A group of compounds containing the porphin structure, four pyrrole rings connected by methine bridges in a cyclic configuration to which a variety of side chains are attached. The nature of the side chain is indicated by a prefix, as uroporphyrin, hematoporphyrin, etc. The porphyrins, in combination with iron, form the heme component in biologically significant compounds such as hemoglobin and myoglobin.
Transforming proteins coded by sis oncogenes. Transformation of cells by v-sis is related to its interaction with the PDGF receptor and also its ability to alter other transcription factors.
The GENETIC TRANSLATION product from a GENE FUSION between a sequence from the tpr protein gene on the human CHROMOSOME 1 and the gene for PROTO-ONCOGENE PROTEINS C-MET.
An oncogene protein that was originally isolated from a spontaneous musculo-aponeurotic FIBROSARCOMA in CHICKEN and shown to be the transforming gene of the avian retrovirus AS42. It is a basic leucine zipper TRANSCRIPTION FACTOR and the founding member of the MAF TRANSCRIPTION FACTORS.
Transforming glycoprotein coded by the fms oncogene from the Susan McDonough strain of feline sarcoma virus (SM-FeSV). The oncogene protein v-fms lacks sequences, which, in the highly homologous proto-oncogene protein c-fms (CSF-1 receptor), normally serve to regulate its tyrosine kinase activity. The missing sequences in v-fms mimic the effect of ligand and lead to constitutive cell growth. The protein gp120(v-fms) is post-translationally modified to generate gp140(v-fms).
Transforming proteins coded by mos oncogenes. The v-mos proteins were originally isolated from the Moloney murine sarcoma virus (Mo-MSV).
Transforming protein coded by myc oncogenes. The v-myc protein has been found in several replication-defective avian retrovirus isolates which induce a broad spectrum of malignancies.
Transforming protein coded by jun oncogenes (GENES, JUN). This is a gag-onc fusion protein of about 65 kDa derived from avian sarcoma virus. v-jun lacks a negative regulatory domain that regulates transcription in c-jun.
A family of transforming proteins isolated from retroviruses such as MOUSE SARCOMA VIRUSES. They are viral-derived members of the raf-kinase family of serine-theonine kinases.
Transforming proteins coded by fos oncogenes. These proteins have been found in the Finkel-Biskis-Jinkins (FBJ-MSV) and Finkel-Biskis-Reilly (FBR-MSV) murine sarcoma viruses which induce osteogenic sarcomas in mice. The FBJ-MSV v-fos gene encodes a p55-kDa protein and the FBR-MSV v-fos gene encodes a p75-kDa fusion protein.
A signal transducing adaptor protein that is encoded by the crk ONCOGENE from TYPE C AVIAN RETROVIRUSES. It contains SRC HOMOLOGY DOMAINS and is closely related to its cellular homolog, PROTO-ONCOGENE PROTEIN C-CRK.
Transforming proteins coded by myb oncogenes. Transformation of cells by v-myb in conjunction with v-ets is seen in the avian E26 leukemia virus.
An oncoprotein from the Cas NS-1 murine retrovirus that induces pre- B-CELL LYMPHOMA and MYELOID LEUKEMIAS. v-cbl protein is a tyrosine-phosphorylated, truncated form of its cellular homologue, PROTO-ONCOGENE PROTEIN C-CBL.
Transforming proteins encoded by erbB oncogenes from the avian erythroblastosis virus. The protein is a truncated form of the EGF receptor (RECEPTOR, EPIDERMAL GROWTH FACTOR) whose kinase domain is constitutively activated by deletion of the ligand-binding domain.
Transforming proteins encoded by the abl oncogenes. Oncogenic transformation of c-abl to v-abl occurs by insertional activation that results in deletions of specific N-terminal amino acids.
Genes whose gain-of-function alterations lead to NEOPLASTIC CELL TRANSFORMATION. They include, for example, genes for activators or stimulators of CELL PROLIFERATION such as growth factors, growth factor receptors, protein kinases, signal transducers, nuclear phosphoproteins, and transcription factors. A prefix of "v-" before oncogene symbols indicates oncogenes captured and transmitted by RETROVIRUSES; the prefix "c-" before the gene symbol of an oncogene indicates it is the cellular homolog (PROTO-ONCOGENES) of a v-oncogene.
Transforming proteins coded by rel oncogenes. The v-rel protein competes with rel-related proteins and probably transforms cells by acting as a dominant negative version of c-rel. This results in the induction of a broad range of leukemias and lymphomas.
Transforming proteins encoded by erbA oncogenes from the avian erythroblastosis virus. They are truncated versions of c-erbA, the thyroid hormone receptor (RECEPTORS, THYROID HORMONE) that have retained both the DNA-binding and hormone-binding domains. Mutations in the hormone-binding domains abolish the transcriptional activation function. v-erbA acts as a dominant repressor of c-erbA, inducing transformation by disinhibiting proliferation.
Proteins coded by oncogenes. They include proteins resulting from the fusion of an oncogene and another gene (ONCOGENE PROTEINS, FUSION).
Transforming protein encoded by ras oncogenes. Point mutations in the cellular ras gene (c-ras) can also result in a mutant p21 protein that can transform mammalian cells. Oncogene protein p21(ras) has been directly implicated in human neoplasms, perhaps accounting for as much as 15-20% of all human tumors. This enzyme was formerly listed as EC
A tyrosine-specific protein kinase encoded by the v-src oncogene of ROUS SARCOMA VIRUS. The transforming activity of pp60(v-src) depends on both the lack of a critical carboxy-terminal tyrosine phosphorylation site at position 527, and the attachment of pp60(v-src) to the plasma membrane which is accomplished by myristylation of its N-terminal glycine.
Products of viral oncogenes, most commonly retroviral oncogenes. They usually have transforming and often protein kinase activities.
The GENETIC TRANSLATION products of the fusion between an ONCOGENE and another gene. The latter may be of viral or cellular origin.
Family of retrovirus-associated DNA sequences (ras) originally isolated from Harvey (H-ras, Ha-ras, rasH) and Kirsten (K-ras, Ki-ras, rasK) murine sarcoma viruses. Ras genes are widely conserved among animal species and sequences corresponding to both H-ras and K-ras genes have been detected in human, avian, murine, and non-vertebrate genomes. The closely related N-ras gene has been detected in human neuroblastoma and sarcoma cell lines. All genes of the family have a similar exon-intron structure and each encodes a p21 protein.
A viral oncoprotein originally isolated from a murine T CELL LYMPHOMA infected with the acutely transforming retrovirus AKT8. v-akt protein is the viral homologue of PROTO-ONCOGENE PROTEINS C-AKT.
Cell changes manifested by escape from control mechanisms, increased growth potential, alterations in the cell surface, karyotypic abnormalities, morphological and biochemical deviations from the norm, and other attributes conferring the ability to invade, metastasize, and kill.
Normal cellular genes homologous to viral oncogenes. The products of proto-oncogenes are important regulators of biological processes and appear to be involved in the events that serve to maintain the ordered procession through the cell cycle. Proto-oncogenes have names of the form c-onc.
Products of proto-oncogenes. Normally they do not have oncogenic or transforming properties, but are involved in the regulation or differentiation of cell growth. They often have protein kinase activity.
Family of retrovirus-associated DNA sequences (myc) originally isolated from an avian myelocytomatosis virus. The proto-oncogene myc (c-myc) codes for a nuclear protein which is involved in nucleic acid metabolism and in mediating the cellular response to growth factors. Truncation of the first exon, which appears to regulate c-myc expression, is crucial for tumorigenicity. The human c-myc gene is located at 8q24 on the long arm of chromosome 8.
A selective increase in the number of copies of a gene coding for a specific protein without a proportional increase in other genes. It occurs naturally via the excision of a copy of the repeating sequence from the chromosome and its extrachromosomal replication in a plasmid, or via the production of an RNA transcript of the entire repeating sequence of ribosomal RNA followed by the reverse transcription of the molecule to produce an additional copy of the original DNA sequence. Laboratory techniques have been introduced for inducing disproportional replication by unequal crossing over, uptake of DNA from lysed cells, or generation of extrachromosomal sequences from rolling circle replication.
Cellular DNA-binding proteins encoded by the c-myc genes. They are normally involved in nucleic acid metabolism and in mediating the cellular response to growth factors. Elevated and deregulated (constitutive) expression of c-myc proteins can cause tumorigenesis.
Cellular proteins encoded by the H-ras, K-ras and N-ras genes. The proteins have GTPase activity and are involved in signal transduction as monomeric GTP-binding proteins. Elevated levels of p21 c-ras have been associated with neoplasia. This enzyme was formerly listed as EC
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in neoplastic tissue.
Retroviral proteins that have the ability to transform cells. They can induce sarcomas, leukemias, lymphomas, and mammary carcinomas. Not all retroviral proteins are oncogenic.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
An inheritable change in cells manifested by changes in cell division and growth and alterations in cell surface properties. It is induced by infection with a transforming virus.
The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.
Established cell cultures that have the potential to propagate indefinitely.
Eukaryotic cell line obtained in a quiescent or stationary phase which undergoes conversion to a state of unregulated growth in culture, resembling an in vitro tumor. It occurs spontaneously or through interaction with viruses, oncogenes, radiation, or drugs/chemicals.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
A cell line derived from cultured tumor cells.
The erbB-2 gene is a proto-oncogene that codes for the erbB-2 receptor (RECEPTOR, ERBB-2), a protein with structural features similar to the epidermal growth factor receptor. Its name originates from the viral oncogene homolog (v-erbB) which is a truncated form of the chicken erbB gene found in the avian erythroblastosis virus. Overexpression and amplification of the gene is associated with a significant number of adenocarcinomas. The human c-erbB-2 gene is located at 17q21.2.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
Cells grown in vitro from neoplastic tissue. If they can be established as a TUMOR CELL LINE, they can be propagated in cell culture indefinitely.
Small, monomeric GTP-binding proteins encoded by ras genes (GENES, RAS). The protooncogene-derived protein, PROTO-ONCOGENE PROTEIN P21(RAS), plays a role in normal cellular growth, differentiation and development. The oncogene-derived protein (ONCOGENE PROTEIN P21(RAS)) can play a role in aberrant cellular regulation during neoplastic cell transformation (CELL TRANSFORMATION, NEOPLASTIC). This enzyme was formerly listed as EC
The fission of a CELL. It includes CYTOKINESIS, when the CYTOPLASM of a cell is divided, and CELL NUCLEUS DIVISION.
RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.
The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.
The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.
DNA present in neoplastic tissue.
A cell surface protein-tyrosine kinase receptor that is overexpressed in a variety of ADENOCARCINOMAS. It has extensive homology to and heterodimerizes with the EGF RECEPTOR, the ERBB-3 RECEPTOR, and the ERBB-4 RECEPTOR. Activation of the erbB-2 receptor occurs through heterodimer formation with a ligand-bound erbB receptor family member.
A type of chromosome aberration characterized by CHROMOSOME BREAKAGE and transfer of the broken-off portion to another location, often to a different chromosome.
Cell lines whose original growing procedure consisted being transferred (T) every 3 days and plated at 300,000 cells per plate (J Cell Biol 17:299-313, 1963). Lines have been developed using several different strains of mice. Tissues are usually fibroblasts derived from mouse embryos but other types and sources have been developed as well. The 3T3 lines are valuable in vitro host systems for oncogenic virus transformation studies, since 3T3 cells possess a high sensitivity to CONTACT INHIBITION.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control (induction or repression) of gene action at the level of transcription or translation.
Mutant mice homozygous for the recessive gene "nude" which fail to develop a thymus. They are useful in tumor studies and studies on immune responses.
Proteins found in the nucleus of a cell. Do not confuse with NUCLEOPROTEINS which are proteins conjugated with nucleic acids, that are not necessarily present in the nucleus.
Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process.
Protein kinases that catalyze the PHOSPHORYLATION of TYROSINE residues in proteins with ATP or other nucleotides as phosphate donors.
Family of RNA viruses that infects birds and mammals and encodes the enzyme reverse transcriptase. The family contains seven genera: DELTARETROVIRUS; LENTIVIRUS; RETROVIRUSES TYPE B, MAMMALIAN; ALPHARETROVIRUS; GAMMARETROVIRUS; RETROVIRUSES TYPE D; and SPUMAVIRUS. A key feature of retrovirus biology is the synthesis of a DNA copy of the genome which is integrated into cellular DNA. After integration it is sometimes not expressed but maintained in a latent state (PROVIRUSES).
Laboratory mice that have been produced from a genetically manipulated EGG or EMBRYO, MAMMALIAN.
Proteins which bind to DNA. The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases.
Nuclear phosphoprotein encoded by the p53 gene (GENES, P53) whose normal function is to control CELL PROLIFERATION and APOPTOSIS. A mutant or absent p53 protein has been found in LEUKEMIA; OSTEOSARCOMA; LUNG CANCER; and COLORECTAL CANCER.
Connective tissue cells which secrete an extracellular matrix rich in collagen and other macromolecules.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
The GENETIC RECOMBINATION of the parts of two or more GENES, including an ONCOGENE as at least one of the fusion partners. Such gene fusions are often detected in neoplastic cells and are transcribed into ONCOGENE FUSION PROTEINS.
Proteins whose abnormal expression (gain or loss) are associated with the development, growth, or progression of NEOPLASMS. Some neoplasm proteins are tumor antigens (ANTIGENS, NEOPLASM), i.e. they induce an immune reaction to their tumor. Many neoplasm proteins have been characterized and are used as tumor markers (BIOMARKERS, TUMOR) when they are detectable in cells and body fluids as monitors for the presence or growth of tumors. Abnormal expression of ONCOGENE PROTEINS is involved in neoplastic transformation, whereas the loss of expression of TUMOR SUPPRESSOR PROTEINS is involved with the loss of growth control and progression of the neoplasm.
All of the processes involved in increasing CELL NUMBER including CELL DIVISION.
Retrovirus-associated DNA sequences (src) originally isolated from the Rous sarcoma virus (RSV). The proto-oncogene src (c-src) codes for a protein that is a member of the tyrosine kinase family and was the first proto-oncogene identified in the human genome. The human c-src gene is located at 20q12-13 on the long arm of chromosome 20.
A group of replication-defective viruses, in the genus GAMMARETROVIRUS, which are capable of transforming cells, but which replicate and produce tumors only in the presence of Murine leukemia viruses (LEUKEMIA VIRUS, MURINE).
One of the mechanisms by which CELL DEATH occurs (compare with NECROSIS and AUTOPHAGOCYTOSIS). Apoptosis is the mechanism responsible for the physiological deletion of cells and appears to be intrinsically programmed. It is characterized by distinctive morphologic changes in the nucleus and cytoplasm, chromatin cleavage at regularly spaced sites, and the endonucleolytic cleavage of genomic DNA; (DNA FRAGMENTATION); at internucleosomal sites. This mode of cell death serves as a balance to mitosis in regulating the size of animal tissues and in mediating pathologic processes associated with tumor growth.
The type species of ALPHARETROVIRUS producing latent or manifest lymphoid leukosis in fowl.
DNA sequences which are recognized (directly or indirectly) and bound by a DNA-dependent RNA polymerase during the initiation of transcription. Highly conserved sequences within the promoter include the Pribnow box in bacteria and the TATA BOX in eukaryotes.
Translation products of a fusion gene derived from CHROMOSOMAL TRANSLOCATION of C-ABL GENES to the genetic locus of the breakpoint cluster region gene on chromosome 22. Several different variants of the bcr-abl fusion proteins occur depending upon the precise location of the chromosomal breakpoint. These variants can be associated with distinct subtypes of leukemias such as PRECURSOR CELL LYMPHOBLASTIC LEUKEMIA-LYMPHOMA; LEUKEMIA, MYELOGENOUS, CHRONIC, BCR-ABL POSITIVE; and NEUTROPHILIC LEUKEMIA, CHRONIC.
The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.
A replication-defective mouse sarcoma virus (SARCOMA VIRUSES, MURINE) first described by J.J. Harvey in 1964.
Proteins transcribed from the E1A genome region of ADENOVIRUSES which are involved in positive regulation of transcription of the early genes of host infection.
Polyomavirus antigens which cause infection and cellular transformation. The large T antigen is necessary for the initiation of viral DNA synthesis, repression of transcription of the early region and is responsible in conjunction with the middle T antigen for the transformation of primary cells. Small T antigen is necessary for the completion of the productive infection cycle.
Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.

Stromal cells mediate retinoid-dependent functions essential for renal development. (1/24774)

The essential role of vitamin A and its metabolites, retinoids, in kidney development has been demonstrated in vitamin A deficiency and gene targeting studies. Retinoids signal via nuclear transcription factors belonging to the retinoic acid receptor (RAR) and retinoid X receptor (RXR) families. Inactivation of RARaplpha and RARbeta2 receptors together, but not singly, resulted in renal malformations, suggesting that within a given renal cell type, their concerted function is required for renal morphogenesis. At birth, RARalpha beta2(-) mutants displayed small kidneys, containing few ureteric bud branches, reduced numbers of nephrons and lacking the nephrogenic zone where new nephrons are continuously added. These observations have prompted us to investigate the role of RARalpha and RARbeta2 in renal development in detail. We have found that within the embryonic kidney, RARalpha and RARbeta2 are colocalized in stromal cells, but not in other renal cell types, suggesting that stromal cells mediate retinoid-dependent functions essential for renal development. Analysis of RARalpha beta2(-) mutant kidneys at embryonic stages revealed that nephrons were formed and revealed no changes in the intensity or distribution of molecular markers specific for different metanephric mesenchymal cell types. In contrast the development of the collecting duct system was greatly impaired in RARalpha beta2(-) mutant kidneys. Fewer ureteric bud branches were present, and ureteric bud ends were positioned abnormally, at a distance from the renal capsule. Analysis of genes important for ureteric bud morphogenesis revealed that the proto-oncogene c-ret was downregulated. Our results suggest that RARalpha and RARbeta2 are required for generating stromal cell signals that maintain c-ret expression in the embryonic kidney. Since c-ret signaling is required for ureteric bud morphogenesis, loss of c-ret expression is a likely cause of impaired ureteric bud branching in RARalpha beta2(-) mutants.  (+info)

VEGF is required for growth and survival in neonatal mice. (2/24774)

We employed two independent approaches to inactivate the angiogenic protein VEGF in newborn mice: inducible, Cre-loxP- mediated gene targeting, or administration of mFlt(1-3)-IgG, a soluble VEGF receptor chimeric protein. Partial inhibition of VEGF achieved by inducible gene targeting resulted in increased mortality, stunted body growth and impaired organ development, most notably of the liver. Administration of mFlt(1-3)-IgG, which achieves a higher degree of VEGF inhibition, resulted in nearly complete growth arrest and lethality. Ultrastructural analysis documented alterations in endothelial and other cell types. Histological and biochemical changes consistent with liver and renal failure were observed. Endothelial cells isolated from the liver of mFlt(1-3)-IgG-treated neonates demonstrated an increased apoptotic index, indicating that VEGF is required not only for proliferation but also for survival of endothelial cells. However, such treatment resulted in less significant alterations as the animal matured, and the dependence on VEGF was eventually lost some time after the fourth postnatal week. Administration of mFlt(1-3)-IgG to juvenile mice failed to induce apoptosis in liver endothelial cells. Thus, VEGF is essential for growth and survival in early postnatal life. However, in the fully developed animal, VEGF is likely to be involved primarily in active angiogenesis processes such as corpus luteum development.  (+info)

FGF8 induces formation of an ectopic isthmic organizer and isthmocerebellar development via a repressive effect on Otx2 expression. (3/24774)

Beads containing recombinant FGF8 (FGF8-beads) were implanted in the prospective caudal diencephalon or midbrain of chick embryos at stages 9-12. This induced the neuroepithelium rostral and caudal to the FGF8-bead to form two ectopic, mirror-image midbrains. Furthermore, cells in direct contact with the bead formed an outgrowth that protruded laterally from the neural tube. Tissue within such lateral outgrowths developed proximally into isthmic nuclei and distally into a cerebellum-like structure. These morphogenetic effects were apparently due to FGF8-mediated changes in gene expression in the vicinity of the bead, including a repressive effect on Otx2 and an inductive effect on En1, Fgf8 and Wnt1 expression. The ectopic Fgf8 and Wnt1 expression domains formed nearly complete concentric rings around the FGF8-bead, with the Wnt1 ring outermost. These observations suggest that FGF8 induces the formation of a ring-like ectopic signaling center (organizer) in the lateral wall of the brain, similar to the one that normally encircles the neural tube at the isthmic constriction, which is located at the boundary between the prospective midbrain and hindbrain. This ectopic isthmic organizer apparently sends long-range patterning signals both rostrally and caudally, resulting in the development of the two ectopic midbrains. Interestingly, our data suggest that these inductive signals spread readily in a caudal direction, but are inhibited from spreading rostrally across diencephalic neuromere boundaries. These results provide insights into the mechanism by which FGF8 induces an ectopic organizer and suggest that a negative feedback loop between Fgf8 and Otx2 plays a key role in patterning the midbrain and anterior hindbrain.  (+info)

A Wnt5a pathway underlies outgrowth of multiple structures in the vertebrate embryo. (4/24774)

Morphogenesis depends on the precise control of basic cellular processes such as cell proliferation and differentiation. Wnt5a may regulate these processes since it is expressed in a gradient at the caudal end of the growing embryo during gastrulation, and later in the distal-most aspect of several structures that extend from the body. A loss-of-function mutation of Wnt5a leads to an inability to extend the A-P axis due to a progressive reduction in the size of caudal structures. In the limbs, truncation of the proximal skeleton and absence of distal digits correlates with reduced proliferation of putative progenitor cells within the progress zone. However, expression of progress zone markers, and several genes implicated in distal outgrowth and patterning including Distalless, Hoxd and Fgf family members was not altered. Taken together with the outgrowth defects observed in the developing face, ears and genitals, our data indicates that Wnt5a regulates a pathway common to many structures whose development requires extension from the primary body axis. The reduced number of proliferating cells in both the progress zone and the primitive streak mesoderm suggests that one function of Wnt5a is to regulate the proliferation of progenitor cells.  (+info)

Membrane-tethered Drosophila Armadillo cannot transduce Wingless signal on its own. (5/24774)

Drosophila Armadillo and its vertebrate homolog beta-catenin are key effectors of Wingless/Wnt signaling. In the current model, Wingless/Wnt signal stabilizes Armadillo/beta-catenin, which then accumulates in nuclei and binds TCF/LEF family proteins, forming bipartite transcription factors which activate transcription of Wingless/Wnt responsive genes. This model was recently challenged. Overexpression in Xenopus of membrane-tethered beta-catenin or its paralog plakoglobin activates Wnt signaling, suggesting that nuclear localization of Armadillo/beta-catenin is not essential for signaling. Tethered plakoglobin or beta-catenin might signal on their own or might act indirectly by elevating levels of endogenous beta-catenin. We tested these hypotheses in Drosophila by removing endogenous Armadillo. We generated a series of mutant Armadillo proteins with altered intracellular localizations, and expressed these in wild-type and armadillo mutant backgrounds. We found that membrane-tethered Armadillo cannot signal on its own; however it can function in adherens junctions. We also created mutant forms of Armadillo carrying heterologous nuclear localization or nuclear export signals. Although these signals alter the subcellular localization of Arm when overexpressed in Xenopus, in Drosophila they have little effect on localization and only subtle effects on signaling. This supports a model in which Armadillo's nuclear localization is key for signaling, but in which Armadillo intracellular localization is controlled by the availability and affinity of its binding partners.  (+info)

Intracellular signalling: PDK1--a kinase at the hub of things. (6/24774)

Phosphoinositide-dependent kinase 1 (PDK1) is at the hub of many signalling pathways, activating PKB and PKC isoenzymes, as well as p70 S6 kinase and perhaps PKA. PDK1 action is determined by colocalization with substrate and by target site availability, features that may enable it to operate in both resting and stimulated cells.  (+info)

Alzheimer's disease: clues from flies and worms. (7/24774)

Presenilin mutations give rise to familial Alzheimer's disease and result in elevated production of amyloid beta peptide. Recent evidence that presenilins act in developmental signalling pathways may be the key to understanding how senile plaques, neurofibrillary tangles and apoptosis are all biochemically linked.  (+info)

Concomitant activation of pathways downstream of Grb2 and PI 3-kinase is required for MET-mediated metastasis. (8/24774)

The Met tyrosine kinase - the HGF receptor - induces cell transformation and metastasis when constitutively activated. Met signaling is mediated by phosphorylation of two carboxy-terminal tyrosines which act as docking sites for a number of SH2-containing molecules. These include Grb2 and p85 which couple the receptor, respectively, with Ras and PI 3-kinase. We previously showed that a Met mutant designed to obtain preferential coupling with Grb2 (Met2xGrb2) is permissive for motility, increases transformation, but - surprisingly - is impaired in causing invasion and metastasis. In this work we used Met mutants optimized for binding either p85 alone (Met2xPI3K) or p85 and Grb2 (MetPI3K/Grb2) to evaluate the relative importance of Ras and PI 3-kinase as downstream effectors of Met. Met2xPI3K was competent in eliciting motility, but not transformation, invasion, or metastasis. Conversely, MetP13K/Grb2 induced motility, transformation, invasion and metastasis as efficiently as wild type Met. Furthermore, the expression of constitutively active PI 3-kinase in cells transformed by the Met2xGrb2 mutant, fully rescued their ability to invade and metastasize. These data point to a central role for PI 3-kinase in Met-mediated invasiveness, and indicate that simultaneous activation of Ras and PI 3-kinase is required to unleash the Met metastatic potential.  (+info)

Porphyrins are complex organic compounds that contain four pyrrole rings joined together by methine bridges (=CH-). They play a crucial role in the biochemistry of many organisms, as they form the core structure of various heme proteins and other metalloproteins. Some examples of these proteins include hemoglobin, myoglobin, cytochromes, and catalases, which are involved in essential processes such as oxygen transport, electron transfer, and oxidative metabolism.

In the human body, porphyrins are synthesized through a series of enzymatic reactions known as the heme biosynthesis pathway. Disruptions in this pathway can lead to an accumulation of porphyrins or their precursors, resulting in various medical conditions called porphyrias. These disorders can manifest as neurological symptoms, skin lesions, and gastrointestinal issues, depending on the specific type of porphyria and the site of enzyme deficiency.

It is important to note that while porphyrins are essential for life, their accumulation in excessive amounts or at inappropriate locations can result in pathological conditions. Therefore, understanding the regulation and function of porphyrin metabolism is crucial for diagnosing and managing porphyrias and other related disorders.

The oncogene proteins v-sis are derived from the simian sarcoma virus (SSV). The v-sis gene in SSV is derived from a cellular gene called c-sis, which encodes for the platelet-derived growth factor B (PDGFB) protein. The v-sis oncogene protein is a truncated and altered version of the PDGFB protein, which has lost its regulatory mechanisms and can lead to uncontrolled cell growth and division, contributing to the development of cancer.

In normal cells, the c-sis gene produces a precursor protein that is cleaved into two identical subunits, forming the functional PDGFB homodimer. This growth factor plays an essential role in the regulation of cell growth, proliferation, and survival, particularly in mesenchymal cells such as fibroblasts and smooth muscle cells.

However, in SSV-infected cells, the v-sis oncogene encodes a fusion protein that includes the viral gag protein and a truncated version of the c-sis gene product. This fusion protein can form homodimers or heterodimers with cellular PDGFB, leading to unregulated activation of PDGF receptors and subsequent intracellular signaling pathways, promoting tumor growth and progression.

In summary, v-sis oncogene proteins are aberrant forms of the platelet-derived growth factor B (PDGFB) that lack proper regulation and contribute to uncontrolled cell growth and division, potentially leading to cancer development.

I could not find a specific protein named "tpr-met" in oncology or any other field of medicine. However, I was able to find information about the proteins TPR and MET, which can be relevant in the context of oncogenes.

TPR (Translocated Promoter Region) is a coiled-coil protein that plays a role in nuclear transport, chromatin remodeling, and transcription regulation. It has been found to interact with several other proteins, including the MET receptor tyrosine kinase.

MET is a proto-oncogene that encodes a receptor tyrosine kinase for hepatocyte growth factor (HGF). Upon HGF binding, MET activates various intracellular signaling pathways involved in cell proliferation, survival, motility, and morphogenesis. Dysregulation of the MET signaling pathway can contribute to oncogenic transformation and tumor progression.

In some cases, TPR has been found to interact with and regulate the MET receptor tyrosine kinase. This interaction may lead to aberrant activation of MET signaling, contributing to oncogenesis. However, there is no specific protein named "tpr-met" in the context of oncogene proteins.

The oncogene protein v-maf is a transcription factor that belongs to the basic leucine zipper (bZIP) family. It was originally identified as the viral oncogene product of the avian musculoaponeurotic fibrosarcoma virus (MAFV). The v-maf protein can transform cells and is believed to contribute to tumor development by altering the expression of various genes involved in cell growth, differentiation, and survival.

The v-maf protein contains a basic region that is responsible for DNA binding and a leucine zipper domain that mediates protein-protein interactions. It can form homodimers or heterodimers with other bZIP proteins, allowing it to regulate the transcription of target genes.

The cellular counterpart of v-maf is the maf oncogene, which encodes a family of transcription factors that include MafA, MafB, and NRL. These proteins play important roles in various biological processes, including development, differentiation, and metabolism. Dysregulation of maf gene expression or function has been implicated in the development of several types of cancer.

The v-mos oncogene protein is derived from the retrovirus called Moloney murine sarcoma virus (Mo-MSV). This oncogene encodes for a serine/threonine protein kinase, which is involved in cell proliferation and differentiation. When incorporated into the host genome during viral infection, the v-mos oncogene can cause unregulated cell growth and tumor formation, leading to sarcomas in mice. The normal cellular homolog of v-mos is called c-mos, which plays a crucial role in regulating cell division and is tightly controlled in normal cells. However, mutations or aberrant activation of c-mos can also contribute to oncogenic transformation and tumorigenesis.

An oncogene protein, specifically the v-Raf protein, is a product of the viral oncogene found in certain retroviruses that are capable of transforming cells and causing cancer. The v-Raf protein is derived from the cellular homolog, c-Raf, which is a serine/threonine kinase that plays a crucial role in regulating cell growth, differentiation, and survival.

The v-Raf protein, when compared to its cellular counterpart, lacks regulatory domains and possesses constitutive kinase activity. This results in uncontrolled signaling through the Ras/MAPK pathway, leading to aberrant cell proliferation and tumorigenesis. The activation of the v-Raf oncogene has been implicated in various types of cancer, including some leukemias and sarcomas. However, it is important to note that mutations in the c-Raf gene can also contribute to cancer development, highlighting the importance of proper regulation of this signaling pathway in maintaining cellular homeostasis.

An oncogene protein, specifically the v-fos protein, is a product of the v-fos gene found in the FBJ murine osteosarcoma virus. This viral oncogene can transform cells and cause cancer in animals. The normal cellular counterpart of v-fos is the c-fos gene, which encodes a nuclear protein that forms a heterodimer with other proteins to function as a transcription factor, regulating the expression of target genes involved in various cellular processes such as proliferation, differentiation, and transformation.

However, when the v-fos gene is integrated into the viral genome and expressed at high levels, it can lead to unregulated and constitutive activation of these cellular processes, resulting in oncogenic transformation and tumor formation. The v-fos protein can interact with other cellular proteins and modify their functions, leading to aberrant signaling pathways that contribute to the development of cancer.

The Crk protein is a human homolog of the viral oncogene v-crk, which was first discovered in the avian retrovirus CT10. The v-crk oncogene encodes for a truncated and constitutively active version of the Crk protein, which has been shown to contribute to cancer development by promoting cell growth signaling and inhibiting apoptosis (programmed cell death).

The human Crk protein is a cytoplasmic adaptor protein that plays a role in various intracellular signaling pathways. It contains several domains, including an N-terminal Src homology 2 (SH2) domain and two C-terminal Src homology 3 (SH3) domains, which allow it to interact with other signaling proteins and transmit signals from cell surface receptors to downstream effectors.

Crk protein has been implicated in several cellular processes, including cell proliferation, differentiation, migration, and adhesion. Dysregulation of Crk protein function or expression has been associated with various human diseases, including cancer. In particular, overexpression or hyperactivation of Crk protein has been observed in several types of cancer, such as leukemia, lymphoma, and solid tumors, and has been linked to increased cell proliferation, survival, and invasiveness.

Therefore, the oncogene protein v-crk is a truncated and constitutively active version of the Crk protein that contributes to cancer development by promoting aberrant signaling pathways leading to uncontrolled cell growth and inhibition of apoptosis.

v-Myb, also known as v-mybl2, is a retroviral oncogene that was originally isolated from the avian myeloblastosis virus (AMV). The protein product of this oncogene shares significant sequence homology with the human c-Myb protein, which is a member of the Myb family of transcription factors.

The c-Myb protein is involved in the regulation of gene expression during normal cell growth, differentiation, and development. However, when its function is deregulated or its expression is altered, it can contribute to tumorigenesis by promoting cell proliferation and inhibiting apoptosis (programmed cell death).

The v-Myb oncogene protein has a higher transforming potential than the c-Myb protein due to the presence of additional sequences that enhance its activity. These sequences allow v-Myb to bind to DNA more strongly, interact with other proteins more efficiently, and promote the expression of target genes involved in cell growth and survival.

Overexpression or mutation of c-Myb has been implicated in various human cancers, including leukemia, lymphoma, and carcinomas of the breast, colon, and prostate. Therefore, understanding the function and regulation of Myb proteins is important for developing new strategies to prevent and treat cancer.

v-Cbl is a type of oncogene protein that is derived from the cellular c-Cbl protein. Oncogenes are genes that have the potential to cause cancer, and they can do this by promoting cell growth and division when they should not. The v-Cbl protein is created when a virus called the avian reticuloendotheliosis virus infects a host cell and inserts its own version of the c-Cbl gene into the host's DNA. This results in the production of the abnormal v-Cbl protein, which can contribute to the development of cancer by disrupting the normal regulation of cell growth and division.

The c-Cbl protein is a type of E3 ubiquitin ligase, which is an enzyme that helps to tag other proteins for degradation. The v-Cbl protein retains this function, but it also has additional activities that allow it to promote cell growth and division. For example, v-Cbl can activate signaling pathways that lead to the activation of transcription factors, which are proteins that control the expression of genes involved in cell growth and division.

In addition to its role in cancer, v-Cbl has also been implicated in the development of other diseases, including immune disorders and neurological conditions. However, more research is needed to fully understand the various functions of this oncogene protein and how it contributes to disease.

The oncogene proteins v-erbB are derived from the erbB oncogene, which is a retroviral oncogene first discovered in avian erythroblastosis viruses (AEV). The erbB oncogene is homologous to the human epidermal growth factor receptor 2 (HER2/erbB-2) gene, which encodes a transmembrane tyrosine kinase receptor involved in cell proliferation and differentiation.

The v-erbB oncogene protein is a truncated and mutated version of the normal EGFR/erbB-1 receptor, which has lost its extracellular ligand-binding domain and gained constitutive tyrosine kinase activity. This results in uncontrolled cell growth and division, leading to the development of cancer.

The v-erbB oncogene protein has been extensively studied as a model system for understanding the molecular mechanisms of oncogenesis and has provided valuable insights into the regulation of cell growth and differentiation. Additionally, the study of v-erbB and other oncogenes has led to the development of targeted cancer therapies that inhibit the activity of these aberrant proteins and slow or stop the growth of cancer cells.

An oncogene protein, specifically the v-abl protein, is a tyrosine kinase enzyme that plays a role in cell growth, differentiation, and survival. The v-abl gene was originally discovered in the Abelson murine leukemia virus (Ab-MLV), which is a retrovirus that can cause leukemia in mice. The viral v-abl gene is a truncated and mutated version of the cellular c-abl gene, which is normally involved in important signaling pathways within cells.

The v-abl protein has gained oncogenic potential due to its altered regulation and constitutive activation, leading to uncontrolled cell growth and division, ultimately resulting in cancer. In humans, abnormal expression or activation of the c-abl gene and its protein product have been implicated in several types of cancer, including leukemia and some solid tumors. The oncogenic nature of v-abl has made it an important target for cancer therapy, with drugs like Imatinib mesylate (Gleevec) being developed to inhibit its activity.

Oncogenes are genes that have the potential to cause cancer. They can do this by promoting cell growth and division (cellular proliferation), preventing cell death (apoptosis), or enabling cells to invade surrounding tissue and spread to other parts of the body (metastasis). Oncogenes can be formed when normal genes, called proto-oncogenes, are mutated or altered in some way. This can happen as a result of exposure to certain chemicals or radiation, or through inherited genetic mutations. When activated, oncogenes can contribute to the development of cancer by causing cells to divide and grow in an uncontrolled manner.

I'm happy to help! However, I believe there might be a slight confusion in your question. "Oncogene proteins v-rel" is not a standard medical term. Instead, it seems like you are referring to the "v-rel" oncogene protein. Here's a definition:

The v-rel oncogene protein is a viral transcription factor initially discovered in the reticuloendotheliosis virus (REV), which causes avian lymphoma. The v-rel gene shares homology with the cellular c-rel gene, which encodes a member of the NF-κB (nuclear factor kappa-light-chain-enhancer of activated B cells) family of transcription factors.

The v-rel protein is capable of transforming cells and contributing to tumorigenesis due to its ability to constitutively activate gene expression, particularly through the NF-κB signaling pathway. This aberrant activation can lead to uncontrolled cell growth, inhibition of apoptosis (programmed cell death), and ultimately cancer development.

The v-rel protein is an example of a viral oncogene, which are genes that have been acquired by a virus from the host organism and contribute to tumor formation when expressed in the host. Viral oncogenes can provide valuable insights into the mechanisms of cancer development and potential therapeutic targets.

The oncogene proteins v-erbA are a subset of oncogenes that were initially discovered in retroviruses, specifically the avian erythroblastosis virus (AEV). These oncogenes are derived from normal cellular genes called proto-oncogenes, which play crucial roles in various cellular processes such as growth, differentiation, and survival.

The v-erbA oncogene protein is a truncated and mutated version of the thyroid hormone receptor alpha (THRA) gene, which is a nuclear receptor that regulates gene expression in response to thyroid hormones. The v-erbA protein can bind to DNA but cannot interact with thyroid hormones, leading to aberrant regulation of gene expression and uncontrolled cell growth, ultimately resulting in cancer.

In particular, the v-erbA oncogene has been implicated in the development of erythroblastosis, a disease characterized by the proliferation of immature red blood cells, leading to anemia and other symptoms. The activation of the v-erbA oncogene can also contribute to the development of other types of cancer, such as leukemia and lymphoma.

Oncogene proteins are derived from oncogenes, which are genes that have the potential to cause cancer. Normally, these genes help regulate cell growth and division, but when they become altered or mutated, they can become overactive and lead to uncontrolled cell growth and division, which is a hallmark of cancer. Oncogene proteins can contribute to tumor formation and progression by promoting processes such as cell proliferation, survival, angiogenesis, and metastasis. Examples of oncogene proteins include HER2/neu, EGFR, and BCR-ABL.

Oncogene proteins, viral, are cancer-causing proteins that are encoded by the genetic material (DNA or RNA) of certain viruses. These viral oncogenes can be acquired through infection with retroviruses, such as human immunodeficiency virus (HIV), human T-cell leukemia virus (HTLV), and certain types of papillomaviruses and polyomaviruses.

When these viruses infect host cells, they can integrate their genetic material into the host cell's genome, leading to the expression of viral oncogenes. These oncogenes may then cause uncontrolled cell growth and division, ultimately resulting in the formation of tumors or cancers. The process by which viruses contribute to cancer development is complex and involves multiple steps, including the alteration of signaling pathways that regulate cell proliferation, differentiation, and survival.

Examples of viral oncogenes include the v-src gene found in the Rous sarcoma virus (RSV), which causes chicken sarcoma, and the E6 and E7 genes found in human papillomaviruses (HPVs), which are associated with cervical cancer and other anogenital cancers. Understanding viral oncogenes and their mechanisms of action is crucial for developing effective strategies to prevent and treat virus-associated cancers.

An oncogene protein fusion is a result of a genetic alteration in which parts of two different genes combine to create a hybrid gene that can contribute to the development of cancer. This fusion can lead to the production of an abnormal protein that promotes uncontrolled cell growth and division, ultimately resulting in a malignant tumor. Oncogene protein fusions are often caused by chromosomal rearrangements such as translocations, inversions, or deletions and are commonly found in various types of cancer, including leukemia and sarcoma. These genetic alterations can serve as potential targets for cancer diagnosis and therapy.

Ras genes are a group of genes that encode for proteins involved in cell signaling pathways that regulate cell growth, differentiation, and survival. Mutations in Ras genes have been associated with various types of cancer, as well as other diseases such as developmental disorders and autoimmune diseases. The Ras protein family includes H-Ras, K-Ras, and N-Ras, which are activated by growth factor receptors and other signals to activate downstream effectors involved in cell proliferation and survival. Abnormal activation of Ras signaling due to mutations or dysregulation can contribute to tumor development and progression.

According to the National Center for Biotechnology Information (NCBI), AKT (also known as protein kinase B or PKB) is a type of oncogene protein that plays a crucial role in cell survival and signal transduction pathways. It is a serine/threonine-specific protein kinase that acts downstream of the PI3K (phosphatidylinositol 3-kinase) signaling pathway, which regulates various cellular processes such as proliferation, differentiation, and survival.

The activation of AKT promotes cell survival by inhibiting apoptosis or programmed cell death through the phosphorylation and inactivation of several downstream targets, including pro-apoptotic proteins such as BAD and caspase-9. Dysregulation of the AKT signaling pathway has been implicated in various human cancers, leading to uncontrolled cell growth and survival, angiogenesis, and metastasis.

The activation of AKT occurs through a series of phosphorylation events initiated by the binding of growth factors or other extracellular signals to their respective receptors. This leads to the recruitment and activation of PI3K, which generates phosphatidylinositol (3,4,5)-trisphosphate (PIP3) at the plasma membrane. PIP3 then recruits AKT to the membrane, where it is activated by phosphorylation at two key residues (Thr308 and Ser473) by upstream kinases such as PDK1 and mTORC2.

Overall, AKT plays a critical role in regulating cell survival and growth, and its dysregulation can contribute to the development and progression of various human cancers.

Neoplastic cell transformation is a process in which a normal cell undergoes genetic alterations that cause it to become cancerous or malignant. This process involves changes in the cell's DNA that result in uncontrolled cell growth and division, loss of contact inhibition, and the ability to invade surrounding tissues and metastasize (spread) to other parts of the body.

Neoplastic transformation can occur as a result of various factors, including genetic mutations, exposure to carcinogens, viral infections, chronic inflammation, and aging. These changes can lead to the activation of oncogenes or the inactivation of tumor suppressor genes, which regulate cell growth and division.

The transformation of normal cells into cancerous cells is a complex and multi-step process that involves multiple genetic and epigenetic alterations. It is characterized by several hallmarks, including sustained proliferative signaling, evasion of growth suppressors, resistance to cell death, enabling replicative immortality, induction of angiogenesis, activation of invasion and metastasis, reprogramming of energy metabolism, and evading immune destruction.

Neoplastic cell transformation is a fundamental concept in cancer biology and is critical for understanding the molecular mechanisms underlying cancer development and progression. It also has important implications for cancer diagnosis, prognosis, and treatment, as identifying the specific genetic alterations that underlie neoplastic transformation can help guide targeted therapies and personalized medicine approaches.

Proto-oncogenes are normal genes that are present in all cells and play crucial roles in regulating cell growth, division, and death. They code for proteins that are involved in signal transduction pathways that control various cellular processes such as proliferation, differentiation, and survival. When these genes undergo mutations or are activated abnormally, they can become oncogenes, which have the potential to cause uncontrolled cell growth and lead to cancer. Oncogenes can contribute to tumor formation through various mechanisms, including promoting cell division, inhibiting programmed cell death (apoptosis), and stimulating blood vessel growth (angiogenesis).

Proto-oncogene proteins are normal cellular proteins that play crucial roles in various cellular processes, such as signal transduction, cell cycle regulation, and apoptosis (programmed cell death). They are involved in the regulation of cell growth, differentiation, and survival under physiological conditions.

When proto-oncogene proteins undergo mutations or aberrations in their expression levels, they can transform into oncogenic forms, leading to uncontrolled cell growth and division. These altered proteins are then referred to as oncogene products or oncoproteins. Oncogenic mutations can occur due to various factors, including genetic predisposition, environmental exposures, and aging.

Examples of proto-oncogene proteins include:

1. Ras proteins: Involved in signal transduction pathways that regulate cell growth and differentiation. Activating mutations in Ras genes are found in various human cancers.
2. Myc proteins: Regulate gene expression related to cell cycle progression, apoptosis, and metabolism. Overexpression of Myc proteins is associated with several types of cancer.
3. EGFR (Epidermal Growth Factor Receptor): A transmembrane receptor tyrosine kinase that regulates cell proliferation, survival, and differentiation. Mutations or overexpression of EGFR are linked to various malignancies, such as lung cancer and glioblastoma.
4. Src family kinases: Intracellular tyrosine kinases that regulate signal transduction pathways involved in cell proliferation, survival, and migration. Dysregulation of Src family kinases is implicated in several types of cancer.
5. Abl kinases: Cytoplasmic tyrosine kinases that regulate various cellular processes, including cell growth, differentiation, and stress responses. Aberrant activation of Abl kinases, as seen in chronic myelogenous leukemia (CML), leads to uncontrolled cell proliferation.

Understanding the roles of proto-oncogene proteins and their dysregulation in cancer development is essential for developing targeted cancer therapies that aim to inhibit or modulate these aberrant signaling pathways.

I'm sorry for any confusion, but "Genes, myc" is not a recognized medical term or abbreviation. It seems like there might be a misunderstanding or a missing word in the request. "Myc" could refer to the Myc family of transcription factors that are involved in cell growth and division, and are often deregulated in cancer. However, without more context, it's difficult to provide an accurate definition. If you could provide more information or clarify your question, I would be happy to help further!

Gene amplification is a process in molecular biology where a specific gene or set of genes are copied multiple times, leading to an increased number of copies of that gene within the genome. This can occur naturally in cells as a response to various stimuli, such as stress or exposure to certain chemicals, but it can also be induced artificially through laboratory techniques for research purposes.

In cancer biology, gene amplification is often associated with tumor development and progression, where the amplified genes can contribute to increased cell growth, survival, and drug resistance. For example, the overamplification of the HER2/neu gene in breast cancer has been linked to more aggressive tumors and poorer patient outcomes.

In diagnostic and research settings, gene amplification techniques like polymerase chain reaction (PCR) are commonly used to detect and analyze specific genes or genetic sequences of interest. These methods allow researchers to quickly and efficiently generate many copies of a particular DNA sequence, facilitating downstream analysis and detection of low-abundance targets.

Proto-oncogene proteins, such as c-Myc, are crucial regulators of normal cell growth, differentiation, and apoptosis (programmed cell death). When proto-oncogenes undergo mutations or alterations in their regulation, they can become overactive or overexpressed, leading to the formation of oncogenes. Oncogenic forms of c-Myc contribute to uncontrolled cell growth and division, which can ultimately result in cancer development.

The c-Myc protein is a transcription factor that binds to specific DNA sequences, influencing the expression of target genes involved in various cellular processes, such as:

1. Cell cycle progression: c-Myc promotes the expression of genes required for the G1 to S phase transition, driving cells into the DNA synthesis and division phase.
2. Metabolism: c-Myc regulates genes associated with glucose metabolism, glycolysis, and mitochondrial function, enhancing energy production in rapidly dividing cells.
3. Apoptosis: c-Myc can either promote or inhibit apoptosis, depending on the cellular context and the presence of other regulatory factors.
4. Differentiation: c-Myc generally inhibits differentiation by repressing genes that are necessary for specialized cell functions.
5. Angiogenesis: c-Myc can induce the expression of pro-angiogenic factors, promoting the formation of new blood vessels to support tumor growth.

Dysregulation of c-Myc is frequently observed in various types of cancer, making it an important therapeutic target for cancer treatment.

Neoplastic gene expression regulation refers to the processes that control the production of proteins and other molecules from genes in neoplastic cells, or cells that are part of a tumor or cancer. In a normal cell, gene expression is tightly regulated to ensure that the right genes are turned on or off at the right time. However, in cancer cells, this regulation can be disrupted, leading to the overexpression or underexpression of certain genes.

Neoplastic gene expression regulation can be affected by a variety of factors, including genetic mutations, epigenetic changes, and signals from the tumor microenvironment. These changes can lead to the activation of oncogenes (genes that promote cancer growth and development) or the inactivation of tumor suppressor genes (genes that prevent cancer).

Understanding neoplastic gene expression regulation is important for developing new therapies for cancer, as targeting specific genes or pathways involved in this process can help to inhibit cancer growth and progression.

Retroviridae proteins, oncogenic, refer to the proteins expressed by retroviruses that have the ability to transform normal cells into cancerous ones. These oncogenic proteins are typically encoded by viral genes known as "oncogenes," which are acquired through the process of transduction from the host cell's DNA during retroviral replication.

The most well-known example of an oncogenic retrovirus is the Human T-cell Leukemia Virus Type 1 (HTLV-1), which encodes the Tax and HBZ oncoproteins. These proteins manipulate various cellular signaling pathways, leading to uncontrolled cell growth and malignant transformation.

It is important to note that not all retroviruses are oncogenic, and only a small subset of them have been associated with cancer development in humans or animals.

A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.

Cell transformation, viral refers to the process by which a virus causes normal cells to become cancerous or tumorigenic. This occurs when the genetic material of the virus integrates into the DNA of the host cell and alters its regulation, leading to uncontrolled cell growth and division. Some viruses known to cause cell transformation include human papillomavirus (HPV), hepatitis B virus (HBV), and certain types of herpesviruses.

Transfection is a term used in molecular biology that refers to the process of deliberately introducing foreign genetic material (DNA, RNA or artificial gene constructs) into cells. This is typically done using chemical or physical methods, such as lipofection or electroporation. Transfection is widely used in research and medical settings for various purposes, including studying gene function, producing proteins, developing gene therapies, and creating genetically modified organisms. It's important to note that transfection is different from transduction, which is the process of introducing genetic material into cells using viruses as vectors.

A cell line is a culture of cells that are grown in a laboratory for use in research. These cells are usually taken from a single cell or group of cells, and they are able to divide and grow continuously in the lab. Cell lines can come from many different sources, including animals, plants, and humans. They are often used in scientific research to study cellular processes, disease mechanisms, and to test new drugs or treatments. Some common types of human cell lines include HeLa cells (which come from a cancer patient named Henrietta Lacks), HEK293 cells (which come from embryonic kidney cells), and HUVEC cells (which come from umbilical vein endothelial cells). It is important to note that cell lines are not the same as primary cells, which are cells that are taken directly from a living organism and have not been grown in the lab.

A "cell line, transformed" is a type of cell culture that has undergone a stable genetic alteration, which confers the ability to grow indefinitely in vitro, outside of the organism from which it was derived. These cells have typically been immortalized through exposure to chemical or viral carcinogens, or by introducing specific oncogenes that disrupt normal cell growth regulation pathways.

Transformed cell lines are widely used in scientific research because they offer a consistent and renewable source of biological material for experimentation. They can be used to study various aspects of cell biology, including signal transduction, gene expression, drug discovery, and toxicity testing. However, it is important to note that transformed cells may not always behave identically to their normal counterparts, and results obtained using these cells should be validated in more physiologically relevant systems when possible.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

A cell line that is derived from tumor cells and has been adapted to grow in culture. These cell lines are often used in research to study the characteristics of cancer cells, including their growth patterns, genetic changes, and responses to various treatments. They can be established from many different types of tumors, such as carcinomas, sarcomas, and leukemias. Once established, these cell lines can be grown and maintained indefinitely in the laboratory, allowing researchers to conduct experiments and studies that would not be feasible using primary tumor cells. It is important to note that tumor cell lines may not always accurately represent the behavior of the original tumor, as they can undergo genetic changes during their time in culture.

ERBB-2, also known as HER2/neu or HER2, is a gene that encodes for a tyrosine kinase receptor protein. This receptor is part of the EGFR/ERBB family and plays crucial roles in cell growth, differentiation, and survival. Amplification or overexpression of this gene has been found in various types of human cancers, including breast, ovarian, lung, and gastric cancers. In breast cancer, ERBB-2 overexpression is associated with aggressive tumor behavior and poorer prognosis. Therefore, ERBB-2 has become an important therapeutic target for cancer treatment, with various targeted therapies developed to inhibit its activity.

A mutation is a permanent change in the DNA sequence of an organism's genome. Mutations can occur spontaneously or be caused by environmental factors such as exposure to radiation, chemicals, or viruses. They may have various effects on the organism, ranging from benign to harmful, depending on where they occur and whether they alter the function of essential proteins. In some cases, mutations can increase an individual's susceptibility to certain diseases or disorders, while in others, they may confer a survival advantage. Mutations are the driving force behind evolution, as they introduce new genetic variability into populations, which can then be acted upon by natural selection.

'Tumor cells, cultured' refers to the process of removing cancerous cells from a tumor and growing them in controlled laboratory conditions. This is typically done by isolating the tumor cells from a patient's tissue sample, then placing them in a nutrient-rich environment that promotes their growth and multiplication.

The resulting cultured tumor cells can be used for various research purposes, including the study of cancer biology, drug development, and toxicity testing. They provide a valuable tool for researchers to better understand the behavior and characteristics of cancer cells outside of the human body, which can lead to the development of more effective cancer treatments.

It is important to note that cultured tumor cells may not always behave exactly the same way as they do in the human body, so findings from cell culture studies must be validated through further research, such as animal models or clinical trials.

Ras proteins are a group of small GTPases that play crucial roles as regulators of intracellular signaling pathways in cells. They are involved in various cellular processes, such as cell growth, differentiation, and survival. Ras proteins cycle between an inactive GDP-bound state and an active GTP-bound state to transmit signals from membrane receptors to downstream effectors. Mutations in Ras genes can lead to constitutive activation of Ras proteins, which has been implicated in various human cancers and developmental disorders.

Cell division is the process by which a single eukaryotic cell (a cell with a true nucleus) divides into two identical daughter cells. This complex process involves several stages, including replication of DNA, separation of chromosomes, and division of the cytoplasm. There are two main types of cell division: mitosis and meiosis.

Mitosis is the type of cell division that results in two genetically identical daughter cells. It is a fundamental process for growth, development, and tissue repair in multicellular organisms. The stages of mitosis include prophase, prometaphase, metaphase, anaphase, and telophase, followed by cytokinesis, which divides the cytoplasm.

Meiosis, on the other hand, is a type of cell division that occurs in the gonads (ovaries and testes) during the production of gametes (sex cells). Meiosis results in four genetically unique daughter cells, each with half the number of chromosomes as the parent cell. This process is essential for sexual reproduction and genetic diversity. The stages of meiosis include meiosis I and meiosis II, which are further divided into prophase, prometaphase, metaphase, anaphase, and telophase.

In summary, cell division is the process by which a single cell divides into two daughter cells, either through mitosis or meiosis. This process is critical for growth, development, tissue repair, and sexual reproduction in multicellular organisms.

Messenger RNA (mRNA) is a type of RNA (ribonucleic acid) that carries genetic information copied from DNA in the form of a series of three-base code "words," each of which specifies a particular amino acid. This information is used by the cell's machinery to construct proteins, a process known as translation. After being transcribed from DNA, mRNA travels out of the nucleus to the ribosomes in the cytoplasm where protein synthesis occurs. Once the protein has been synthesized, the mRNA may be degraded and recycled. Post-transcriptional modifications can also occur to mRNA, such as alternative splicing and addition of a 5' cap and a poly(A) tail, which can affect its stability, localization, and translation efficiency.

Signal transduction is the process by which a cell converts an extracellular signal, such as a hormone or neurotransmitter, into an intracellular response. This involves a series of molecular events that transmit the signal from the cell surface to the interior of the cell, ultimately resulting in changes in gene expression, protein activity, or metabolism.

The process typically begins with the binding of the extracellular signal to a receptor located on the cell membrane. This binding event activates the receptor, which then triggers a cascade of intracellular signaling molecules, such as second messengers, protein kinases, and ion channels. These molecules amplify and propagate the signal, ultimately leading to the activation or inhibition of specific cellular responses.

Signal transduction pathways are highly regulated and can be modulated by various factors, including other signaling molecules, post-translational modifications, and feedback mechanisms. Dysregulation of these pathways has been implicated in a variety of diseases, including cancer, diabetes, and neurological disorders.

Genetic transcription is the process by which the information in a strand of DNA is used to create a complementary RNA molecule. This process is the first step in gene expression, where the genetic code in DNA is converted into a form that can be used to produce proteins or functional RNAs.

During transcription, an enzyme called RNA polymerase binds to the DNA template strand and reads the sequence of nucleotide bases. As it moves along the template, it adds complementary RNA nucleotides to the growing RNA chain, creating a single-stranded RNA molecule that is complementary to the DNA template strand. Once transcription is complete, the RNA molecule may undergo further processing before it can be translated into protein or perform its functional role in the cell.

Transcription can be either "constitutive" or "regulated." Constitutive transcription occurs at a relatively constant rate and produces essential proteins that are required for basic cellular functions. Regulated transcription, on the other hand, is subject to control by various intracellular and extracellular signals, allowing cells to respond to changing environmental conditions or developmental cues.

The term "DNA, neoplasm" is not a standard medical term or concept. DNA refers to deoxyribonucleic acid, which is the genetic material present in the cells of living organisms. A neoplasm, on the other hand, is a tumor or growth of abnormal tissue that can be benign (non-cancerous) or malignant (cancerous).

In some contexts, "DNA, neoplasm" may refer to genetic alterations found in cancer cells. These genetic changes can include mutations, amplifications, deletions, or rearrangements of DNA sequences that contribute to the development and progression of cancer. Identifying these genetic abnormalities can help doctors diagnose and treat certain types of cancer more effectively.

However, it's important to note that "DNA, neoplasm" is not a term that would typically be used in medical reports or research papers without further clarification. If you have any specific questions about DNA changes in cancer cells or neoplasms, I would recommend consulting with a healthcare professional or conducting further research on the topic.

"ErbB-2" is also known as "HER2" or "human epidermal growth factor receptor 2." It is a type of receptor tyrosine kinase (RTK) found on the surface of some cells. ErbB-2 does not bind to any known ligands, but it can form heterodimers with other ErbB family members, such as ErbB-3 and ErbB-4, which do have identified ligands. When a ligand binds to one of these receptors, it causes a conformational change that allows the ErbB-2 receptor to become activated through transphosphorylation. This activation triggers a signaling cascade that regulates cell growth, differentiation, and survival.

Overexpression or amplification of the ERBB2 gene, which encodes the ErbB-2 protein, is observed in approximately 20-30% of breast cancers and is associated with a more aggressive disease phenotype and poorer prognosis. Therefore, ErbB-2 has become an important target for cancer therapy, and several drugs that target this receptor have been developed, including trastuzumab (Herceptin), lapatinib (Tykerb), and pertuzumab (Perjeta).

Translocation, genetic, refers to a type of chromosomal abnormality in which a segment of a chromosome is transferred from one chromosome to another, resulting in an altered genome. This can occur between two non-homologous chromosomes (non-reciprocal translocation) or between two homologous chromosomes (reciprocal translocation). Genetic translocations can lead to various clinical consequences, depending on the genes involved and the location of the translocation. Some translocations may result in no apparent effects, while others can cause developmental abnormalities, cancer, or other genetic disorders. In some cases, translocations can also increase the risk of having offspring with genetic conditions.

3T3 cells are a type of cell line that is commonly used in scientific research. The name "3T3" is derived from the fact that these cells were developed by treating mouse embryo cells with a chemical called trypsin and then culturing them in a flask at a temperature of 37 degrees Celsius.

Specifically, 3T3 cells are a type of fibroblast, which is a type of cell that is responsible for producing connective tissue in the body. They are often used in studies involving cell growth and proliferation, as well as in toxicity tests and drug screening assays.

One particularly well-known use of 3T3 cells is in the 3T3-L1 cell line, which is a subtype of 3T3 cells that can be differentiated into adipocytes (fat cells) under certain conditions. These cells are often used in studies of adipose tissue biology and obesity.

It's important to note that because 3T3 cells are a type of immortalized cell line, they do not always behave exactly the same way as primary cells (cells that are taken directly from a living organism). As such, researchers must be careful when interpreting results obtained using 3T3 cells and consider any potential limitations or artifacts that may arise due to their use.

'Gene expression regulation' refers to the processes that control whether, when, and where a particular gene is expressed, meaning the production of a specific protein or functional RNA encoded by that gene. This complex mechanism can be influenced by various factors such as transcription factors, chromatin remodeling, DNA methylation, non-coding RNAs, and post-transcriptional modifications, among others. Proper regulation of gene expression is crucial for normal cellular function, development, and maintaining homeostasis in living organisms. Dysregulation of gene expression can lead to various diseases, including cancer and genetic disorders.

"Nude mice" is a term used in the field of laboratory research to describe a strain of mice that have been genetically engineered to lack a functional immune system. Specifically, nude mice lack a thymus gland and have a mutation in the FOXN1 gene, which results in a failure to develop a mature T-cell population. This means that they are unable to mount an effective immune response against foreign substances or organisms.

The name "nude" refers to the fact that these mice also have a lack of functional hair follicles, resulting in a hairless or partially hairless phenotype. This feature is actually a secondary consequence of the same genetic mutation that causes their immune deficiency.

Nude mice are commonly used in research because their weakened immune system makes them an ideal host for transplanted tumors, tissues, and cells from other species, including humans. This allows researchers to study the behavior of these foreign substances in a living organism without the complication of an immune response. However, it's important to note that because nude mice lack a functional immune system, they must be kept in sterile conditions and are more susceptible to infection than normal mice.

Nuclear proteins are a category of proteins that are primarily found in the nucleus of a eukaryotic cell. They play crucial roles in various nuclear functions, such as DNA replication, transcription, repair, and RNA processing. This group includes structural proteins like lamins, which form the nuclear lamina, and regulatory proteins, such as histones and transcription factors, that are involved in gene expression. Nuclear localization signals (NLS) often help target these proteins to the nucleus by interacting with importin proteins during active transport across the nuclear membrane.

Transcription factors are proteins that play a crucial role in regulating gene expression by controlling the transcription of DNA to messenger RNA (mRNA). They function by binding to specific DNA sequences, known as response elements, located in the promoter region or enhancer regions of target genes. This binding can either activate or repress the initiation of transcription, depending on the properties and interactions of the particular transcription factor. Transcription factors often act as part of a complex network of regulatory proteins that determine the precise spatiotemporal patterns of gene expression during development, differentiation, and homeostasis in an organism.

Protein-Tyrosine Kinases (PTKs) are a type of enzyme that plays a crucial role in various cellular functions, including signal transduction, cell growth, differentiation, and metabolism. They catalyze the transfer of a phosphate group from ATP to the tyrosine residues of proteins, thereby modifying their activity, localization, or interaction with other molecules.

PTKs can be divided into two main categories: receptor tyrosine kinases (RTKs) and non-receptor tyrosine kinases (NRTKs). RTKs are transmembrane proteins that become activated upon binding to specific ligands, such as growth factors or hormones. NRTKs, on the other hand, are intracellular enzymes that can be activated by various signals, including receptor-mediated signaling and intracellular messengers.

Dysregulation of PTK activity has been implicated in several diseases, such as cancer, diabetes, and inflammatory disorders. Therefore, PTKs are important targets for drug development and therapy.

Retroviridae is a family of viruses that includes human immunodeficiency virus (HIV) and other viruses that primarily use RNA as their genetic material. The name "retrovirus" comes from the fact that these viruses reverse transcribe their RNA genome into DNA, which then becomes integrated into the host cell's genome. This is a unique characteristic of retroviruses, as most other viruses use DNA as their genetic material.

Retroviruses can cause a variety of diseases in animals and humans, including cancer, neurological disorders, and immunodeficiency syndromes like AIDS. They have a lipid membrane envelope that contains glycoprotein spikes, which allow them to attach to and enter host cells. Once inside the host cell, the viral RNA is reverse transcribed into DNA by the enzyme reverse transcriptase, which is then integrated into the host genome by the enzyme integrase.

Retroviruses can remain dormant in the host genome for extended periods of time, and may be reactivated under certain conditions to produce new viral particles. This ability to integrate into the host genome has also made retroviruses useful tools in molecular biology, where they are used as vectors for gene therapy and other genetic manipulations.

Transgenic mice are genetically modified rodents that have incorporated foreign DNA (exogenous DNA) into their own genome. This is typically done through the use of recombinant DNA technology, where a specific gene or genetic sequence of interest is isolated and then introduced into the mouse embryo. The resulting transgenic mice can then express the protein encoded by the foreign gene, allowing researchers to study its function in a living organism.

The process of creating transgenic mice usually involves microinjecting the exogenous DNA into the pronucleus of a fertilized egg, which is then implanted into a surrogate mother. The offspring that result from this procedure are screened for the presence of the foreign DNA, and those that carry the desired genetic modification are used to establish a transgenic mouse line.

Transgenic mice have been widely used in biomedical research to model human diseases, study gene function, and test new therapies. They provide a valuable tool for understanding complex biological processes and developing new treatments for a variety of medical conditions.

DNA-binding proteins are a type of protein that have the ability to bind to DNA (deoxyribonucleic acid), the genetic material of organisms. These proteins play crucial roles in various biological processes, such as regulation of gene expression, DNA replication, repair and recombination.

The binding of DNA-binding proteins to specific DNA sequences is mediated by non-covalent interactions, including electrostatic, hydrogen bonding, and van der Waals forces. The specificity of binding is determined by the recognition of particular nucleotide sequences or structural features of the DNA molecule.

DNA-binding proteins can be classified into several categories based on their structure and function, such as transcription factors, histones, and restriction enzymes. Transcription factors are a major class of DNA-binding proteins that regulate gene expression by binding to specific DNA sequences in the promoter region of genes and recruiting other proteins to modulate transcription. Histones are DNA-binding proteins that package DNA into nucleosomes, the basic unit of chromatin structure. Restriction enzymes are DNA-binding proteins that recognize and cleave specific DNA sequences, and are widely used in molecular biology research and biotechnology applications.

Tumor suppressor protein p53, also known as p53 or tumor protein p53, is a nuclear phosphoprotein that plays a crucial role in preventing cancer development and maintaining genomic stability. It does so by regulating the cell cycle and acting as a transcription factor for various genes involved in apoptosis (programmed cell death), DNA repair, and cell senescence (permanent cell growth arrest).

In response to cellular stress, such as DNA damage or oncogene activation, p53 becomes activated and accumulates in the nucleus. Activated p53 can then bind to specific DNA sequences and promote the transcription of target genes that help prevent the proliferation of potentially cancerous cells. These targets include genes involved in cell cycle arrest (e.g., CDKN1A/p21), apoptosis (e.g., BAX, PUMA), and DNA repair (e.g., GADD45).

Mutations in the TP53 gene, which encodes p53, are among the most common genetic alterations found in human cancers. These mutations often lead to a loss or reduction of p53's tumor suppressive functions, allowing cancer cells to proliferate uncontrollably and evade apoptosis. As a result, p53 has been referred to as "the guardian of the genome" due to its essential role in preventing tumorigenesis.

Fibroblasts are specialized cells that play a critical role in the body's immune response and wound healing process. They are responsible for producing and maintaining the extracellular matrix (ECM), which is the non-cellular component present within all tissues and organs, providing structural support and biochemical signals for surrounding cells.

Fibroblasts produce various ECM proteins such as collagens, elastin, fibronectin, and laminins, forming a complex network of fibers that give tissues their strength and flexibility. They also help in the regulation of tissue homeostasis by controlling the turnover of ECM components through the process of remodeling.

In response to injury or infection, fibroblasts become activated and start to proliferate rapidly, migrating towards the site of damage. Here, they participate in the inflammatory response, releasing cytokines and chemokines that attract immune cells to the area. Additionally, they deposit new ECM components to help repair the damaged tissue and restore its functionality.

Dysregulation of fibroblast activity has been implicated in several pathological conditions, including fibrosis (excessive scarring), cancer (where they can contribute to tumor growth and progression), and autoimmune diseases (such as rheumatoid arthritis).

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

An oncogene fusion, also known as oncogenic fusion or chimeric oncogene, is a result of a genetic rearrangement where parts of two different genes combine to form a hybrid gene. This fusion can lead to the production of an abnormal protein that contributes to cancer development and progression. In many cases, one of the fused genes is a proto-oncogene, a normal gene that regulates cell growth and division. When this gene is altered through fusion, it can acquire increased activity or new functions, promoting uncontrolled cell growth and eventually leading to tumor formation. Oncogene fusions are often associated with specific types of cancer and can be used as diagnostic markers or therapeutic targets for cancer treatment.

A neoplasm is a tumor or growth that is formed by an abnormal and excessive proliferation of cells, which can be benign or malignant. Neoplasm proteins are therefore any proteins that are expressed or produced in these neoplastic cells. These proteins can play various roles in the development, progression, and maintenance of neoplasms.

Some neoplasm proteins may contribute to the uncontrolled cell growth and division seen in cancer, such as oncogenic proteins that promote cell cycle progression or inhibit apoptosis (programmed cell death). Others may help the neoplastic cells evade the immune system, allowing them to proliferate undetected. Still others may be involved in angiogenesis, the formation of new blood vessels that supply the tumor with nutrients and oxygen.

Neoplasm proteins can also serve as biomarkers for cancer diagnosis, prognosis, or treatment response. For example, the presence or level of certain neoplasm proteins in biological samples such as blood or tissue may indicate the presence of a specific type of cancer, help predict the likelihood of cancer recurrence, or suggest whether a particular therapy will be effective.

Overall, understanding the roles and behaviors of neoplasm proteins can provide valuable insights into the biology of cancer and inform the development of new diagnostic and therapeutic strategies.

Cell proliferation is the process by which cells increase in number, typically through the process of cell division. In the context of biology and medicine, it refers to the reproduction of cells that makes up living tissue, allowing growth, maintenance, and repair. It involves several stages including the transition from a phase of quiescence (G0 phase) to an active phase (G1 phase), DNA replication in the S phase, and mitosis or M phase, where the cell divides into two daughter cells.

Abnormal or uncontrolled cell proliferation is a characteristic feature of many diseases, including cancer, where deregulated cell cycle control leads to excessive and unregulated growth of cells, forming tumors that can invade surrounding tissues and metastasize to distant sites in the body.

I'm happy to help! However, I believe there may be a slight mistake in your question. "src" is not a term that is typically used in the context of genetics or genetics research. It is more commonly associated with computer programming and refers to the source code of a program.

On the other hand, genes are indeed an important concept in genetics! Genes are segments of DNA (deoxyribonucleic acid) that contain the instructions for making proteins, which are essential building blocks of all living organisms. Genes can also contain regulatory sequences that control when and where proteins are made.

Each gene has a specific location on a chromosome, and humans have around 20,000-25,000 genes distributed across 23 pairs of chromosomes. Variations in the DNA sequence of genes can lead to differences in traits between individuals, including susceptibility to certain diseases.

If you meant to ask about something else related to genetics or healthcare, please let me know and I'll do my best to provide a helpful answer!

Sarcoma viruses, murine, are a group of RNA viruses that primarily affect mice and other rodents. They are classified as type C retroviruses, which means they contain an envelope, have reverse transcriptase enzyme activity, and replicate through a DNA intermediate.

The murine sarcoma viruses (MSVs) are associated with the development of various types of tumors in mice, particularly fibrosarcomas, which are malignant tumors that originate from fibroblasts, the cells that produce collagen and other fibers in connective tissue.

The MSVs are closely related to the murine leukemia viruses (MLVs), and together they form a complex called the murine leukemia virus-related viruses (MLVRVs). The MLVRVs can undergo recombination events, leading to the generation of new viral variants with altered biological properties.

The MSVs are important tools in cancer research because they can transform normal cells into tumor cells in vitro and in vivo. The study of these viruses has contributed significantly to our understanding of the molecular mechanisms underlying cancer development and progression.

Apoptosis is a programmed and controlled cell death process that occurs in multicellular organisms. It is a natural process that helps maintain tissue homeostasis by eliminating damaged, infected, or unwanted cells. During apoptosis, the cell undergoes a series of morphological changes, including cell shrinkage, chromatin condensation, and fragmentation into membrane-bound vesicles called apoptotic bodies. These bodies are then recognized and engulfed by neighboring cells or phagocytic cells, preventing an inflammatory response. Apoptosis is regulated by a complex network of intracellular signaling pathways that involve proteins such as caspases, Bcl-2 family members, and inhibitors of apoptosis (IAPs).

Avian leukosis virus (ALV) is a type of retrovirus that primarily affects chickens and other birds. It is responsible for a group of diseases known as avian leukosis, which includes various types of tumors and immunosuppressive conditions. The virus is transmitted horizontally through the shedder's dander, feathers, and vertical transmission through infected eggs.

There are several subgroups of ALV (A, B, C, D, E, and J), each with different host ranges and pathogenicity. Some strains can cause rapid death in young chickens, while others may take years to develop clinical signs. The most common form of the disease is neoplastic, characterized by the development of various types of tumors such as lymphomas, myelomas, and sarcomas.

Avian leukosis virus infection can have significant economic impacts on the poultry industry due to decreased growth rates, increased mortality, and condemnation of infected birds at processing. Control measures include eradication programs, biosecurity practices, vaccination, and breeding for genetic resistance.

Promoter regions in genetics refer to specific DNA sequences located near the transcription start site of a gene. They serve as binding sites for RNA polymerase and various transcription factors that regulate the initiation of gene transcription. These regulatory elements help control the rate of transcription and, therefore, the level of gene expression. Promoter regions can be composed of different types of sequences, such as the TATA box and CAAT box, and their organization and composition can vary between different genes and species.

A fusion protein known as "BCR-ABL" is formed due to a genetic abnormality called the Philadelphia chromosome (derived from a reciprocal translocation between chromosomes 9 and 22). This results in the formation of the oncogenic BCR-ABL tyrosine kinase, which contributes to unregulated cell growth and division, leading to chronic myeloid leukemia (CML) and some types of acute lymphoblastic leukemia (ALL). The BCR-ABL fusion protein has constitutively active tyrosine kinase activity, which results in the activation of various signaling pathways promoting cell proliferation, survival, and inhibition of apoptosis. This genetic alteration is crucial in the development and progression of CML and some types of ALL, making BCR-ABL an important therapeutic target for these malignancies.

Gene expression is the process by which the information encoded in a gene is used to synthesize a functional gene product, such as a protein or RNA molecule. This process involves several steps: transcription, RNA processing, and translation. During transcription, the genetic information in DNA is copied into a complementary RNA molecule, known as messenger RNA (mRNA). The mRNA then undergoes RNA processing, which includes adding a cap and tail to the mRNA and splicing out non-coding regions called introns. The resulting mature mRNA is then translated into a protein on ribosomes in the cytoplasm through the process of translation.

The regulation of gene expression is a complex and highly controlled process that allows cells to respond to changes in their environment, such as growth factors, hormones, and stress signals. This regulation can occur at various stages of gene expression, including transcriptional activation or repression, RNA processing, mRNA stability, and translation. Dysregulation of gene expression has been implicated in many diseases, including cancer, genetic disorders, and neurological conditions.

Harvey murine sarcoma virus (HMSV) is a type of retrovirus, specifically a sarcoma virus that was first isolated from mice. It is named after J. Harvey, who discovered the virus in 1964. HMSV is closely related to Moloney murine leukemia virus (M-MuLV).

HMSV is a complex retrovirus, which contains several accessory genes that are not required for replication but contribute to viral pathogenesis and oncogenic transformation. The most well-known oncogene carried by HMSV is v-src, which encodes the pp60v-src protein tyrosine kinase. This oncogene was the first cellular oncogene (c-src) to be discovered, and it plays a crucial role in the transformation of cells and the development of sarcomas in infected mice.

HMSV infection typically occurs through the direct introduction of viral particles into susceptible tissues or by the transfer of infected cells. Once inside the host, HMSV integrates its genetic material into the host cell's DNA, leading to the expression of viral genes and the production of new virus particles. The activation of the v-src oncogene results in uncontrolled cell growth and division, ultimately leading to the formation of tumors.

In summary, Harvey murine sarcoma virus is a retrovirus that carries the v-src oncogene, causing uncontrolled cell growth and leading to the development of sarcomas in infected mice.

Adenovirus E1A proteins are the early region 1A proteins encoded by adenoviruses, a group of viruses that commonly cause respiratory infections in humans. The E1A proteins play a crucial role in the regulation of the viral life cycle and host cell response. They function as transcriptional regulators, interacting with various cellular proteins to modulate gene expression and promote viral replication.

There are two major E1A protein isoforms, 289R and 243R, which differ in their amino-terminal regions due to alternative splicing of the E1A mRNA. The 289R isoform contains an additional 46 amino acids at its N-terminus compared to the 243R isoform. Both isoforms share conserved regions, including a strong transcriptional activation domain and a binding domain for cellular proteins involved in transcriptional regulation, such as retinoblastoma protein (pRb) and p300/CBP.

The interaction between E1A proteins and pRb is particularly important because it leads to the release of E2F transcription factors, which are essential for the initiation of viral DNA replication. By binding and inactivating pRb, E1A proteins promote the expression of cell cycle-regulated genes that facilitate viral replication in dividing cells.

In summary, adenovirus E1A proteins are multifunctional regulatory proteins involved in the control of viral gene expression and host cell response during adenovirus infection. They manipulate cellular transcription factors and pathways to create a favorable environment for viral replication.

Polyomavirus transforming antigens refer to specific proteins expressed by polyomaviruses that can induce cellular transformation and lead to the development of cancer. These antigens are called large T antigen (T-Ag) and small t antigen (t-Ag). They manipulate key cellular processes, such as cell cycle regulation and DNA damage response, leading to uncontrolled cell growth and malignant transformation.

The large T antigen is a multifunctional protein that plays a crucial role in viral replication and transformation. It has several domains with different functions:

1. Origin binding domain (OBD): Binds to the viral origin of replication, initiating DNA synthesis.
2. Helicase domain: Unwinds double-stranded DNA during replication.
3. DNA binding domain: Binds to specific DNA sequences and acts as a transcriptional regulator.
4. Protein phosphatase 1 (PP1) binding domain: Recruits PP1 to promote viral DNA replication and inhibit host cell defense mechanisms.
5. p53-binding domain: Binds and inactivates the tumor suppressor protein p53, promoting cell cycle progression and preventing apoptosis.
6. Rb-binding domain: Binds to and inactivates the retinoblastoma protein (pRb), leading to deregulation of the cell cycle and uncontrolled cell growth.

The small t antigen shares a common N-terminal region with large T antigen but lacks some functional domains, such as the OBD and helicase domain. Small t antigen can also bind to and inactivate PP1 and pRb, contributing to transformation. However, its primary role is to stabilize large T antigen by preventing its proteasomal degradation.

Polyomavirus transforming antigens are associated with various human cancers, such as Merkel cell carcinoma (caused by Merkel cell polyomavirus) and some forms of brain tumors, sarcomas, and lymphomas (associated with simian virus 40).

"Cells, cultured" is a medical term that refers to cells that have been removed from an organism and grown in controlled laboratory conditions outside of the body. This process is called cell culture and it allows scientists to study cells in a more controlled and accessible environment than they would have inside the body. Cultured cells can be derived from a variety of sources, including tissues, organs, or fluids from humans, animals, or cell lines that have been previously established in the laboratory.

Cell culture involves several steps, including isolation of the cells from the tissue, purification and characterization of the cells, and maintenance of the cells in appropriate growth conditions. The cells are typically grown in specialized media that contain nutrients, growth factors, and other components necessary for their survival and proliferation. Cultured cells can be used for a variety of purposes, including basic research, drug development and testing, and production of biological products such as vaccines and gene therapies.

It is important to note that cultured cells may behave differently than they do in the body, and results obtained from cell culture studies may not always translate directly to human physiology or disease. Therefore, it is essential to validate findings from cell culture experiments using additional models and ultimately in clinical trials involving human subjects.

... , also known as proto-oncogene c-Src, or simply c-Src (cellular Src; pronounced "sarc ... Proto-oncogene tyrosine-protein kinase Src) at the PDBe-KB. Portal: Biology (Articles with short description, Short description ... This proto-oncogene may play a role in the regulation of embryonic development and cell growth. When src is activated, it ... Eventually this normal gene mutated into an abnormally functioning oncogene within the Rous sarcoma virus. Once the oncogene is ...
Proto-oncogenes code for proteins that help to regulate the cell growth and differentiation. Proto-oncogenes are often involved ... a proto-oncogene becomes a tumor-inducing agent, an oncogene. Examples of proto-oncogenes include RAS, WNT, MYC, ERK, and TRK. ... Wikimedia Commons has media related to Proto-oncogene proteins. Drosophila Oncogenes and Tumor Suppressors - The Interactive ... The resultant protein encoded by an oncogene is termed oncoprotein. Oncogenes play an important role in the regulation or ...
Alexiadis V, Waldmann T, Andersen J, Mann M, Knippers R, Gruss C (2000). "The protein encoded by the proto-oncogene DEK changes ... Kappes F, Burger K, Baack M, Fackelmayer FO, Gruss C (2001). "Subcellular localization of the human proto-oncogene protein DEK ... The human DEK gene encodes the DEK protein. This gene encodes a protein with one SAP domain. The protein binds to cruciform DNA ... PDBe-KB provides an overview of all the structure information available in the PDB for Human Protein DEK v t e (Articles with ...
NCBI (April 2015). "MDM2 MDM2 proto-oncogene, E3 ubiquitin protein ligase [ Homo sapiens (human) ]". {{cite journal}}: Cite ... Glutamate-rich protein 3, also known as Uncharacterized Protein C1orf173, is a protein encoded by the ERICH3 gene. ERICH3 was ... The C1orf173 protein has been predicted or experimentally observed to interact with the following proteins: CRISPLD2 GIMAP4 ... C1orf173 is predicted to be a nuclear protein based on PSORT II analysis and the suggested protein interactions found between ...
... proto-oncogene protein also known as N-Myc or basic helix-loop-helix protein 37 (bHLHe37), is a protein that in humans is ... Ramsay G, Stanton L, Schwab M, Bishop JM (1987). "Human proto-oncogene N-myc encodes nuclear proteins that bind DNA". Mol. Cell ... This protein is located in the cell nucleus and must dimerize with another bHLH protein in order to bind DNA. N-Myc is highly ... "Identification and characterization of the protein encoded by the human N-myc oncogene". Science. 232 (4751): 768-72. Bibcode: ...
Nishida K, Kaziro Y, Satoh T (1999). "Association of the proto-oncogene product dbl with G protein betagamma subunits". FEBS ... Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 is a protein that in humans is encoded by the GNB1 gene. ... Huang CL, Jan YN, Jan LY (1997). "Binding of the G protein betagamma subunit to multiple regions of G protein-gated inward- ... "Entrez Gene: GNB1 guanine nucleotide binding protein (G protein), beta polypeptide 1". Ogorodnikov A, Levin M, Tattikota S, ...
The DBL proto-oncogene is a protein that in humans is encoded by the MCF2 gene. The commonly-used name DBL is derived from " ... Nishida K, Kaziro Y, Satoh T (October 1999). "Association of the proto-oncogene product dbl with G protein betagamma subunits ... Ron D, Tronick SR, Aaronson SA, Eva A (August 1988). "Molecular cloning and characterization of the human dbl proto-oncogene: ... July 2000). "Human dbl proto-oncogene in 85 kb of xq26, and determination of the transcription initiation site". Gene. 253 (1 ...
Nishida K, Kaziro Y, Satoh T (1999). "Association of the proto-oncogene product dbl with G protein betagamma subunits". FEBS ... Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 is a protein that in humans is encoded by the GNG2 gene. ... Heterotrimeric G proteins play vital roles in cellular responses to external signals. The specificity of a G protein-receptor ... 2004). "A single Gbeta subunit locus controls cross-talk between protein kinase C and G protein regulation of N-type calcium ...
Wnt1 is a proto-oncogene protein (Wingless-type MMTV integration site family, member 1). This gene was originally thought to ... Fgf8 is also known as Fibroblast Growth Factor 8. It is a protein that is widely thought to be the most important organizing ...
"Effects of antibiotics and a proto-oncogene homolog on destruction of protein translocator SecY". Science. 325 (5941): 753-6. ... Protein families, Membrane proteins, Transmembrane proteins, Transmembrane transporters, Transport proteins, Integral membrane ... the YccA protein of Escherichia coli and the YetJ protein of Bacillus subtilis. These proteins are about 200-250 residues in ... These proteins are distantly related to the ionotropic glutamate-binding protein of the N-methyl D-aspartate (NMDA) receptor of ...
Proto-oncogene tyrosine-protein kinase Fyn (p59-FYN, Slk, Syn, MGC45350, Gene ID 2534) is an enzyme that in humans is encoded ... By definition as a proto-oncogene, Fyn codes for proteins that help regulate cell growth. Changes in its DNA sequence transform ... SH3 domain-mediated protein-protein interaction blocking drug". Oncogene. 21 (13): 2037-50. doi:10.1038/sj.onc.1205271. PMID ... Fyn is a member of the Src-family of kinases (SFK), the first proto-oncogene to be identified. The discovery of the Src-family ...
... is a protein that in humans is encoded by the MYBL1 gene. GRCh38: Ensembl release 89: ENSG00000185697 ... "Entrez Gene: MYB proto-oncogene like 1". Retrieved 2016-11-15. Ramkissoon LA, Horowitz PM, Craig JM, Ramkissoon SH, Rich BE, ...
Myb proto-oncogene protein is a member of the MYB (myeloblastosis) family of transcription factors. The protein contains three ... In humans, it includes Myb proto-oncogene like 1 and Myb-related protein B in addition to MYB proper. Members of the extended ... Jacobs SM, Gorse KM, Westin EH (1994). "Identification of a second promoter in the human c-myb proto-oncogene". Oncogene. 9 (1 ... MYB+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Drosophila Myb oncogene-like - The ...
Proto-oncogene vav is a protein that in humans is encoded by the VAV1 gene. The protein encoded by this proto-oncogene is a ... Shigematsu H, Iwasaki H, Otsuka T, Ohno Y, Arima F, Niho Y (May 1997). "Role of the vav proto-oncogene product (Vav) in ... Adams JM, Houston H, Allen J, Lints T, Harvey R (1992). "The hematopoietically expressed vav proto-oncogene shares homology ... Bustelo XR, Barbacid M (1992). "Tyrosine phosphorylation of the vav proto-oncogene product in activated B cells". Science. 256 ...
... is a proto-oncogene, meaning that mutations of this protein can lead to cancer. Mutations of the FLT3 receptor can lead ... receptor-type tyrosine-protein kinase FLT3, or fetal liver kinase-2 (Flk2) is a protein that in humans is encoded by the FLT3 ... Overview of all the structural information available in the PDB for UniProt: P36888 (Receptor-type tyrosine-protein kinase FLT3 ... Cluster of differentiation cytokine receptor receptor tyrosine kinase tyrosine kinase oncogene hematopoiesis Lymphopoiesis# ...
"Interaction of the c-cbl proto-oncogene product with the Tyk-2 protein tyrosine kinase". Biochemical and Biophysical Research ... "The WD motif-containing protein RACK-1 functions as a scaffold protein within the type I IFN receptor-signaling complex". ... Non-receptor tyrosine-protein kinase TYK2 is an enzyme that in humans is encoded by the TYK2 gene. TYK2 was the first member of ... This protein associates with the cytoplasmic domain of type I and type II cytokine receptors and promulgate cytokine signals by ...
Proto-oncogene FRAT1 is a protein that in humans is encoded by the FRAT1 gene. The protein encoded by this gene belongs to the ... Jonkers J, Korswagen HC, Acton D, Breuer M, Berns A (Mar 1997). "Activation of a novel proto-oncogene, Frat1, contributes to ... Saitoh T, Mine T, Katoh M (2002). "Molecular cloning and expression of proto-oncogene FRAT1 in human cancer". Int. J. Oncol. 20 ... 2007). "FRAT1, a substrate-specific regulator of glycogen synthase kinase-3 activity, is a cellular substrate of protein kinase ...
Raf is a proto-oncogene because mutations in this protein have been found in many cancers. The Rho GTPase Vav1, which can be ... GEFs are multi-domain proteins and interact with other proteins inside the cell through these domains. Adaptor proteins can ... G protein-coupled receptors are trans-membrane receptors that act as GEFs for their cognate G proteins upon binding of a ligand ... This 200 amino acid region is homologous to the yeast Sec7p protein. GEFs are often recruited by adaptor proteins in response ...
"SH3 domain-dependent interaction of the proto-oncogene product Vav with the focal contact protein zyxin". Oncogene. 12 (7): ... Degenhardt YY, Silverstein S (2001). "Interaction of Zyxin, a Focal Adhesion Protein, with the E6 Protein from Human ... SH3 domains of proteins involved in signal transduction pathways while the LIM domains are likely involved in protein-protein ... and characterization of a zyxin-related protein that binds the focal adhesion and microfilament protein VASP (vasodilator- ...
"Association of the vav proto-oncogene product with poly(rC)-specific RNA-binding proteins". Molecular and Cellular Biology. 15 ... RNA binding protein domains in other proteins that are similar to the RNA binding domain of protein K are called K-homology or ... Both proteins bind to single-stranded DNA as well as to RNA and can stimulate the activity of RNA polymerase II, the protein ... The hnRNP proteins have distinct nucleic acid binding properties. The protein encoded by this gene is located in the ...
Interestingly, uORFs were found in two thirds of proto-oncogenes and related proteins. 64-75% of experimentally found ... If transcription were to cease before the stop codon, an incomplete protein would be made during translation. In eukaryotic ... Long ORFs are often used, along with other evidence, to initially identify candidate protein-coding regions or functional RNA- ... Pearson WR, Wood T, Zhang Z, Miller W (November 1997). "Comparison of DNA sequences with protein sequences". Genomics. 46 (1): ...
Gupta K, Chevrette M, Gray DA (1994). "The Unp proto-oncogene encodes a nuclear protein". Oncogene. 9 (6): 1729-31. PMID ... 1995). "Elevated expression of Unph, a proto-oncogene at 3p21.3, in human lung tumors". Oncogene. 10 (11): 2179-83. PMID ... "Entrez Gene: USP4 ubiquitin specific peptidase 4 (proto-oncogene)". Gilchrist CA, Gray DA, Baker RT (December 1997). "A ... 2001). "The de-ubiquitinating enzyme Unp interacts with the retinoblastoma protein". Oncogene. 20 (39): 5538-5542. doi:10.1038/ ...
Proto-oncogene tyrosine-protein kinase Src Myristoylation SH2 domain SH3 domain Parsons SJ, Parsons JT (October 2004). "Src ... It allows for weak protein-protein and protein-lipid interactions. Myristoylation aids in the membrane association of Src ... Src family kinases interact with many cellular cytosolic, nuclear and membrane proteins, modifying these proteins by ... Myristoylation and fusion proteins work together to localize Src to cellular membranes. Src kinases transduce signals related ...
Proto-oncogene protein Wnt-3 is a protein that in humans is encoded by the WNT3 gene. The WNT gene family consists of ... It encodes a protein showing 98% amino acid identity to mouse Wnt3 protein, and 84% to human WNT3A protein, another WNT gene ... These proteins have been implicated in oncogenesis and in several developmental processes, including regulation of cell fate ... Smolich BD, McMahon JA, McMahon AP, Papkoff J (1994). "Wnt family proteins are secreted and associated with the cell surface". ...
The proto-oncogene c-Rel is a protein that in humans is encoded by the REL gene. The c-Rel protein is a member of the NF-κB ... "The v-rel oncogene product is complexed with cellular proteins including its proto-oncogene product and heat shock protein 70 ... "A human rel proto-oncogene cDNA containing an Alu fragment as a potential coding exon". Oncogene. 4 (7): 935-42. PMID 2666912. ... Kochel T, Rice NR (1992). "v-rel- and c-rel-protein complexes bind to the NF-kappa B site in vitro". Oncogene. 7 (3): 567-72. ...
The SKI protein is a nuclear proto-oncogene that is associated with tumors at high cellular concentrations. SKI has been shown ... The name SKI comes from the Sloan-Kettering Institute where the protein was initially discovered. The SKI proto-oncogene is ... The SKI protein and the CPB protein compete for binding with the Smad proteins, specifically competing with the Smad-3 and CReB ... The SnoN protein was identified as a similar protein and is often discussed in conjugation with the Ski protein in publications ...
1996). "SH3 domain-dependent interaction of the proto-oncogene product Vav with the focal contact protein zyxin". Oncogene. 12 ... "A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling". Nat. Biotechnol. 21 (3): ... Guanine nucleotide exchange factor VAV3 is a protein that in humans is encoded by the VAV3 gene. This gene is a member of the ... The VAV proteins are guanine nucleotide exchange factors (GEFs) for Rho family GTPases that activate pathways leading to actin ...
Proto-oncogene tyrosine-protein kinase FER is an enzyme that in humans is encoded by the FER gene. Fer protein is a member of ... Kim, L; Wong T W (Sep 1998). "Growth factor-dependent phosphorylation of the actin-binding protein cortactin is mediated by the ... 1990). "The FER gene is evolutionarily conserved and encodes a widely expressed member of the FPS/FES protein-tyrosine kinase ... Lee ST, Strunk KM, Spritz RA (1993). "A survey of protein tyrosine kinase mRNAs expressed in normal human melanocytes". ...
Proto-oncogene tyrosine-protein kinase ROS is an enzyme that in humans is encoded by the ROS1 gene. This proto-oncogene, highly ... The protein encoded by this gene is a type I integral membrane protein with tyrosine kinase activity. The protein may function ... protein; it is encoded by the c-ros oncogene and was first identified in 1986. The exact role of the ROS1 protein in normal ... Rabin M, Birnbaum D, Young D, Birchmeier C, Wigler M, Ruddle FH (July 1987). "Human ros1 and mas1 oncogenes located in regions ...
Proto-oncogene tyrosine-protein kinase MER is an enzyme that in humans is encoded by the MERTK gene. This gene is a member of ... "Entrez Gene: MERTK c-mer proto-oncogene tyrosine kinase". Iwase T, Tanaka M, Suzuki M, Naito Y, Sugimura H, Kino I (July 1993 ... "Ectopic expression of the proto-oncogene Mer in pediatric T-cell acute lymphoblastic leukemia". Clinical Cancer Research. 12 (9 ... Weier HU, Fung J, Lersch RA (Jun 1999). "Assignment of protooncogene MERTK (a.k.a. c-mer) to human chromosome 2q14.1 by in situ ...
  • pronounced "sarc", as it is short for sarcoma), is a non-receptor tyrosine kinase protein that in humans is encoded by the SRC gene. (wikipedia.org)
  • This induces long-range allostery via protein domain dynamics, causing the structure to be destabilized, resulting in the opening up of the SH3, SH2 and kinase domains and the autophosphorylation of the residue tyrosine 416. (wikipedia.org)
  • Protein kinase Cd and c-Abl kinase are required for transforming growth factor ß induction of endothelial-mesenchymal transition in vitro. (jefferson.edu)
  • This gene is a member of the protein-tyrosine kinase oncogene family. (cancerindex.org)
  • The protein associates with the p85 subunit of phosphatidylinositol 3-kinase and interacts with the fyn-binding protein. (cancerindex.org)
  • The protein encoded by this gene is a member of the Tyro3-Axl-Mer (TAM) receptor tyrosine kinase subfamily. (cancerindex.org)
  • Epidermal growth factor receptor (EGFR) is a transmembrane glycoprotein and member of the protein kinase superfamily that regulates cell growth and differentiation. (biolegend.com)
  • Proto-oncogene proteins that negatively regulate RECEPTOR PROTEIN-TYROSINE KINASE signaling. (nih.gov)
  • Belongs to the tyr protein kinase family. (lu.se)
  • The proteins have GTPase activity and are involved in signal transduction as monomeric GTP-binding proteins. (uchicago.edu)
  • Proto-oncogenes are often involved in signal transduction and execution of mitogenic signals, usually through their protein products. (wikipedia.org)
  • Wnt proteins constitute a family of secreted glyocoproteins that activate signal transduction pathways to mediate tissue homeostasis, cell fate, cell proliferation, and self-renewal. (thermofisher.com)
  • Upon acquiring an activating mutation, a proto-oncogene becomes a tumor-inducing agent, an oncogene. (wikipedia.org)
  • The mutation affects a single amino acid in the BRAF protein. (medlineplus.gov)
  • This mutation leads to production of a BRAF protein that is abnormally active, which disrupts regulation of cell proliferation and may allow histiocytes to grow and divide uncontrollably, leading to the abnormal accumulation of histiocytes that occurs in Erdheim-Chester disease. (medlineplus.gov)
  • This mutation leads to production of a BRAF protein that is abnormally active, which disrupts regulation of cell proliferation. (medlineplus.gov)
  • The BRAF gene mutations change single amino acids in the BRAF protein: One mutation replaces the amino acid threonine with the amino acid proline at position 241 (written as Thr241Pro or T241P) and the other mutation replaces the amino acid leucine with the amino acid phenylalanine at position 245 (written as Leu245Phe or L245F). (medlineplus.gov)
  • These mutations change single protein building blocks (amino acids) in the BRAF protein. (medlineplus.gov)
  • Activated oncogenes can cause those cells designated for apoptosis to survive and proliferate instead. (wikipedia.org)
  • Most oncogenes began as proto-oncogenes: normal genes involved in cell growth and proliferation or inhibition of apoptosis. (wikipedia.org)
  • Our previous study has shown that CCAAT-enhancer binding protein β (C/EBPβ) is an important regulator in METH-induced neuronal autophagy and apoptosis. (cancerindex.org)
  • In addition, hepatotoxicity and the expression of apoptosis proteins Bax and Bcl-2 were correlated qualitatively with the TP exposure duration and its intracellular concentration, which, in turn, can be modulated by P-gp inhibitors or inducers. (curehunter.com)
  • A proto-oncogene is a normal gene that could become an oncogene due to mutations or increased expression. (wikipedia.org)
  • Scope includes mutations and abnormal protein expression. (cancerindex.org)
  • Possible mechanisms for developing acquired resistance to anti-cancer drugs include mutations of genes encoding proteins that are the targets of drugs or are present in downstream pathways of proteins inhibited by drugs as well as the activation of collateral pathways ( 19 , 20 ). (spandidos-publications.com)
  • c-Src can be activated by many transmembrane proteins that include: adhesion receptors, receptor tyrosine kinases, G-protein coupled receptors and cytokine receptors. (wikipedia.org)
  • Its activity is directed by intracellular signals mediated by various types of receptors such as G protein-coupled receptors. (embl.de)
  • Two transcript variants encoding the same protein have been found for this gene. (wikipedia.org)
  • Eventually this normal gene mutated into an abnormally functioning oncogene within the Rous sarcoma virus. (wikipedia.org)
  • The protein was identified as a product of the murine double minute 2 gene (mdm-2). (nih.gov)
  • An oncogene is a gene that has the potential to cause cancer. (wikipedia.org)
  • Experiments performed by Dr. G. Steve Martin of the University of California, Berkeley demonstrated that SRC was indeed the gene of the virus that acted as an oncogene upon infection. (wikipedia.org)
  • Another example of an oncogene is the Bcr-Abl gene found on the Philadelphia chromosome, a piece of genetic material seen in Chronic Myelogenous Leukemia caused by the translocation of pieces from chromosomes 9 and 22. (wikipedia.org)
  • The BRAF gene provides instructions for making a protein that helps transmit chemical signals from outside the cell to the cell's nucleus. (medlineplus.gov)
  • The BRAF gene belongs to a class of genes known as oncogenes. (medlineplus.gov)
  • Since it was recognized that interstitial cells of Cajal express the gene product of c-kit, we performed immunohistochemistry for c-kit protein in ciliary muscle specimens of monkeys' eyes. (scielo.br)
  • What does this gene/protein do? (cancerindex.org)
  • What pathways are this gene/protein implicaed in? (cancerindex.org)
  • The protein product of the murine double minute gene 2 (mdm-2) plays a central role in the regulation of p53. (lu.se)
  • Cellular DNA-binding proteins encoded by the rel gene (GENES, REL). (bvsalud.org)
  • The bcl-3 protein does not inhibit either the DNA-binding activity of the Rel protein or its ability to trans-activate genes linked to the kappa B site. (duke.edu)
  • Cellular proteins encoded by the H-ras, K-ras and N-ras genes. (uchicago.edu)
  • Usually multiple oncogenes, along with mutated apoptotic or tumor suppressor genes will all act in concert to cause cancer. (wikipedia.org)
  • Oncogenes are a physically and functionally diverse set of genes, and as a result, their protein products have pleiotropic effects on a variety of intricate regulatory cascades within the cell. (wikipedia.org)
  • Proto-Oncogene Proteins c-mdm2" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (umassmed.edu)
  • Proto-Oncogene Proteins p21(ras)" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (uchicago.edu)
  • Scholars@Duke publication: The proto-oncogene bcl-3 encodes an I kappa B protein. (duke.edu)
  • ORF1 encodes ~40 kDa nucleic acid binding protein (ORF1p) [ 12 - 16 ] with nucleic acid chaperone activity [ 16 , 17 ]. (kosinmedj.org)
  • ORF2 encodes a ~150 kDa protein (ORF2p) with DNA endonuclease [ 18 ] and reverse transcriptase activity [ 19 , 20 ]. (kosinmedj.org)
  • ATP + a protein tyrosine = ADP + a protein tyrosine phosphate. (lu.se)
  • Replacement of wild-type RB can suppress the tumorigenicity of some of these cells, suggesting that the RB protein (Rb) may negatively regulate cell growth. (wdv.com)
  • NFAT2, as an important transcriptional promoter, regulates expression of TNF-α, myc proto-oncogene protein (c-myc), cyclooxygenase-2 (COX-2), Fas ligand (FasL) and also generates crosstalks with ERK/MAPK pathway and AKT/GSK3b signaling, which achieves its control of the cell fate [7-12]. (researchsquare.com)
  • The CRAL-TRIO domain is found in GTPase-activating proteins (GAPs), guanine nucleotide exchange factors (GEFs) and a family of hydrophobic ligand binding proteins, including the yeast SEC14 protein and mammalian retinaldehyde- and alpha-tocopherol-binding proteins. (embl.de)
  • Proto-oncogenes code for proteins that help to regulate the cell growth and differentiation. (wikipedia.org)
  • According to recent studies, the long interspersed element-1 (LINE-1) retrotransposon open reading frame (ORF) is located in the intron of the c-Met proto-oncogene, which is involved in cancer progression and metastasis, and regulates its expression. (kosinmedj.org)
  • LINE-1 hypomethylation induces the activation of proto-oncogenes in human colorectal cancer metastasis. (kosinmedj.org)
  • Specifically, the activation of proto-oncogene c-Met is involved in liver metastasis of colorectal cancer patients [ 7 ]. (kosinmedj.org)
  • Malignant transformation is usually the result of chromosomal translocations that activate proto-oncogenes or create a chimeric fusion protein. (oncolink.org)
  • Rel frequently combines with other related proteins (NF-KAPPA B, I-kappa B, relA) to form heterodimers that regulate transcription. (bvsalud.org)
  • Src contains at least three flexible protein domains, which, in conjunction with myristoylation, can mediate attachment to membranes and determine subcellular localization. (wikipedia.org)
  • Our results suggest that a screening approach using protein crystallography is particularly useful to identify universal fragments for the conserved hydrophilic recognition sites found in target families such as SH2 domains, phosphatases, kinases, proteases, and esterases. (rcsb.org)
  • There are 22196 SEC14 domains in 22009 proteins in SMART's nrdb database. (embl.de)
  • Sec14p-like domains in NF1 and Dbl-like proteins indicate lipid regulation of Ras and Rho signaling. (embl.de)
  • This Recombinant Human MYCN protein is an essential resource for cancer researchers. (cusabio.com)
  • Equipped with an N-terminal 6xHis-tag, our Recombinant Human MYCN protein facilitates effortless purification and detection. (cusabio.com)
  • Choose between liquid and lyophilized powder forms to best suit your experimental requirements and elevate your research with our Recombinant Human MYCN protein. (cusabio.com)
  • Review: In vitro glutathione S-transferase (GST) pull-down assay with recombinant GST-CCNT1, GST-CDK9, and GST-EAF1 together with His-tagged MYCN proteins demonstrated that MYCN directly binds to EAF1 with the highest affinity. (cusabio.com)
  • A cellular phosphoprotein with an apparent molecular mass of 90 kd (p90) that forms a complex with both mutant and wild-type p53 protein has been characterized, purified, and identified. (nih.gov)
  • Bishop and Varmus were awarded the Nobel Prize in Physiology or Medicine in 1989 for their discovery of the cellular origin of retroviral oncogenes. (wikipedia.org)
  • The domain is named after cellular retinaldehyde-binding protein (CRALBP) and TRIO guanine exchange factor. (embl.de)
  • The Rho family of GTP-binding proteins has been implicated in the regulation of various cellular functions including actin cytoskeleton-dependent morphological change. (embl.de)
  • These compounds exhibit high selectivity for SFKs over a panel of recombinant protein kinases, excellent pharmacokinetics, and in vivo activity following oral dosing. (rcsb.org)
  • The c-Fos and c-Jun oncoproteins and the p53 tumor suppressor protein are short-lived transcription factors. (cnrs.fr)
  • In the CYTOPLASM, I-kappa B proteins bind to the transcription factor NF-KAPPA B. Cell stimulation causes its dissociation and translocation of active NF-kappa B to the nucleus. (bvsalud.org)
  • Purification: This antibody is purified through a protein A column, followed by peptide affinity purification. (hatinhibitor.com)
  • Targeted protein degrader (TPD) drugs have seen a greater than 2,000% increase in the total value of venture financing deals, rising from $33 million in 2017 to $707 million in 2022, according to GlobalData's Pharma Intelligence Center Deals Database. (pharmaceutical-technology.com)
  • It was originally identified as a protein that provides a retroviral integration site for integration of FRIEND MURINE LEUKEMIA VIRUS. (childrensmercy.org)
  • Almost all of these genetic changes abnormally activate the protein, which disrupts the tightly regulated RAS/MAPK signaling pathway in cells throughout the body. (medlineplus.gov)
  • After blocking endogenous peroxidase activity and nonspecific protein binding, 1:100 dilution of mouse monoclonal antibody against c-kit human oncoprotein was applied to tissues. (scielo.br)
  • Furthermore, bcl-3 antisera immunoprecipitates an in vitro-radiolabeled 37-kD (I kappa B alpha) protein. (duke.edu)
  • Comparison of tryptic peptide maps of the bcl-3 protein synthesized in vitro, and p56 and p38 from HeLa cells, shows that they are all structurally related. (duke.edu)
  • The c-myc protein is localized in the nucleus and can physically associate with RB protein in vitro, hence c-myc may functionally antagonize RB function. (wdv.com)
  • Phosphatidylinositol transfer proteins (PITPs) can bind specifically and transfer a single phosphatidylinositol (PI) molecule between phospholipid membranes in an ATP-independent manner in vitro. (embl.de)
  • The first confirmed oncogene was discovered in 1970 and was termed SRC (pronounced "sarc" as it is short for sarcoma). (wikipedia.org)
  • The bcl-3 protein is able to inhibit the DNA binding and trans-activation of authentic NF-kappa B heterodimers p50-p65 and p49-p65, as well as p50 and p49 homodimers. (duke.edu)
  • A human 37-kD protein (I kappa B alpha), identified previously as a member of the I kappa B family, is also unable to inhibit DNA-binding activity of the Rel protein. (duke.edu)
  • However, unlike bcl-3, the 37-kD (I kappa B alpha) protein has no effect on the DNA-binding activity of p50 or p49 homodimers. (duke.edu)
  • Two dimensional phosphotryptic peptide maps of the human bcl-3 and the human 37-kD (I kappa B alpha) proteins reveal that the phosphopeptides from the 37-kD (I kappa B alpha) protein are nested within the bcl-3 protein. (duke.edu)
  • Removal of the amino-terminal sequences of the bcl-3 protein generates a protein that inhibits the DNA binding of the p50-p65 heterodimer but, like the 37-kD (I kappa B alpha) protein, is no longer able to inhibit the binding of the p50 and p49 homodimers with kappa B DNA. (duke.edu)
  • We propose that the bcl-3 and 37-kD (I kappa B alpha) proteins are related and are members of the I kappa B family. (duke.edu)
  • En el CITOPLASMA, las proteínas B I-kappa se unen al factor de transcripción NF-KAPPA B. La estimulación celular causa su disociación y traslocación del NF-kappa B activo al núcleo. (bvsalud.org)
  • It transduces signals from the extracellular matrix into the cytoplasm by binding to the vitamin K-dependent protein growth arrest-specific 6 (Gas6). (cancerindex.org)
  • Targeting a DNA binding motif of the EVI1 protein by a pyrrole-imidazole polyamide. (rochester.edu)
  • An amino-terminal portion conserved among a subset of Dbl family proteins is sufficient for the binding of Gbetagamma. (embl.de)
  • In 1976, Drs. Dominique Stéhelin [fr], J. Michael Bishop and Harold E. Varmus of the University of California, San Francisco demonstrated that oncogenes were activated proto-oncogenes as is found in many organisms, including humans. (wikipedia.org)
  • The Myc protein and proteins that participate in mitosis represent attractive targets for cancer therapy. (nih.gov)
  • TPD drugs are an emerging modality that selectively targets disease-causing proteins by leveraging intracellular protein degradation mechanisms, such as the ubiquitin-proteasome system and autophagy. (pharmaceutical-technology.com)
  • The guanine nucleotide exchange factor (GEF) Dbl targets Rho family proteins thereby stimulating their GDP/GTP exchange, and thus is believed to be involved in receptor-mediated regulation of the proteins. (embl.de)
  • Using Ingenuity Pathway Analysis bioinformatics software, it was revealed that the activity of multiple signaling pathways varied alongside the changes in expression of these proteins, and c‑SRC was identified as a protein involved in a number of these signaling pathways, with its activity varying markedly upon the acquisition of resistance. (spandidos-publications.com)
  • Are there multiple proteolytic pathways contributing to c-Fos, c-Jun and p53 protein degradation in vivo? (cnrs.fr)