Il10 is the prototypic member of the IL-10 cytokine family, including IL-10, IL-19, IL-20, IL-22 (IL-TIF), IL-24 and IL-26. Many viruses encode viral members of the IL-10 family, such as Epstein-Barr virus (EBV) and human cytomegalovirus (HCMV).Its main function is inhibiting the synthesis of a number of cytokines, including IFN-gamma, IL-2, IL-3, TNF and GM-CSF produced by activated macrophages and by helper T-cells. Although human and mouse IL-10 are 81% identical at the nucleotide and amino acid level, mouse IL-10 is species-specific and does not act on human cells. Interestingly, Human IL-10 is active on mouse cells.

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Heat-Responsive Protein 12 (HRSP12) is an endoribonuclease that belongs to the Rut family. HRSP12 is found mainly in the human adult kidney and liver and is responsible for inhibiting protein translation by cleaving mRNA. HRSP12 only cleaves phosphodiester bonds in single-stranded RNA and inhibits cell-free protein synthesis. The levels of both mRNA and protein are markedly reduced in heptatocellular tumors and in human hepatoma cell lines compared with normal liver tissues. Moreover the levels of HRSP12 are different depending on the grade of the tumor. This had led to the suggestion that HRSP12 may be an important biomarker for heptatic carcinoma.

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Interferon gamma-inducible protein (IP) 10 or CXCL10 is a member of the CXC chemokine family. It binds CXCR3 activating ERK1/2, p38/MAPK, JNK, and PI3-kinase/AKT signaling pathways, inducing intracellular calcium influx, DNA synthesis, cell proliferation, and chemotaxis. IP-10 regulates innate and adaptive immune responses by affecting the function of activated T cells, natural killer cells, inflammatory dendritic cells, macrophages, and B cells. IP-10 is produced by leukocytes, activated neutrophils, eosinophils, monocytes, epithelial cells, endothelial cells, fibroblasts, and keratinocytes in response to IFN-gamma. IP-10 has been implicated in a wide range of diseases, including infectious diseases and chronic inflammatory and autoimmune diseases, as well as in tumor formation (Liu et al.).

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Thiostrepton is a thiazole-containing peptide antibiotic that inhibits protein synthesis by preventing binding of GTP to 50S ribosomal subunit.

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Mouse Vascular endothelial growth factor (VEGF or VEGF­A), is a potent mediator of both angiogenesis and vasculogenesis in the fetus and adult. It is a member of the PDGF/VEGF growth factor family that is characterized by a cystine knot structure formed by eight conserved cysteine residues. Alternately spliced isoforms of 120, 164 and 188 aa found in mouse. VEGF binds the type I transmembrane receptor tyrosine kinases VEGF R1 (also called Flt­1) and VEGF R2 (Flk­/KDR) on endothelial cells.Although affinity is highest for binding to VEGF R1, VEGF R2 appears to be the primary mediator of VEGF angiogenic activity. VEGF is required during embryogenesis to regulate the proliferation, migration, and survival of endothelial cells.It may play a role in increasing vascular permeability during lactation, when increased transport of molecules from the blood is required for efficient milk protein synthesis.

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EGF is a single-pass type I membrane protein,containing 8 LDL-receptor class B repeats and 9 EGF-like domains. EGF results in cellular proliferation, differentiation, and survival.EGF is a low-molecular-weight polypeptide first purified from the mouse submandibular gland, but since then found in many human tissues including submandibular gland, parotid gland. Salivary EGF, which seems also regulated by dietary inorganic iodine, also plays an important physiological role in the maintenance of oro-esophageal and gastric tissue integrity. The biological effects of salivary EGF include healing of oral and gastroesophageal ulcers, inhibition of gastric acid secretion, stimulation of DNA synthesis as well as mucosal protection from intraluminal injurious factors such as gastric acid, bile acids, pepsin, and trypsin and to physical, chemical and bacterial agents.

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Bone morphogenetic protein 2 (BMP-2) is a member of the BMP subgroup of the TGF-beta superfamily. It plays a dominant role in embryonic dorsalventral patterning, organogenesis, limb bud formation and bone formation and regeneration. BMP-2 signals through heterodimeric complexes composed of a type I receptor (Activin RI, BMP-RIA or BMP-RIB) and a type II receptor (BMP-RII or Activin RIIB). BMP-2 induces chondrocyte proliferation, endochondral bone formation, longitudinal bone growth and bone and cartilage repair. It induces ectopic bone formation or calcification by promoting osteogenic and chondrogenic differentiation in mesenchymal cells, stem cells and vascular smooth muscle cells. It also promotes the maintenance and repair of colonic epithelium, suppresses neuronal dopamine synthesis and release, induces apoptosis in medulloblastoma cells and is required for cardiac contractility.

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Interleukin 12 (IL-12p70) is a heterodimeric cytokine composed of p35 and p40 subunits. IL-12 is produced by monocytes, macrophages, dendritic cells, neutrophils, and B cells in response to bacterial products and cytokines such as IFN-γ. The IL-12 receptor is expressed on T, NK, and dendritic cells. Upon binding, IL-12 initiates signaling via the JAK/STAT signaling pathway and stimulates NK, B, and T cells to produce IFN-γ (Watford et al.). It also regulates cytokine synthesis, proliferation of T and NK cells, and stimulates differentiation of CD4+ and CD8+ T cells (Germann and Rüde). Mice that are deficient in IL-12 are susceptible to many intracellular pathogens and have impaired IFN-γ secretion, Th1 differentiation, and NK cytolytic activity; however, Th2 development and IL-4 production are enhanced (Watford et al.).

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Bone morphogenetic protein 2 (BMP-2) is a member of the BMP subgroup of the TGF-beta superfamily. It plays a dominant role in embryonic dorsalventral patterning, organogenesis, limb bud formation and bone formation and regeneration. BMP-2 signals through heterodimeric complexes composed of a type I receptor (Activin RI, BMP-RIA or BMP-RIB) and a type II receptor (BMP-RII or Activin RIIB). BMP-2 induces chondrocyte proliferation, endochondral bone formation, longitudinal bone growth and bone and cartilage repair. It induces ectopic bone formation or calcification by promoting osteogenic and chondrogenic differentiation in mesenchymal cells, stem cells and vascular smooth muscle cells. It also promotes the maintenance and repair of colonic epithelium, suppresses neuronal dopamine synthesis and release, induces apoptosis in medulloblastoma cells and is required for cardiac contractility.

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MHC Class I Polypeptide-Related Sequence A (MICA) is a transmembrane glycoprotein that functions as a ligand for human NKG2D. Unlike classical MHC class I molecules, MICA does not form a heterodimer with beta-2-microglobulin. MICA shares 85% amino acid identity with a closely related protein, MICB. MICA acts as a stress-induced self-antigen that is recognized by NK cells, NKT cells, and most of the subtypes of T cells. As a Ligand for the KLRK1/NKG2D receptor, MICA binds to KLRK1 leads to cell lysis. MICA functions as an antigen for gamma delta T cells and is frequently expressed in epithelial tumors. MICA antigens are able to elicit the synthesis of alloantibodies in transplant recipients. Studies have shown that anti-MICA antibodies are associated with acute renal allograft rejection and failure. MICA recognition is involved in tumor surveillance, viral infections, and autoimmune diseases.

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Midkine is a member of a unique family of heparin-binding growth factors that are structurally different from other fibroblast growth factors (Muramatsu; Takada et al.). Midkine is a proinflammatory cytokine, promoting the migration of leukocytes, fibrinolysis, and acting as a chemotactic agent towards neutrophils (Muramatsu; Said et al.; Takada et al.). It also regulates growth, differentiation, and development during the midgestion stage of embryogenesis, and promotes angiogenesis (Muramatsu; Said et al.; Takada et al.). The protein structure consists of three antiparallel β-sheets and is highly conserved between species (Muramatsu; Takada et al.). While the exact signal pathway is not known, proposed pathways include promoting LRP, inhibiting Src kinase, activating paxillin and STAT1α, activating PI2 and MAP kinases, suppressing caspases, binding to α6β1-integrin and tetraspanin, activating FAK, phosphorylating STAT3, suppressing STAT5 phosphorylation, activating ALK, activating PI3 kinase and transcription of NFkB, binding to neuroglycan C or nucleolin, and binding to eIF3 (Muramatsu). In cultured cells, midkine influences growth and survival of neural precursor cells, synthesis of cytokines from endothelial and renal epithelial cells, and promotes synthesis of extracellular matrices from fibroblasts (Muramatsu; Takada et al.).

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Fatty acid-binding protein 2 (FABP2), is also known as Fatty acid-binding protein, intestinal (FABPI), Intestinal-type fatty acid-binding protein (I-FABP). FABP2 belongs to the calycin superfamily and Fatty-acid binding protein (FABP) family. FABP2 / FABPI is expressed in the small intestine and at much lower levels in the large intestine and is highest expressed in the jejunum. FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters. FABP2 is probably involved in triglyceride-rich lipoprotein synthesis. FABP2 binds saturated long-chain fatty acids with a high affinity, but binds with a lower affinity to unsaturated long-chain fatty acids. FABP2 may also help maintain energy homeostasis by functioning as a lipid sensor.

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Bone morphogenetic protein 2 (BMP-2) is a member of the BMP subgroup of the TGF-beta superfamily. It plays a dominant role in embryonic dorsalventral patterning, organogenesis, limb bud formation and bone formation and regeneration. BMP-2 signals through heterodimeric complexes composed of a type I receptor (Activin RI, BMP-RIA or BMP-RIB) and a type II receptor (BMP-RII or Activin RIIB). BMP-2 induces chondrocyte proliferation, endochondral bone formation, longitudinal bone growth and bone and cartilage repair. It induces ectopic bone formation or calcification by promoting osteogenic and chondrogenic differentiation in mesenchymal cells, stem cells and vascular smooth muscle cells. It also promotes the maintenance and repair of colonic epithelium, suppresses neuronal dopamine synthesis and release, induces apoptosis in medulloblastoma cells and is required for cardiac contractility.

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Lipocalin-2 (LCN2) is also known as oncogene 24p3 or neutrophil gelatinase-associated lipocalin (NGAL), MSFI, The binding of lipocalin-2 to bacterial siderophores is important in the innate immune response to bacterial infection. Upon encountering invading bacteria the toll-like receptors on immune cells stimulate the synthesis and secretion of lipocalin-2. Secreted lipocalin-2 then limits bacterial growth by sequestering iron-containing siderophores. Lipocalin-2 also functions as a growth factor. LCN2 is strongly upregulated during inflammation and is upregulated by interleukin 1 (but not TNF alpha) in humans. There are indications that some forms of acne could be caused due to the gene not being transcribed, and that Isotretinoin corrects this. NFAT3 (NFATc4)NFAT by blocking the expression of LCN2 inhibits breast carcinoma cell motility. Recent studies have revealed that NGAL plays an important role in the physiopathology of chronic myeloid leukaemia (CML) mediated by BCR-ABL.