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Annals of Agricultural and... Dec 2021Human oxidative stress-induced growth inhibitor 1 (OSGIN1) is a protein identified in 2001 which belongs to the OKL38 protein family. The aim of the study was to...
INTRODUCTION AND OBJECTIVE
Human oxidative stress-induced growth inhibitor 1 (OSGIN1) is a protein identified in 2001 which belongs to the OKL38 protein family. The aim of the study was to investigate the levels of this protein depending on the severity of alcohol-induced liver cirrhosis.
MATERIAL AND METHODS
The study group consisted of 60 patients: 30 patients with cirrhosis in the P-Ch A and B stage and 30 in the P-Ch C stage. The control group consisted of 18 healthy individuals without liver diseases, who did not abuse alcohol. Oxidative stress induced growth inhibitor 1 (OSGIN1), fibroblast growth factor 1 (FGF1) and fibroblast growth factor 21 (FGF21) were determined in blood serum using enzyme-linked immunosorbent assay (ELISA) kits. All absorbance readings were conducted using an Epoch Microplate Spectrophotometer (BioTek Instrumentals, Inc., Winooski, VT, USA). OSGIN1, FGF1 and FGF21 concentrations were determined using Sandwich enzyme immunoassay kits (by Cloud Clone Corp., Katy, TX, USA). Statistica 13.3 (TIBCO Software, Inc.) was used for data analysis.
RESULTS
The concentration of OSGIN1 was 0.028 ± 0.017 in the control group which increased with the advancement of liver cirrhosis (stage of Pugh-Child): 0.075 ± 0.098 in the P-Ch A + B group and 0.121 ± 0.134 in the P-Ch C stage. Multiple comparison tests confirmed statistically significant differences in OSGIN1 concentration between the control group and P-Ch C (p <0.02). Significant correlations were noted between OSGIN1 and FGF1 (r = 0.39; p = 0.004) and between OSGIN1 and FGF21 (r = 0.53; p <0.0001).
CONCLUSIONS
The study revealed that the level of OSGIN1 increased significantly in the P-Ch C stage of liver cirrhosis. It is possible that OSGIN1 may be used for the non-invasive diagnosis of ALD, but its possible diagnostic value is still very uncertain.
Topics: Child; Fibrosis; Growth Inhibitors; Humans; Liver Cirrhosis; Liver Cirrhosis, Alcoholic; Oxidative Stress
PubMed: 34969228
DOI: 10.26444/aaem/144380 -
Cancer Treatment and Research 1992
Comparative Study Review
Topics: Amino Acid Sequence; Animals; Arachidonic Acids; Carcinoma, Ehrlich Tumor; Carrier Proteins; Cattle; Cell Differentiation; Cell Division; Cell Nucleus; Epithelium; Fatty Acid Binding Protein 3; Fatty Acid-Binding Protein 7; Fatty Acid-Binding Proteins; Female; Gene Expression Regulation; Growth Inhibitors; Lipid Metabolism; Mammary Glands, Animal; Mice; Molecular Sequence Data; Multigene Family; Neoplasm Proteins; Nerve Tissue Proteins; Organ Specificity; Peptides; Pregnancy; Rats; Receptors, Adrenergic, beta; Sequence Alignment; Sequence Homology; Stem Cells
PubMed: 1360246
DOI: 10.1007/978-1-4615-3500-3_5 -
Targeted Oncology Mar 2012Vascular endothelial growth inhibitor (VEGI), also known as tumor necrosis factor superfamily member 15 or TNF ligand-related molecule 1, is identified as one kind of... (Review)
Review
Vascular endothelial growth inhibitor (VEGI), also known as tumor necrosis factor superfamily member 15 or TNF ligand-related molecule 1, is identified as one kind of antiangiogenic cytokine that belongs to the tumor necrosis factor superfamily. VEGI includes three isoforms: VEGI-174, VEGI-192, and VEGI-251. VEGI can activate multiple signaling pathways including nuclear factor-kappaB, c-Jun N-terminal kinase, and p38 mitogen-activated protein kinase. Moreover, it suppresses endothelial cell proliferation, angiopoiesis, and tumor growth. Genetic engineering techniques have been used to produce recombinant human vascular endothelial growth inhibitor, and great progress has been made in its application for curing cancer. VEGI could serve as a potential target in the development of angiogenesis-based cancer therapy, and this paper briefly summarizes the progress of the research on VEGI.
Topics: Animals; Antineoplastic Agents; Clinical Trials as Topic; Endothelial Cells; Genetic Engineering; Growth Inhibitors; Humans; Neoplasms; Neovascularization, Pathologic; Protein Isoforms; Signal Transduction; Tumor Necrosis Factor Ligand Superfamily Member 15
PubMed: 22388993
DOI: 10.1007/s11523-012-0206-0 -
Neuron Glia Biology May 2008Nogo-A is possibly the best characterized myelin-derived inhibitor of nerve growth in the adult central nervous system (CNS). It is a member of the ancient reticulon... (Review)
Review
Nogo-A is possibly the best characterized myelin-derived inhibitor of nerve growth in the adult central nervous system (CNS). It is a member of the ancient reticulon family of mainly endoplasmic reticulum resident proteins with representatives found throughout the eukaryotic domain. Orthologs of the nogo gene were identified in tetrapods and teleost fish but none have been detected in invertebrates. Evolution of the nogo gene has been non-homogeneous. The exon-intron arrangement is conserved from amphibians (Xenopus) to mammals, but partly deviates from that found in several teleost fish species, indicating that the recruitment of nogo exons proceeded along at least two independent lines during early vertebrate evolution. This might have far-reaching consequences. Tetrapod nogo orthologs encode two neurite growth inhibitory domains whereas in fish nogo only one of the inhibitory domains is present. These distinct paths in nogo evolution have potentially contributed to the regeneration permissive CNS in fish as opposed to the non-regenerating CNS in higher vertebrates.
Topics: Animals; Axons; Central Nervous System; Evolution, Molecular; Fishes; Genomics; Growth Inhibitors; Myelin Proteins; Nerve Regeneration; Neurites; Neuronal Plasticity; Nogo Proteins; Vertebrates
PubMed: 19737432
DOI: 10.1017/S1740925X09990147 -
Molecular Endocrinology (Baltimore, Md.) Aug 2012Androgen receptor (AR) signaling exerts an antiestrogenic, growth-inhibitory influence in normal breast tissue, and this role may be sustained in estrogen receptor α... (Review)
Review
Androgen receptor (AR) signaling exerts an antiestrogenic, growth-inhibitory influence in normal breast tissue, and this role may be sustained in estrogen receptor α (ERα)-positive luminal breast cancers. Conversely, AR signaling may promote growth of a subset of ERα-negative, AR-positive breast cancers with a molecular apocrine phenotype. Understanding the molecular mechanisms whereby androgens can elicit distinct gene expression programs and opposing proliferative responses in these two breast cancer phenotypes is critical to the development of new therapeutic strategies to target the AR in breast cancer.
Topics: Androgens; Animals; Breast Neoplasms; Estrogen Receptor alpha; Female; Genes, Tumor Suppressor; Growth Inhibitors; Humans; Mammary Glands, Human; Oncogenes; Receptors, Androgen; Signal Transduction
PubMed: 22745190
DOI: 10.1210/me.2012-1107 -
ACS Infectious Diseases Nov 2022Metabolic profiling of the extracts from a library of actinobacteria led to the identification of a novel polyketide, demurilactone A, produced by strain DEM21308. The...
Metabolic profiling of the extracts from a library of actinobacteria led to the identification of a novel polyketide, demurilactone A, produced by strain DEM21308. The structure of the compound was assigned based on a detailed investigation of 1D/2D NMR spectra and HR-MS. Whole genome DNA sequencing, followed by bioinformatics analysis and insertional mutagenesis, identified type I polyketide synthases encoded by the gene cluster to direct the biosynthesis of this polyene macrolide. While the number of modules is consistent with the carbon backbone of the assigned structure, some discrepancies were identified in the domain organization of five modules. Close investigation of the amino acid sequences identified several mutations in the conserved motifs of nonfunctional domains. Furthermore, the absolute configuration of hydroxy-bearing stereocenters was proposed based on analyses of the ketoreductase domains. Remarkably, although demurilactone A has little detectable activity against normal-walled bacteria, it specifically inhibits the growth of cell wall-deficient "L-form" at a minimum inhibitory concentration value of 16 μg/mL. Time-lapse microscopy analyses revealed that demurilactone affects membrane dynamics, probably by reducing membrane fluidity. This compound could be a powerful reagent for studying long-standing questions about the involvement of L-forms in recurrent infection.
Topics: Bacillus subtilis; Growth Inhibitors; Polyketide Synthases; Streptomyces; Macrolides
PubMed: 36268971
DOI: 10.1021/acsinfecdis.2c00220 -
Glia Jan 2000
Review
Topics: Alternative Splicing; Animals; Antibodies, Monoclonal; Cattle; Cell Division; Central Nervous System; Cloning, Molecular; Fishes; Growth Cones; Growth Inhibitors; Membrane Proteins; Myelin Proteins; Myelin Sheath; Nerve Fibers; Nerve Regeneration; Neurites; Neuronal Plasticity; Nogo Proteins; Rats
PubMed: 10625336
DOI: 10.1002/(sici)1098-1136(20000115)29:2<175::aid-glia11>3.0.co;2-f -
Molecular and Cellular BiochemistryBased on sequence relationships the cytoplasmic fatty acid-binding proteins (FABPs) of mammalian origin are divided into at least three distinct types, namely the... (Review)
Review
Based on sequence relationships the cytoplasmic fatty acid-binding proteins (FABPs) of mammalian origin are divided into at least three distinct types, namely the hepatic-, intestinal- and cardiac-type. Highly conserved sequences of FABPs within the same type correlate with immunological crossreactivities. Isoforms of hepatic-type FABP are found in several mammalian species and for bovine liver FABP specific shifts in isoelectric points upon lipidation with fatty acids are observed. Isoforms of intestinal-type FABP are not known and the occurrence of cardiac-type isoforms so far is confined to bovine heart tissue. A bovine mammary-derived growth inhibitor (MDGI) is 95% homologous to the cardiac-type FABP from bovine heart. Dissociation constants of FABP/fatty acid complexes are in the range of 1 microM and 1:1 stoichiometries are usually found, but the neutral isoform of hepatic FABP from bovine liver binds 2 fatty acids. On subcellular levels hepatic- and cardiac-type FABPs are differently distributed. Though mainly cytosolic in either case, immunoelectron microscopy as well as a gelchromatographic immunofluorescence assay demonstrate the association of hepatic FABP in liver cells with microsomal and outer mitochondrial membranes and with nuclei, whereas in heart cells cardiac FABP is confined to mitochondrial matrix and nuclei. In mammary epithelial cells MDGI is associated with neither mitochondria nor endoplasmic reticulum, and is expressed in a strictly developmental-dependent spatial and temporal pattern. The specific role proposed for MDGI is to arrest growth of mammary epithelial cells when they become committed to differentiation in the mammary gland.
Topics: Amino Acid Sequence; Animals; Carrier Proteins; Fatty Acid Binding Protein 3; Fatty Acid-Binding Proteins; Growth Inhibitors; Isomerism; Ligands; Molecular Sequence Data; Neoplasm Proteins; Peptides; Subcellular Fractions
PubMed: 2266970
DOI: 10.1007/BF00231368 -
Transactions of the Association of... 1991These studies demonstrate that mevalonate or the mevalonate phosphates play a number of regulatory roles in cellular proliferation. They are not only required for cell... (Review)
Review
These studies demonstrate that mevalonate or the mevalonate phosphates play a number of regulatory roles in cellular proliferation. They are not only required for cell growth but are also a source of an inhibitor of cell growth. Endogenous concentrations of mevalonate and the mevalonate phosphates are thus critical determinants of cellular proliferation.
Topics: Cell Division; Growth Inhibitors; Growth Substances; Humans; In Vitro Techniques; Lipid Metabolism; Mevalonic Acid; Proteins
PubMed: 1845160
DOI: No ID Found -
Proceedings of the National Academy of... Aug 1986Growth inhibitor/type beta transforming growth factor purified from BSC-1 cells and human platelets is shown to strongly inhibit the proliferation of Con A-stimulated...
Growth inhibitor/type beta transforming growth factor purified from BSC-1 cells and human platelets is shown to strongly inhibit the proliferation of Con A-stimulated mouse thymocytes. The inhibition can be achieved with growth inhibitor/type beta transforming growth factor concentrations approximately equal to 1/10th those necessary to inhibit keratinocyte cultures. The inhibitory effect in thymocyte cultures can be reversed by the addition of interleukin 2. These findings suggest that growth inhibitor/type beta transforming growth factor is a naturally occurring immunoregulator.
Topics: Animals; Cell Line; Chlorocebus aethiops; Growth Inhibitors; Interleukin-2; Lymphocyte Activation; Lymphocytes; Mice; Peptides; Skin; Transforming Growth Factors
PubMed: 3488549
DOI: 10.1073/pnas.83.15.5531