Nuclear Matrix
Nuclear Matrix-Associated Proteins
Extracellular Matrix
Matrix Attachment Regions
Matrix Attachment Region Binding Proteins
Cell Nucleus
Nuclear Proteins
Extracellular Matrix Proteins
Matrix Metalloproteinase 2
Matrix Metalloproteinases
Lamins
Heterogeneous-Nuclear Ribonucleoprotein U
Lamin Type B
Bone Matrix
Chromatin
Matrix Metalloproteinase 1
Matrix Metalloproteinase Inhibitors
DNA
Blotting, Southwestern
RNA, Heterogeneous Nuclear
Electrophoresis, Gel, Two-Dimensional
HeLa Cells
Matrix Metalloproteinase 3
Molecular Sequence Data
Cell Fractionation
Interphase
DNA-Binding Proteins
Physarum polycephalum
Fluorescent Antibody Technique
Microscopy, Electron
Cells, Cultured
Nuclear Envelope
Base Sequence
Electrophoresis, Polyacrylamide Gel
Tumor Cells, Cultured
Amino Acid Sequence
Binding Sites
Deoxyribonuclease I
Protein Binding
Matrix Metalloproteinase 14
Matrix Metalloproteinase 7
Hypotrichida
Matrix Metalloproteinase 13
Subcellular Fractions
Collagen
Fibroblasts
Cell Nucleolus
Transcription, Genetic
Microscopy, Fluorescence
Microscopy, Immunoelectron
Fibronectins
Cell Compartmentation
Transcription Factors
Tetrathionic Acid
Matrix Metalloproteinases, Membrane-Associated
Blotting, Western
Protamines
Self assembly of NuMA: multiarm oligomers as structural units of a nuclear lattice. (1/351)
NuMA is a nuclear matrix protein in interphase and relocates to the spindle poles in mitotis. Different NuMA constructs, in which either N- or C-terminal domains were deleted, and the full-length construct were expressed in Escherichia coli, and the NuMA polypeptides were purified to homogeneity and allowed to assemble in vitro. Electron microscopy showed that NuMA can build multiarm oligomers by interaction of the C-terminal globular domains. Each arm of the oligomer corresponds to a NuMA dimer. Oligomers with up to 10 or 12 arms have been observed for both full-length NuMA and for constructs that still contain the proximal part of the C-terminal tail domain. Other results from this laboratory have shown that transient overexpression of NuMA in HeLa cells induces a nuclear scaffold with a quasi-hexagonal organization that can fill the nuclei. Here we show that computer modelling of the three-dimensional packing of NuMA into such scaffolds can explain the different spacing of the hexagons seen when constructs with different coiled-coil lengths are used. Thus, the 12 arm oligomer, for which we have in vitro evidence, may be the structural unit from which the nuclear scaffold in transfected cells is built. (+info)A nonerythroid isoform of protein 4.1R interacts with the nuclear mitotic apparatus (NuMA) protein. (2/351)
Red blood cell protein 4.1 (4.1R) is an 80- kD erythrocyte phosphoprotein that stabilizes the spectrin/actin cytoskeleton. In nonerythroid cells, multiple 4.1R isoforms arise from a single gene by alternative splicing and predominantly code for a 135-kD isoform. This isoform contains a 209 amino acid extension at its NH2 terminus (head piece; HP). Immunoreactive epitopes specific for HP have been detected within the cell nucleus, nuclear matrix, centrosomes, and parts of the mitotic apparatus in dividing cells. Using a yeast two-hybrid system, in vitro binding assays, coimmunolocalization, and coimmunoprecipitation studies, we show that a 135-kD 4.1R isoform specifically interacts with the nuclear mitotic apparatus (NuMA) protein. NuMA and 4.1R partially colocalize in the interphase nucleus of MDCK cells and redistribute to the spindle poles early in mitosis. Protein 4.1R associates with NuMA in the interphase nucleus and forms a complex with spindle pole organizing proteins, NuMA, dynein, and dynactin during cell division. Overexpression of a 135-kD isoform of 4.1R alters the normal distribution of NuMA in the interphase nucleus. The minimal sequence sufficient for this interaction has been mapped to the amino acids encoded by exons 20 and 21 of 4.1R and residues 1788-1810 of NuMA. Our results not only suggest that 4.1R could, possibly, play an important role in organizing the nuclear architecture, mitotic spindle, and spindle poles, but also could define a novel role for its 22-24-kD domain. (+info)RAE1 is a shuttling mRNA export factor that binds to a GLEBS-like NUP98 motif at the nuclear pore complex through multiple domains. (3/351)
Gle2p is implicated in nuclear export of poly(A)+ RNA and nuclear pore complex (NPC) structure and distribution in Saccharomyces cerevisiae. Gle2p is anchored at the nuclear envelope (NE) via a short Gle2p-binding motif within Nup116p called GLEBS. The molecular mechanism by which Gle2p and the Gle2p-Nup116p interaction function in mRNA export is unknown. Here we show that RAE1, the mammalian homologue of Gle2p, binds to a GLEBS-like NUP98 motif at the NPC through multiple domains that include WD-repeats and a COOH-terminal non-WD-repeat extension. This interaction is direct, as evidenced by in vitro binding studies and chemical cross-linking. Microinjection experiments performed in Xenopus laevis oocytes demonstrate that RAE1 shuttles between the nucleus and the cytoplasm and is exported from the nucleus in a temperature-dependent and RanGTP-independent manner. Docking of RAE1 to the NE is highly dependent on new mRNA synthesis. Overexpression of the GLEBS-like motif also inhibits NE binding of RAE1 and induces nuclear accumulation of poly(A)+ RNA. Both effects are abrogated either by the introduction of point mutations in the GLEBS-like motif or by overexpression of RAE1, indicating a direct role for RAE1 and the NUP98-RAE1 interaction in mRNA export. Together, our data suggest that RAE1 is a shuttling transport factor that directly contributes to nuclear export of mRNAs through its ability to anchor to a specific NUP98 motif at the NPC. (+info)The SRm160/300 splicing coactivator is required for exon-enhancer function. (4/351)
Exonic splicing enhancer (ESE) sequences are important for the recognition of splice sites in pre-mRNA. These sequences are bound by specific serine-arginine (SR) repeat proteins that promote the assembly of splicing complexes at adjacent splice sites. We have recently identified a splicing "coactivator," SRm160/300, which contains SRm160 (the SR nuclear matrix protein of 160 kDa) and a 300-kDa nuclear matrix antigen. In the present study, we show that SRm160/300 is required for a purine-rich ESE to promote the splicing of a pre-mRNA derived from the Drosophila doublesex gene. The association of SRm160/300 and U2 small nuclear ribonucleoprotein particle (snRNP) with this pre-mRNA requires both U1 snRNP and factors bound to the ESE. Independently of pre-mRNA, SRm160/300 specifically interacts with U2 snRNP and with a human homolog of the Drosophila alternative splicing regulator Transformer 2, which binds to purine-rich ESEs. The results suggest a model for ESE function in which the SRm160/300 splicing coactivator promotes critical interactions between ESE-bound "activators" and the snRNP machinery of the spliceosome. (+info)Distinct leukemia phenotypes in transgenic mice and different corepressor interactions generated by promyelocytic leukemia variant fusion genes PLZF-RARalpha and NPM-RARalpha. (5/351)
Acute promyelocytic leukemia (APL) is characterized by a specific chromosome translocation involving RARalpha and one of four fusion partners: PML, PLZF, NPM, and NuMA genes. To study the leukemogenic potential of the fusion genes in vivo, we generated transgenic mice with PLZF-RARalpha and NPM-RARalpha. PLZF-RARalpha transgenic animals developed chronic myeloid leukemia-like phenotypes at an early stage of life (within 3 months in five of six mice), whereas three NPM-RARalpha transgenic mice showed a spectrum of phenotypes from typical APL to chronic myeloid leukemia relatively late in life (from 12 to 15 months). In contrast to bone marrow cells from PLZF-RARalpha transgenic mice, those from NPM-RARalpha transgenic mice could be induced to differentiate by all-trans-retinoic acid (ATRA). We also studied RARE binding properties and interactions between nuclear corepressor SMRT and various fusion proteins in response to ATRA. Dissociation of SMRT from different receptors was observed at ATRA concentrations of 0.01 microM, 0.1 microM, and 1.0 microM for RARalpha-RXRalpha, NPM-RARalpha, and PML-RARalpha, respectively, but not observed for PLZF-RARalpha even in the presence of 10 microM ATRA. We also determined the expression of the tissue factor gene in transgenic mice, which was detected only in bone marrow cells of mice expressing the fusion genes. These data clearly establish the leukemogenic role of PLZF-RARalpha and NPM-RARalpha and the importance of fusion receptor/corepressor interactions in the pathogenesis as well as in determining different clinical phenotypes of APL. (+info)Ran-GTP stabilises microtubule asters and inhibits nuclear assembly in Xenopus egg extracts. (6/351)
Ran is an abundant GTPase of the Ras superfamily that is highly conserved in eukaryotes. In interphase cells, Ran is mainly nuclear and thought to be predominantly GTP-bound, but it is also present in the cytoplasm, probably GDP-bound. This asymmetric distribution plays an important role in directing nucleocytoplasmic transport. Ran has also been implicated in cell cycle control, including the transition from mitosis to interphase when the compartmentalisation of the nucleus is established. Here, we have examined the role of Ran in this transition using a cell-free system of Xenopus egg extracts supplemented with sperm heads that provides a model for microtubule aster formation and post-M phase nuclear assembly. Ran-GTP, added as wild-type protein, a mutant defective in GTPase activity (Q69L), or generated by addition of the specific nucleotide exchange factor RCC1, stabilises large microtubule asters nucleated at the sperm centrosome, prevents the redistribution of NuMA from the aster to the nucleus and blocks chromatin decondensation. In contrast, Ran GDP does not stabilise microtubules or inhibit nuclear assembly. RanT24N and RanBP1, which oppose the generation of Ran-GTP by RCC1, arrest nuclear growth after disappearance of the aster. Ran associates with microtubule asters in egg extracts and with mitotic spindles in somatic Xenopus cells, suggesting that it may affect microtubule stability directly. These results show that Ran has a novel function in the control of microtubule stability that is clearly distinct from nucleocytoplasmic transport. The Ran GDP/GTP switch may play a role in co-ordinating changes in the structure of microtubules and the assembly of the nucleus associated with the transition from mitosis to interphase. (+info)Chromosomal instability and cytoskeletal defects in oral cancer cells. (7/351)
Oral squamous cell carcinomas are characterized by complex, often near-triploid karyotypes with structural and numerical variations superimposed on the initial clonal chromosomal alterations. We used immunohistochemistry combined with classical cytogenetic analysis and spectral karyotyping to investigate the chromosomal segregation defects in cultured oral squamous cell carcinoma cells. During division, these cells frequently exhibit lagging chromosomes at both metaphase and anaphase, suggesting defects in the mitotic apparatus or kinetochore. Dicentric anaphase chromatin bridges and structurally altered chromosomes with consistent long arms and variable short arms, as well as the presence of gene amplification, suggested the occurrence of breakage-fusion-bridge cycles. Some anaphase bridges were observed to persist into telophase, resulting in chromosomal exclusion from the reforming nucleus and micronucleus formation. Multipolar spindles were found to various degrees in the oral squamous cell carcinoma lines. In the multipolar spindles, the poles demonstrated different levels of chromosomal capture and alignment, indicating functional differences between the poles. Some spindle poles showed premature splitting of centrosomal material, a precursor to full separation of the microtubule organizing centers. These results indicate that some of the chromosomal instability observed within these cancer cells might be the result of cytoskeletal defects and breakage-fusion-bridge cycles. (+info)The SRm160/300 splicing coactivator subunits. (8/351)
The SRm160/300 splicing coactivator, which consists of the serine/arginine (SR)-related nuclear matrix protein of 160 kDa and a 300-kDa nuclear matrix antigen, functions in splicing by promoting critical interactions between splicing factors bound to pre-mRNA, including snRNPs and SR family proteins. In this article we report the isolation of a cDNA encoding the 300-kDa antigen and investigate the activity of it and SRm160 in splicing. Like SRm160, the 300-kDa antigen contains domains rich in alternating S and R residues but lacks an RNA recognition motif; the protein is accordingly named "SRm300." SRm300 also contains a novel and highly conserved N-terminal domain, several unique repeated motifs rich in S, R, and proline residues, and two very long polyserine tracts. Surprisingly, specific depletion of SRm300 does not prevent the splicing of pre-mRNAs shown previously to require SRm160/300. Addition of recombinant SRm160 alone to SRm160/300-depleted reactions specifically activates splicing. The results indicate that SRm160 may be the more critical component of the SRm160/300 coactivator in the splicing of SRm160/300-dependent pre-mRNAs. (+info)The nuclear matrix is a complex network of fibrous proteins that forms the structural framework inside the nucleus of a cell. It is involved in various essential cellular processes, such as DNA replication, transcription, repair, and RNA processing. The nuclear matrix provides a platform for these activities by organizing and compacting chromatin, maintaining the spatial organization of the nucleus, and interacting with regulatory proteins and nuclear enzymes. It's crucial for preserving genome stability and regulating gene expression.
Nuclear matrix-associated proteins (NMAPs) are a group of structural and functional proteins that are associated with the nuclear matrix, a network of fibers within the nucleus of a eukaryotic cell. The nuclear matrix provides support to the nuclear envelope and plays a role in DNA replication, transcription, and repair. NMAPs can be categorized into several groups based on their functions, including:
1. Scaffold proteins: These proteins provide structural support to the nuclear matrix and help maintain its architecture.
2. Enzymes: These proteins are involved in various biochemical reactions, such as DNA replication and repair, RNA processing, and chromatin remodeling.
3. Transcription factors: These proteins regulate gene expression by binding to specific DNA sequences and interacting with the transcription machinery.
4. Chromatin-associated proteins: These proteins are involved in the organization and regulation of chromatin structure and function.
5. Signal transduction proteins: These proteins transmit signals from the extracellular environment to the nucleus, regulating gene expression and other nuclear functions.
NMAPs have been implicated in various cellular processes, including cell cycle regulation, differentiation, apoptosis, and oncogenesis. Therefore, understanding the structure and function of NMAPs is crucial for elucidating the mechanisms underlying these processes and developing novel therapeutic strategies for various diseases, including cancer.
The extracellular matrix (ECM) is a complex network of biomolecules that provides structural and biochemical support to cells in tissues and organs. It is composed of various proteins, glycoproteins, and polysaccharides, such as collagens, elastin, fibronectin, laminin, and proteoglycans. The ECM plays crucial roles in maintaining tissue architecture, regulating cell behavior, and facilitating communication between cells. It provides a scaffold for cell attachment, migration, and differentiation, and helps to maintain the structural integrity of tissues by resisting mechanical stresses. Additionally, the ECM contains various growth factors, cytokines, and chemokines that can influence cellular processes such as proliferation, survival, and differentiation. Overall, the extracellular matrix is essential for the normal functioning of tissues and organs, and its dysregulation can contribute to various pathological conditions, including fibrosis, cancer, and degenerative diseases.
Nuclear antigens are proteins or other molecules found in the nucleus of a cell that can stimulate an immune response and produce antibodies when they are recognized as foreign by the body's immune system. These antigens are normally located inside the cell and are not typically exposed to the immune system, but under certain circumstances, such as during cell death or damage, they may be released and become targets of the immune system.
Nuclear antigens can play a role in the development of some autoimmune diseases, such as systemic lupus erythematosus (SLE), where the body's immune system mistakenly attacks its own cells and tissues. In SLE, nuclear antigens such as double-stranded DNA and nucleoproteins are common targets of the abnormal immune response.
Testing for nuclear antigens is often used in the diagnosis and monitoring of autoimmune diseases. For example, a positive test for anti-double-stranded DNA antibodies is a specific indicator of SLE and can help confirm the diagnosis. However, it's important to note that not all people with SLE will have positive nuclear antigen tests, and other factors must also be considered in making a diagnosis.
Matrix Attachment Regions (MARs) are specific DNA sequences that are involved in the attachment of chromatin to the nuclear matrix. The nuclear matrix is a protein structure within the nucleus of a cell, which provides a framework for the organization and function of genetic material. MARs are believed to play a role in the spatial organization of chromosomes within the nucleus, as well as in the regulation of gene expression. They can serve as binding sites for various proteins and enzymes that are involved in DNA replication, transcription, and repair. The precise mechanisms by which MARs function are still being studied and elucidated.
Matrix Attachment Regions (MARs) are specific DNA sequences that serve as anchor points for the attachment of chromosomes to the nuclear matrix, a network of fibers within the nucleus of a eukaryotic cell. MAR Binding Proteins (MARBPs) are a class of proteins that selectively bind to these MARs and play crucial roles in various nuclear processes such as DNA replication, transcription, repair, and chromosome organization.
MARBPs can be categorized into two main groups: structural and functional. Structural MARBPs help tether chromatin to the nuclear matrix and maintain the higher-order structure of chromatin. Functional MARBPs are involved in regulating gene expression, DNA replication, and repair by interacting with various transcription factors, enzymes, and other proteins at the MARs.
Examples of MARBPs include SATB1 (Special AT-rich sequence-binding protein 1), CTCF (CCCTC-binding factor), and NuMA (Nuclear Mitotic Apparatus protein). These proteins have been shown to play essential roles in chromatin organization, gene regulation, and cellular processes such as differentiation and development.
In summary, Matrix Attachment Region Binding Proteins are a class of nuclear proteins that selectively bind to specific DNA sequences called Matrix Attachment Regions (MARs). They contribute to various nuclear processes, including chromatin organization, gene regulation, DNA replication, and repair.
The cell nucleus is a membrane-bound organelle found in the eukaryotic cells (cells with a true nucleus). It contains most of the cell's genetic material, organized as DNA molecules in complex with proteins, RNA molecules, and histones to form chromosomes.
The primary function of the cell nucleus is to regulate and control the activities of the cell, including growth, metabolism, protein synthesis, and reproduction. It also plays a crucial role in the process of mitosis (cell division) by separating and protecting the genetic material during this process. The nuclear membrane, or nuclear envelope, surrounding the nucleus is composed of two lipid bilayers with numerous pores that allow for the selective transport of molecules between the nucleoplasm (nucleus interior) and the cytoplasm (cell exterior).
The cell nucleus is a vital structure in eukaryotic cells, and its dysfunction can lead to various diseases, including cancer and genetic disorders.
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.
Extracellular matrix (ECM) proteins are a group of structural and functional molecules that provide support, organization, and regulation to the cells in tissues and organs. The ECM is composed of a complex network of proteins, glycoproteins, and carbohydrates that are secreted by the cells and deposited outside of them.
ECM proteins can be classified into several categories based on their structure and function, including:
1. Collagens: These are the most abundant ECM proteins and provide strength and stability to tissues. They form fibrils that can withstand high tensile forces.
2. Proteoglycans: These are complex molecules made up of a core protein and one or more glycosaminoglycan (GAG) chains. The GAG chains attract water, making proteoglycans important for maintaining tissue hydration and resilience.
3. Elastin: This is an elastic protein that allows tissues to stretch and recoil, such as in the lungs and blood vessels.
4. Fibronectins: These are large glycoproteins that bind to cells and ECM components, providing adhesion, migration, and signaling functions.
5. Laminins: These are large proteins found in basement membranes, which provide structural support for epithelial and endothelial cells.
6. Tenascins: These are large glycoproteins that modulate cell adhesion and migration, and regulate ECM assembly and remodeling.
Together, these ECM proteins create a microenvironment that influences cell behavior, differentiation, and function. Dysregulation of ECM proteins has been implicated in various diseases, including fibrosis, cancer, and degenerative disorders.
Matrix metalloproteinase 2 (MMP-2), also known as gelatinase A, is an enzyme that belongs to the matrix metalloproteinase family. MMPs are involved in the breakdown of extracellular matrix components, and MMP-2 is responsible for degrading type IV collagen, a major component of the basement membrane. This enzyme plays a crucial role in various physiological processes, including tissue remodeling, wound healing, and angiogenesis. However, its dysregulation has been implicated in several pathological conditions, such as cancer, arthritis, and cardiovascular diseases. MMP-2 is synthesized as an inactive proenzyme and requires activation by other proteases or chemical modifications before it can exert its proteolytic activity.
Matrix metalloproteinases (MMPs) are a group of enzymes responsible for the degradation and remodeling of the extracellular matrix, the structural framework of most tissues in the body. These enzymes play crucial roles in various physiological processes such as tissue repair, wound healing, and embryonic development. They also participate in pathological conditions like tumor invasion, metastasis, and inflammatory diseases by breaking down the components of the extracellular matrix, including collagens, elastins, proteoglycans, and gelatins. MMPs are zinc-dependent endopeptidases that require activation from their proenzyme form to become fully functional. Their activity is tightly regulated at various levels, including gene expression, protein synthesis, and enzyme inhibition by tissue inhibitors of metalloproteinases (TIMPs). Dysregulation of MMPs has been implicated in several diseases, making them potential therapeutic targets for various clinical interventions.
Lamins are type V intermediate filament proteins that play a structural role in the nuclear envelope. They are the main components of the nuclear lamina, a mesh-like structure located inside the inner membrane of the nuclear envelope. Lamins are organized into homo- and heterodimers, which assemble into higher-order polymers to form the nuclear lamina. This structure provides mechanical support to the nucleus, helps maintain the shape and integrity of the nucleus, and plays a role in various nuclear processes such as DNA replication, transcription, and chromatin organization. Mutations in the genes encoding lamins have been associated with various human diseases, collectively known as laminopathies, which include muscular dystrophies, neuropathies, cardiomyopathies, and premature aging disorders.
Heterogeneous Nuclear Ribonucleoprotein U (hnRNP U) is a member of the family of heterogeneous nuclear ribonucleoproteins (hnRNPs). These proteins are involved in various aspects of RNA metabolism, including processing, transport, and stability. Specifically, hnRNP U, also known as scaffold attachment factor B (SAF-B), is a protein that binds to scaffold/matrix attachment regions (S/MARs) of the genome and helps to tether RNA to the nuclear matrix during transcription and processing. It has also been implicated in DNA repair processes.
I'm sorry for any confusion, but "Lamin Type B" is not a recognized medical term or concept in human physiology or pathology. The term "lamin" refers to proteins that are part of the nuclear lamina, a filamentous network found inside the nucleus of cells. There are three types of lamin proteins: A, B, and C.
Lamin A and Lamin C are produced from the LMNA gene, while Lamin B1 and Lamin B2 are produced from the LMNB1 and LMNB2 genes, respectively. Therefore, "Lamin Type B" is not a specific designation, but rather encompasses two distinct proteins: Lamin B1 and Lamin B2.
If you have any questions about lamins or another medical topic, please provide more context or clarify your question so I can give you a more accurate answer.
Nucleoproteins are complexes formed by the association of proteins with nucleic acids (DNA or RNA). These complexes play crucial roles in various biological processes, such as packaging and protecting genetic material, regulating gene expression, and replication and repair of DNA. In these complexes, proteins interact with nucleic acids through electrostatic, hydrogen bonding, and other non-covalent interactions, leading to the formation of stable structures that help maintain the integrity and function of the genetic material. Some well-known examples of nucleoproteins include histones, which are involved in DNA packaging in eukaryotic cells, and reverse transcriptase, an enzyme found in retroviruses that transcribes RNA into DNA.
Bone matrix refers to the non-cellular component of bone that provides structural support and functions as a reservoir for minerals, such as calcium and phosphate. It is made up of organic and inorganic components. The organic component consists mainly of type I collagen fibers, which provide flexibility and tensile strength to the bone. The inorganic component is primarily composed of hydroxyapatite crystals, which give bone its hardness and compressive strength. Bone matrix also contains other proteins, growth factors, and signaling molecules that regulate bone formation, remodeling, and repair.
Chromatin is the complex of DNA, RNA, and proteins that make up the chromosomes in the nucleus of a cell. It is responsible for packaging the long DNA molecules into a more compact form that fits within the nucleus. Chromatin is made up of repeating units called nucleosomes, which consist of a histone protein octamer wrapped tightly by DNA. The structure of chromatin can be altered through chemical modifications to the histone proteins and DNA, which can influence gene expression and other cellular processes.
Medical Definition of Matrix Metalloproteinase 1 (MMP-1):
Matrix metalloproteinase 1, also known as collagenase-1 or fibroblast collagenase, is a member of the matrix metalloproteinase family of enzymes. These enzymes are involved in degrading and remodeling extracellular matrix components, such as collagens, gelatins, and other proteins. MMP-1 specifically targets interstitial collagens (types I, II, III, VII, and X) and plays a crucial role in tissue repair, wound healing, and pathological processes like tumor invasion and metastasis. It is secreted as an inactive proenzyme and requires activation before it can carry out its proteolytic functions. MMP-1 activity is regulated at various levels, including transcription, activation, and inhibition by endogenous tissue inhibitors of metalloproteinases (TIMPs). Dysregulation of MMP-1 has been implicated in several diseases, such as arthritis, cancer, and fibrosis.
Matrix metalloproteinase inhibitors (MMPIs) are a class of pharmaceutical compounds that work by inhibiting the activity of matrix metalloproteinases (MMPs), which are a family of enzymes involved in the breakdown and remodeling of extracellular matrix (ECM) proteins. MMPs play important roles in various physiological processes, including tissue repair, wound healing, and angiogenesis, but they can also contribute to the pathogenesis of several diseases, such as cancer, arthritis, and cardiovascular disease.
MMPIs are designed to block the activity of MMPs by binding to their active site or zinc-binding domain, thereby preventing them from degrading ECM proteins. These inhibitors can be broad-spectrum, targeting multiple MMPs, or selective, targeting specific MMP isoforms.
MMPIs have been studied as potential therapeutic agents for various diseases, including cancer, where they have shown promise in reducing tumor growth, invasion, and metastasis by inhibiting the activity of MMPs that promote these processes. However, clinical trials with MMPIs have yielded mixed results, and some studies have suggested that broad-spectrum MMPIs may have off-target effects that can lead to adverse side effects. Therefore, there is ongoing research into developing more selective MMPIs that target specific MMP isoforms involved in disease pathogenesis while minimizing off-target effects.
Deoxyribonucleic acid (DNA) is the genetic material present in the cells of organisms where it is responsible for the storage and transmission of hereditary information. DNA is a long molecule that consists of two strands coiled together to form a double helix. Each strand is made up of a series of four nucleotide bases - adenine (A), guanine (G), cytosine (C), and thymine (T) - that are linked together by phosphate and sugar groups. The sequence of these bases along the length of the molecule encodes genetic information, with A always pairing with T and C always pairing with G. This base-pairing allows for the replication and transcription of DNA, which are essential processes in the functioning and reproduction of all living organisms.
I'm not aware of a medical term called "blotting, Southwestern." The term "blotting" in the context of laboratory science refers to a technique used to transfer or visualize molecules from one surface to another, typically using a liquid or gel. "Southwestern" is a geographical term that can refer to a region in the southwestern United States. It's possible that you may be referring to a specific medical or scientific technique that combines blotting and Southwestern, but I was unable to find any relevant information on this topic.
If you meant something different or need more information about laboratory techniques for transferring or visualizing molecules, please let me know!
Heterogeneous Nuclear RNA (hnRNA) is a type of RNA molecule found in the nucleus of eukaryotic cells during the early stages of gene expression. The term "heterogeneous" refers to the diverse range of sizes and structures that these RNAs exhibit, which can vary from several hundred to tens of thousands of nucleotides in length.
HnRNA is transcribed from DNA templates by the enzyme RNA polymerase II and includes both introns (non-coding sequences) and exons (coding sequences) that will eventually be spliced together to form mature mRNA molecules. HnRNA also contains additional sequences, such as 5' cap structures and 3' poly(A) tails, which are added during post-transcriptional processing.
Because hnRNA is a precursor to mature mRNA, it is often used as a marker for transcriptionally active genes. However, not all hnRNA molecules are ultimately processed into mRNA; some may be degraded or converted into other types of RNA, such as microRNAs or long non-coding RNAs.
Overall, hnRNA plays a critical role in the regulation and expression of genes in eukaryotic cells.
Two-dimensional (2D) gel electrophoresis is a type of electrophoretic technique used in the separation and analysis of complex protein mixtures. This method combines two types of electrophoresis – isoelectric focusing (IEF) and sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) – to separate proteins based on their unique physical and chemical properties in two dimensions.
In the first dimension, IEF separates proteins according to their isoelectric points (pI), which is the pH at which a protein carries no net electrical charge. The proteins are focused into narrow zones along a pH gradient established within a gel strip. In the second dimension, SDS-PAGE separates the proteins based on their molecular weights by applying an electric field perpendicular to the first dimension.
The separated proteins form distinct spots on the 2D gel, which can be visualized using various staining techniques. The resulting protein pattern provides valuable information about the composition and modifications of the protein mixture, enabling researchers to identify and compare different proteins in various samples. Two-dimensional gel electrophoresis is widely used in proteomics research, biomarker discovery, and quality control in protein production.
HeLa cells are a type of immortalized cell line used in scientific research. They are derived from a cancer that developed in the cervical tissue of Henrietta Lacks, an African-American woman, in 1951. After her death, cells taken from her tumor were found to be capable of continuous division and growth in a laboratory setting, making them an invaluable resource for medical research.
HeLa cells have been used in a wide range of scientific studies, including research on cancer, viruses, genetics, and drug development. They were the first human cell line to be successfully cloned and are able to grow rapidly in culture, doubling their population every 20-24 hours. This has made them an essential tool for many areas of biomedical research.
It is important to note that while HeLa cells have been instrumental in numerous scientific breakthroughs, the story of their origin raises ethical questions about informed consent and the use of human tissue in research.
Matrix metalloproteinase 3 (MMP-3), also known as stromelysin-1, is a member of the matrix metalloproteinase family. These are a group of enzymes involved in the degradation of the extracellular matrix, the network of proteins and other molecules that provides structural and biochemical support to surrounding cells. MMP-3 is secreted by various cell types, including fibroblasts, synovial cells, and chondrocytes, in response to inflammatory cytokines.
MMP-3 has the ability to degrade several extracellular matrix components, such as proteoglycans, laminin, fibronectin, and various types of collagen. It also plays a role in processing and activating other MMPs, thereby contributing to the overall breakdown of the extracellular matrix. This activity is crucial during processes like tissue remodeling, wound healing, and embryonic development; however, uncontrolled or excessive MMP-3 activation can lead to pathological conditions, including arthritis, cancer, and cardiovascular diseases.
In summary, Matrix metalloproteinase 3 (MMP-3) is a proteolytic enzyme involved in the degradation of the extracellular matrix and the activation of other MMPs. Its dysregulation has been implicated in several diseases.
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.
Cell fractionation is a laboratory technique used to separate different cellular components or organelles based on their size, density, and other physical properties. This process involves breaking open the cell (usually through homogenization), and then separating the various components using various methods such as centrifugation, filtration, and ultracentrifugation.
The resulting fractions can include the cytoplasm, mitochondria, nuclei, endoplasmic reticulum, Golgi apparatus, lysosomes, peroxisomes, and other organelles. Each fraction can then be analyzed separately to study the biochemical and functional properties of the individual components.
Cell fractionation is a valuable tool in cell biology research, allowing scientists to study the structure, function, and interactions of various cellular components in a more detailed and precise manner.
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.
Interphase is a phase in the cell cycle during which the cell primarily performs its functions of growth and DNA replication. It is the longest phase of the cell cycle, consisting of G1 phase (during which the cell grows and prepares for DNA replication), S phase (during which DNA replication occurs), and G2 phase (during which the cell grows further and prepares for mitosis). During interphase, the chromosomes are in their relaxed, extended form and are not visible under the microscope. Interphase is followed by mitosis, during which the chromosomes condense and separate to form two genetically identical daughter cells.
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.
Molecular weight, also known as molecular mass, is the mass of a molecule. It is expressed in units of atomic mass units (amu) or daltons (Da). Molecular weight is calculated by adding up the atomic weights of each atom in a molecule. It is a useful property in chemistry and biology, as it can be used to determine the concentration of a substance in a solution, or to calculate the amount of a substance that will react with another in a chemical reaction.
Iodobenzoates are organic compounds that consist of a benzoic acid molecule with an iodine atom substituted at the carboxyl group. Specifically, an iodobenzoate is an ester derived from benzoic acid and iodine, in which the hydrogen atom of the carboxylic acid group (-COOH) has been replaced by an iodine atom.
The general formula for an iodobenzoate can be represented as C6H4(IO)CO2R, where R represents an alkyl or aryl group. Iodobenzoates have various applications in organic synthesis and pharmaceuticals, including the production of dyes, drugs, and other chemical intermediates.
It's worth noting that iodobenzoates are not a medical condition or diagnosis but rather a class of chemical compounds with potential uses in medical research and therapeutics.
"Physarum polycephalum" is not a medical term, but a scientific name for a type of slime mold. It's a unicellular organism that behaves as a single entity, despite not having a true nervous system or muscles. It's often studied in biological research due to its unique abilities in problem-solving and adaptation.
However, if you're asking about the medical relevance of slime molds, they have been researched for their potential biomedical applications, such as drug discovery and toxicology studies. Some compounds produced by slime molds have shown promising antibiotic, antifungal, and anticancer properties. But it's important to note that these are early-stage research findings and further investigation is needed before any medical applications can be confirmed.
The Fluorescent Antibody Technique (FAT) is a type of immunofluorescence assay used in laboratory medicine and pathology for the detection and localization of specific antigens or antibodies in tissues, cells, or microorganisms. In this technique, a fluorescein-labeled antibody is used to selectively bind to the target antigen or antibody, forming an immune complex. When excited by light of a specific wavelength, the fluorescein label emits light at a longer wavelength, typically visualized as green fluorescence under a fluorescence microscope.
The FAT is widely used in diagnostic microbiology for the identification and characterization of various bacteria, viruses, fungi, and parasites. It has also been applied in the diagnosis of autoimmune diseases and certain cancers by detecting specific antibodies or antigens in patient samples. The main advantage of FAT is its high sensitivity and specificity, allowing for accurate detection and differentiation of various pathogens and disease markers. However, it requires specialized equipment and trained personnel to perform and interpret the results.
Electron microscopy (EM) is a type of microscopy that uses a beam of electrons to create an image of the sample being examined, resulting in much higher magnification and resolution than light microscopy. There are several types of electron microscopy, including transmission electron microscopy (TEM), scanning electron microscopy (SEM), and reflection electron microscopy (REM).
In TEM, a beam of electrons is transmitted through a thin slice of the sample, and the electrons that pass through the sample are focused to form an image. This technique can provide detailed information about the internal structure of cells, viruses, and other biological specimens, as well as the composition and structure of materials at the atomic level.
In SEM, a beam of electrons is scanned across the surface of the sample, and the electrons that are scattered back from the surface are detected to create an image. This technique can provide information about the topography and composition of surfaces, as well as the structure of materials at the microscopic level.
REM is a variation of SEM in which the beam of electrons is reflected off the surface of the sample, rather than scattered back from it. This technique can provide information about the surface chemistry and composition of materials.
Electron microscopy has a wide range of applications in biology, medicine, and materials science, including the study of cellular structure and function, disease diagnosis, and the development of new materials and technologies.
"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.
DNA replication is the biological process by which DNA makes an identical copy of itself during cell division. It is a fundamental mechanism that allows genetic information to be passed down from one generation of cells to the next. During DNA replication, each strand of the double helix serves as a template for the synthesis of a new complementary strand. This results in the creation of two identical DNA molecules. The enzymes responsible for DNA replication include helicase, which unwinds the double helix, and polymerase, which adds nucleotides to the growing strands.
The nuclear envelope is a complex and double-membrane structure that surrounds the eukaryotic cell's nucleus. It consists of two distinct membranes: the outer nuclear membrane, which is continuous with the endoplasmic reticulum (ER) membrane, and the inner nuclear membrane, which is closely associated with the chromatin and nuclear lamina.
The nuclear envelope serves as a selective barrier between the nucleus and the cytoplasm, controlling the exchange of materials and information between these two cellular compartments. Nuclear pore complexes (NPCs) are embedded in the nuclear envelope at sites where the inner and outer membranes fuse, forming aqueous channels that allow for the passive or active transport of molecules, such as ions, metabolites, and RNA-protein complexes.
The nuclear envelope plays essential roles in various cellular processes, including DNA replication, transcription, RNA processing, and chromosome organization. Additionally, it is dynamically regulated during the cell cycle, undergoing disassembly and reformation during mitosis to facilitate equal distribution of genetic material between daughter cells.
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.
Electrophoresis, polyacrylamide gel (EPG) is a laboratory technique used to separate and analyze complex mixtures of proteins or nucleic acids (DNA or RNA) based on their size and electrical charge. This technique utilizes a matrix made of cross-linked polyacrylamide, a type of gel, which provides a stable and uniform environment for the separation of molecules.
In this process:
1. The polyacrylamide gel is prepared by mixing acrylamide monomers with a cross-linking agent (bis-acrylamide) and a catalyst (ammonium persulfate) in the presence of a buffer solution.
2. The gel is then poured into a mold and allowed to polymerize, forming a solid matrix with uniform pore sizes that depend on the concentration of acrylamide used. Higher concentrations result in smaller pores, providing better resolution for separating smaller molecules.
3. Once the gel has set, it is placed in an electrophoresis apparatus containing a buffer solution. Samples containing the mixture of proteins or nucleic acids are loaded into wells on the top of the gel.
4. An electric field is applied across the gel, causing the negatively charged molecules to migrate towards the positive electrode (anode) while positively charged molecules move toward the negative electrode (cathode). The rate of migration depends on the size, charge, and shape of the molecules.
5. Smaller molecules move faster through the gel matrix and will migrate farther from the origin compared to larger molecules, resulting in separation based on size. Proteins and nucleic acids can be selectively stained after electrophoresis to visualize the separated bands.
EPG is widely used in various research fields, including molecular biology, genetics, proteomics, and forensic science, for applications such as protein characterization, DNA fragment analysis, cloning, mutation detection, and quality control of nucleic acid or protein samples.
'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.
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.
In the context of medical and biological sciences, a "binding site" refers to a specific location on a protein, molecule, or cell where another molecule can attach or bind. This binding interaction can lead to various functional changes in the original protein or molecule. The other molecule that binds to the binding site is often referred to as a ligand, which can be a small molecule, ion, or even another protein.
The binding between a ligand and its target binding site can be specific and selective, meaning that only certain ligands can bind to particular binding sites with high affinity. This specificity plays a crucial role in various biological processes, such as signal transduction, enzyme catalysis, or drug action.
In the case of drug development, understanding the location and properties of binding sites on target proteins is essential for designing drugs that can selectively bind to these sites and modulate protein function. This knowledge can help create more effective and safer therapeutic options for various diseases.
Deoxyribonuclease I (DNase I) is an enzyme that cleaves the phosphodiester bonds in the DNA molecule, breaking it down into smaller pieces. It is also known as DNase A or bovine pancreatic deoxyribonuclease. This enzyme specifically hydrolyzes the internucleotide linkages of DNA by cleaving the phosphodiester bond between the 3'-hydroxyl group of one deoxyribose sugar and the phosphate group of another, leaving 3'-phosphomononucleotides as products.
DNase I plays a crucial role in various biological processes, including DNA degradation during apoptosis (programmed cell death), DNA repair, and host defense against pathogens by breaking down extracellular DNA from invading microorganisms or damaged cells. It is widely used in molecular biology research for applications such as DNA isolation, removing contaminating DNA from RNA samples, and generating defined DNA fragments for cloning purposes. DNase I can be found in various sources, including bovine pancreas, human tears, and bacterial cultures.
Protein binding, in the context of medical and biological sciences, refers to the interaction between a protein and another molecule (known as the ligand) that results in a stable complex. This process is often reversible and can be influenced by various factors such as pH, temperature, and concentration of the involved molecules.
In clinical chemistry, protein binding is particularly important when it comes to drugs, as many of them bind to proteins (especially albumin) in the bloodstream. The degree of protein binding can affect a drug's distribution, metabolism, and excretion, which in turn influence its therapeutic effectiveness and potential side effects.
Protein-bound drugs may be less available for interaction with their target tissues, as only the unbound or "free" fraction of the drug is active. Therefore, understanding protein binding can help optimize dosing regimens and minimize adverse reactions.
Matrix metalloproteinase 14 (MMP-14), also known as membrane-type 1 matrix metalloproteinase (MT1-MMP), is a type of enzyme that belongs to the matrix metalloproteinase (MMP) family. MMPs are involved in the breakdown and remodeling of extracellular matrix (ECM) components, such as collagens, elastins, and proteoglycans.
MMP-14 is unique among MMPs because it is membrane-bound and can be found on the cell surface. It plays a crucial role in the activation of other MMPs, including proMMP-2, by cleaving their prodomains. Additionally, MMP-14 can degrade various ECM components directly, such as collagen types I, II, III, and IV, gelatin, fibronectin, and laminin.
The regulation of MMP-14 is complex and involves transcriptional, post-transcriptional, and post-translational mechanisms. Its expression can be induced by various growth factors, cytokines, and oncogenes, and it can be regulated by tissue inhibitors of metalloproteinases (TIMPs).
MMP-14 has been implicated in several physiological processes, including wound healing, angiogenesis, and cell migration. However, its overexpression or dysregulation has also been associated with various pathological conditions, such as cancer, arthritis, and cardiovascular diseases.
Matrix metalloproteinase 7 (MMP-7), also known as matrilysin, is a type of enzyme that belongs to the matrix metalloproteinase family. These enzymes are capable of degrading various components of the extracellular matrix, which is the structural framework of tissues in the body. MMP-7 has a broad range of substrates and can break down proteins such as collagens, gelatins, and caseins, as well as other matrix proteins. It plays important roles in tissue remodeling, wound healing, and cell migration, among other processes.
MMP-7 is synthesized and secreted by various cells, including epithelial cells, fibroblasts, and immune cells. It is a small enzyme with a molecular weight of around 28 kDa and is secreted in an active form, unlike many other MMPs that are secreted as inactive proenzymes and require activation by other proteases.
Increased expression of MMP-7 has been implicated in several pathological conditions, including cancer, where it can contribute to tumor invasion and metastasis by degrading the extracellular matrix and releasing growth factors. It has also been associated with inflammatory diseases such as rheumatoid arthritis and periodontitis.
I apologize for any confusion, but "Hypotrichida" is not a medical term. It is a taxonomic category in the field of biology, specifically in protistology, which is the study of protozoa. Hypotrichida is an order of ciliates, a group of unicellular organisms with hair-like structures called cilia.
In a biological context, Hypotrichida are characterized by their complex ciliary patterns and the presence of a compound oral apparatus. They are commonly found in various aquatic environments and some can be found in the gut of animals.
I hope this clarifies any confusion. If you have any questions about biology or any medical topic, I'd be happy to help!
Medical Definition:
Matrix Metalloproteinase 13 (MMP-13), also known as collagenase 3, is an enzyme belonging to the family of Matrix Metalloproteinases. These enzymes are involved in the degradation of extracellular matrix components, playing crucial roles in various physiological and pathological processes such as tissue remodeling, wound healing, and cancer progression.
MMP-13 has a specific affinity for cleaving type II collagen, one of the major structural proteins found in articular cartilage. It is also capable of degrading other extracellular matrix components like proteoglycans, elastin, and gelatin. This enzyme is primarily produced by chondrocytes, synovial fibroblasts, and osteoblasts.
Increased expression and activity of MMP-13 have been implicated in the pathogenesis of several diseases, most notably osteoarthritis (OA) and cancer. In OA, overexpression of MMP-13 leads to excessive degradation of articular cartilage, contributing to joint damage and degeneration. In cancer, MMP-13 facilitates tumor cell invasion and metastasis by breaking down the surrounding extracellular matrix.
Regulation of MMP-13 activity is essential for maintaining tissue homeostasis and preventing disease progression. Various therapeutic strategies aiming to inhibit MMP-13 activity are being explored as potential treatments for osteoarthritis and cancer.
Subcellular fractions refer to the separation and collection of specific parts or components of a cell, including organelles, membranes, and other structures, through various laboratory techniques such as centrifugation and ultracentrifugation. These fractions can be used in further biochemical and molecular analyses to study the structure, function, and interactions of individual cellular components. Examples of subcellular fractions include nuclear extracts, mitochondrial fractions, microsomal fractions (membrane vesicles), and cytosolic fractions (cytoplasmic extracts).
Collagen is the most abundant protein in the human body, and it is a major component of connective tissues such as tendons, ligaments, skin, and bones. Collagen provides structure and strength to these tissues and helps them to withstand stretching and tension. It is made up of long chains of amino acids, primarily glycine, proline, and hydroxyproline, which are arranged in a triple helix structure. There are at least 16 different types of collagen found in the body, each with slightly different structures and functions. Collagen is important for maintaining the integrity and health of tissues throughout the body, and it has been studied for its potential therapeutic uses in various medical conditions.
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).
Ribonucleoproteins (RNPs) are complexes composed of ribonucleic acid (RNA) and proteins. They play crucial roles in various cellular processes, including gene expression, RNA processing, transport, stability, and degradation. Different types of RNPs exist, such as ribosomes, spliceosomes, and signal recognition particles, each having specific functions in the cell.
Ribosomes are large RNP complexes responsible for protein synthesis, where messenger RNA (mRNA) is translated into proteins. They consist of two subunits: a smaller subunit containing ribosomal RNA (rRNA) and proteins that recognize the start codon on mRNA, and a larger subunit with rRNA and proteins that facilitate peptide bond formation during translation.
Spliceosomes are dynamic RNP complexes involved in pre-messenger RNA (pre-mRNA) splicing, where introns (non-coding sequences) are removed, and exons (coding sequences) are joined together to form mature mRNA. Spliceosomes consist of five small nuclear ribonucleoproteins (snRNPs), each containing a specific small nuclear RNA (snRNA) and several proteins, as well as numerous additional proteins.
Other RNP complexes include signal recognition particles (SRPs), which are responsible for targeting secretory and membrane proteins to the endoplasmic reticulum during translation, and telomerase, an enzyme that maintains the length of telomeres (the protective ends of chromosomes) by adding repetitive DNA sequences using its built-in RNA component.
In summary, ribonucleoproteins are essential complexes in the cell that participate in various aspects of RNA metabolism and protein synthesis.
I'm sorry for any confusion, but "Leukemia L5178" is not a recognized medical term or classification for leukemia. The World Health Organization (WHO) and other organizations have established specific classifications for different types of leukemias based on factors such as cell type, genetic mutations, and other characteristics. However, "L5178" does not appear in these classifications.
It's possible that "L5178" might refer to a specific research cell line used in scientific studies, but without more context, it's difficult to provide a precise definition. If you have more information about where you encountered this term, I may be able to provide a more accurate response.
The nucleolus is a structure found within the nucleus of eukaryotic cells (cells that contain a true nucleus). It plays a central role in the production and assembly of ribosomes, which are complex molecular machines responsible for protein synthesis. The nucleolus is not a distinct organelle with a membrane surrounding it, but rather a condensed region within the nucleus where ribosomal biogenesis takes place.
The process of ribosome formation begins in the nucleolus with the transcription of ribosomal DNA (rDNA) genes into long precursor RNA molecules called rRNAs (ribosomal RNAs). Within the nucleolus, these rRNA molecules are cleaved, modified, and assembled together with ribosomal proteins to form small and large ribosomal subunits. Once formed, these subunits are transported through the nuclear pores to the cytoplasm, where they come together to form functional ribosomes that can engage in protein synthesis.
In addition to its role in ribosome biogenesis, the nucleolus has been implicated in other cellular processes such as stress response, cell cycle regulation, and aging. Changes in nucleolar structure and function have been associated with various diseases, including cancer and neurodegenerative 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.
Fluorescence microscopy is a type of microscopy that uses fluorescent dyes or proteins to highlight and visualize specific components within a sample. In this technique, the sample is illuminated with high-energy light, typically ultraviolet (UV) or blue light, which excites the fluorescent molecules causing them to emit lower-energy, longer-wavelength light, usually visible light in the form of various colors. This emitted light is then collected by the microscope and detected to produce an image.
Fluorescence microscopy has several advantages over traditional brightfield microscopy, including the ability to visualize specific structures or molecules within a complex sample, increased sensitivity, and the potential for quantitative analysis. It is widely used in various fields of biology and medicine, such as cell biology, neuroscience, and pathology, to study the structure, function, and interactions of cells and proteins.
There are several types of fluorescence microscopy techniques, including widefield fluorescence microscopy, confocal microscopy, two-photon microscopy, and total internal reflection fluorescence (TIRF) microscopy, each with its own strengths and limitations. These techniques can provide valuable insights into the behavior of cells and proteins in health and disease.
Immunoelectron microscopy (IEM) is a specialized type of electron microscopy that combines the principles of immunochemistry and electron microscopy to detect and localize specific antigens within cells or tissues at the ultrastructural level. This technique allows for the visualization and identification of specific proteins, viruses, or other antigenic structures with a high degree of resolution and specificity.
In IEM, samples are first fixed, embedded, and sectioned to prepare them for electron microscopy. The sections are then treated with specific antibodies that have been labeled with electron-dense markers, such as gold particles or ferritin. These labeled antibodies bind to the target antigens in the sample, allowing for their visualization under an electron microscope.
There are several different methods of IEM, including pre-embedding and post-embedding techniques. Pre-embedding involves labeling the antigens before embedding the sample in resin, while post-embedding involves labeling the antigens after embedding. Post-embedding techniques are generally more commonly used because they allow for better preservation of ultrastructure and higher resolution.
IEM is a valuable tool in many areas of research, including virology, bacteriology, immunology, and cell biology. It can be used to study the structure and function of viruses, bacteria, and other microorganisms, as well as the distribution and localization of specific proteins and antigens within cells and tissues.
Fibronectin is a high molecular weight glycoprotein that is found in many tissues and body fluids, including plasma, connective tissue, and the extracellular matrix. It is composed of two similar subunits that are held together by disulfide bonds. Fibronectin plays an important role in cell adhesion, migration, and differentiation by binding to various cell surface receptors, such as integrins, and other extracellular matrix components, such as collagen and heparan sulfate proteoglycans.
Fibronectin has several isoforms that are produced by alternative splicing of a single gene transcript. These isoforms differ in their biological activities and can be found in different tissues and developmental stages. Fibronectin is involved in various physiological processes, such as wound healing, tissue repair, and embryonic development, and has been implicated in several pathological conditions, including fibrosis, tumor metastasis, and thrombosis.
Cell compartmentation, also known as intracellular compartmentalization, refers to the organization of cells into distinct functional and spatial domains. This is achieved through the separation of cellular components and biochemical reactions into membrane-bound organelles or compartments. Each compartment has its unique chemical composition and environment, allowing for specific biochemical reactions to occur efficiently and effectively without interfering with other processes in the cell.
Some examples of membrane-bound organelles include the nucleus, mitochondria, chloroplasts, endoplasmic reticulum, Golgi apparatus, lysosomes, peroxisomes, and vacuoles. These organelles have specific functions, such as energy production (mitochondria), protein synthesis and folding (endoplasmic reticulum and Golgi apparatus), waste management (lysosomes), and lipid metabolism (peroxisomes).
Cell compartmentation is essential for maintaining cellular homeostasis, regulating metabolic pathways, protecting the cell from potentially harmful substances, and enabling complex biochemical reactions to occur in a controlled manner. Dysfunction of cell compartmentation can lead to various diseases, including neurodegenerative disorders, cancer, and metabolic disorders.
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.
I'm sorry for any confusion, but Tetrathionic Acid is not a medical term. It is a chemical compound with the formula S4O62-. It's an acidic oxyanion of sulfur with the sulfur in the +5 oxidation state. It is not related to human health or medicine directly. If you have any questions about a medical topic, I'd be happy to help with that instead!
Matrix metalloproteinases (MMPs) are a group of enzymes that can degrade various components of the extracellular matrix (ECM). Membrane-associated matrix metalloproteinases (MT-MMPs) are a subgroup of MMPs that are bound to the cell membrane through a transmembrane domain. They play important roles in ECM remodeling, tissue repair and regeneration, as well as in various pathological processes such as cancer invasion and metastasis.
MT-MMPs can activate other MMPs and convert pro-MMPs into their active forms. They also have the ability to cleave cell surface receptors, adhesion molecules, and growth factors, thereby regulating various cellular processes such as cell migration, proliferation, and apoptosis.
The membrane-associated matrix metalloproteinases include MMP-14 (MT1-MMP), MMP-15 (MT2-MMP), MMP-16 (MT3-MMP), MMP-17 (MT4-MMP), and MMP-24 (MT5-MMP). Dysregulation of MT-MMPs has been implicated in various diseases, including cancer, fibrosis, and neurodegenerative disorders.
Western blotting is a laboratory technique used in molecular biology to detect and quantify specific proteins in a mixture of many different proteins. This technique is commonly used to confirm the expression of a protein of interest, determine its size, and investigate its post-translational modifications. The name "Western" blotting distinguishes this technique from Southern blotting (for DNA) and Northern blotting (for RNA).
The Western blotting procedure involves several steps:
1. Protein extraction: The sample containing the proteins of interest is first extracted, often by breaking open cells or tissues and using a buffer to extract the proteins.
2. Separation of proteins by electrophoresis: The extracted proteins are then separated based on their size by loading them onto a polyacrylamide gel and running an electric current through the gel (a process called sodium dodecyl sulfate-polyacrylamide gel electrophoresis or SDS-PAGE). This separates the proteins according to their molecular weight, with smaller proteins migrating faster than larger ones.
3. Transfer of proteins to a membrane: After separation, the proteins are transferred from the gel onto a nitrocellulose or polyvinylidene fluoride (PVDF) membrane using an electric current in a process called blotting. This creates a replica of the protein pattern on the gel but now immobilized on the membrane for further analysis.
4. Blocking: The membrane is then blocked with a blocking agent, such as non-fat dry milk or bovine serum albumin (BSA), to prevent non-specific binding of antibodies in subsequent steps.
5. Primary antibody incubation: A primary antibody that specifically recognizes the protein of interest is added and allowed to bind to its target protein on the membrane. This step may be performed at room temperature or 4°C overnight, depending on the antibody's properties.
6. Washing: The membrane is washed with a buffer to remove unbound primary antibodies.
7. Secondary antibody incubation: A secondary antibody that recognizes the primary antibody (often coupled to an enzyme or fluorophore) is added and allowed to bind to the primary antibody. This step may involve using a horseradish peroxidase (HRP)-conjugated or alkaline phosphatase (AP)-conjugated secondary antibody, depending on the detection method used later.
8. Washing: The membrane is washed again to remove unbound secondary antibodies.
9. Detection: A detection reagent is added to visualize the protein of interest by detecting the signal generated from the enzyme-conjugated or fluorophore-conjugated secondary antibody. This can be done using chemiluminescent, colorimetric, or fluorescent methods.
10. Analysis: The resulting image is analyzed to determine the presence and quantity of the protein of interest in the sample.
Western blotting is a powerful technique for identifying and quantifying specific proteins within complex mixtures. It can be used to study protein expression, post-translational modifications, protein-protein interactions, and more. However, it requires careful optimization and validation to ensure accurate and reproducible results.
Protamines are small, arginine-rich proteins that are found in the sperm cells of many organisms. They play a crucial role in the process of sperm maturation, also known as spermiogenesis. During this process, the DNA in the sperm cell is tightly packed and compacted by the protamines, which helps to protect the genetic material during its journey to fertilize an egg.
Protamines are typically composed of around 50-100 amino acids and have a high proportion of positively charged arginine residues, which allow them to interact strongly with the negatively charged DNA molecule. This interaction results in the formation of highly condensed chromatin structures that are resistant to enzymatic digestion and other forms of damage.
In addition to their role in sperm maturation, protamines have also been studied for their potential use in drug delivery and gene therapy applications. Their ability to bind strongly to DNA makes them attractive candidates for delivering drugs or genetic material directly to the nucleus of a cell. However, more research is needed to fully understand the potential benefits and risks associated with these applications.
The liver is a large, solid organ located in the upper right portion of the abdomen, beneath the diaphragm and above the stomach. It plays a vital role in several bodily functions, including:
1. Metabolism: The liver helps to metabolize carbohydrates, fats, and proteins from the food we eat into energy and nutrients that our bodies can use.
2. Detoxification: The liver detoxifies harmful substances in the body by breaking them down into less toxic forms or excreting them through bile.
3. Synthesis: The liver synthesizes important proteins, such as albumin and clotting factors, that are necessary for proper bodily function.
4. Storage: The liver stores glucose, vitamins, and minerals that can be released when the body needs them.
5. Bile production: The liver produces bile, a digestive juice that helps to break down fats in the small intestine.
6. Immune function: The liver plays a role in the immune system by filtering out bacteria and other harmful substances from the blood.
Overall, the liver is an essential organ that plays a critical role in maintaining overall health and well-being.
Nuclear matrix
TRIM27
MATR3
PRPF19
Len R. Troncale
Lamin B1
LIG1
MORC3
NMP22
EIF4A3
PDIA2
RuvB-like 1
EIF4A
Nuclear bodies
SATB1
SFPQ
CHMP1B
AKAP8L
Lamin B receptor
Thymopoietin
CHMP1A
Emerin
SPTBN4
PGK1
Nuclear lamina
Retinoblastoma protein
ENC1
Translin-associated factor X
Importin subunit alpha-6
Importin subunit alpha-7
Promyelocytic leukemia protein
Behavior of nuclear matrix proteins during camptothecin-induced apoptosis in HL-60 human leukemia cells
Searching for the S/MAR binding proteins; where DNA and nuclear matrix meet each other | Research Institute of Molecular...
Interaction of MAR‐sequences with nuclear matrix proteins<...
Surveillance for Recurrent Bladder Cancer: Practice Essentials, Imaging Studies, Complications of Cystoscopy
Nuclear matrix - Wikipedia
Pharmaceuticals
Hematuria in Adults
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LMNB2 lamin B2 [Homo sapiens (human)] - Gene - NCBI
Academic Unit: Biochemistry and Molecular Biophysics / Language: English | Search Results | Academic Commons
MATR3 gene: MedlinePlus Genetics
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PDF) Mapping of scaffold/matrix attachment regions in human genome: a data mining exercise
Page 1 | Search Results | Journal of Cell Biology | Rockefeller University Press
SP2 Sp2 transcription factor [Homo sapiens (human)] - Gene - NCBI
SMART: DEATH domain annotation
Turkish Journal of Medical Sciences | Vol 36 | No. 2
Purified Mouse Anti-SATB1
Purified Mouse Anti-SATB1
Refs3400-3499
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KoreaMed
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Citrate Synthase Polyclonal Antibody (PA5-22126)
Chromatin11
- A common feature, particularly evident for 125- and 160-kDa proteins, was their absence from cap-shaped chromatin marginations, whereas they were present in the areas of remaining decondensed chromatin. (nih.gov)
- These results show that, in addition to the well-known chromatin changes, nuclear organization undergoes other rearrangements during the apoptotic process. (nih.gov)
- abstract = "The recent discovery of DNA sequences responsible for the specific attachment of chromosomal DNA to the nuclear skeleton (MARs/SARs) was an important step towards our understanding of the functional and structural organization of eukaryotic chromatin [Mirkovitch et al. (nebraska.edu)
- The presence of intra-cellular proteins is common ground, and it is agreed that proteins such as the Scaffold, or Matrix Associated Proteins (SAR or MAR) have some role in the organisation of chromatin in the living cell. (wikipedia.org)
- The nuclear matrix proteome consists of structural proteins, chaperones, DNA/RNA-binding proteins, chromatin remodeling and transcription factors. (wikipedia.org)
- Lamin proteins are thought to be involved in nuclear stability, chromatin structure and gene expression. (nih.gov)
- Scaffold/matrix attachment regions (S/MARs) are DNA elements that serve to compartmentalize the chromatin into structural and functional domains. (researchgate.net)
- Central to the formation of nucleosomes, which consist of octameric histone cores with defined segments of chromatin wound around them, are the interactions of nucleosomes with nuclear matrix components. (bdbiosciences.com)
- 3420. J.R. Davie, 'Nuclear matrix, dynamic histone acetylation and transcriptionally active chromatin,' Mol. (nanomedicine.com)
- Eukaryotic genomes are functionally compartmentalized into chromatin domains by their attachment to a supporting structure that has traditionally been termed the nuclear matrix. (nih.gov)
- Modified FANCD2 interacts with BRCA2 PROTEIN in a stable complex with CHROMATIN, and it is involved in DNA REPAIR by homologous RECOMBINATION. (bvsalud.org)
Membrane9
- The nuclear lamina consists of a two-dimensional matrix of proteins located next to the inner nuclear membrane. (nih.gov)
- Ankyrins link integral membrane proteins to the spectrin-based membrane skeleton. (dana-farber.org)
- Hereditary defects in membrane skeleton proteins. (dana-farber.org)
- This indicates that AE1 and probably other integral membrane proteins have a 'lipid-anchoring' function. (dana-farber.org)
- In eukaryotic cells the genetic material is surrounded by a membrane system called the nuclear envelope (NE). (brookes.ac.uk)
- Mid-SUN proteins are a neglected family of conserved type III membrane proteins of ancient origin with representatives in plants, animals and fungi. (brookes.ac.uk)
- The role of SUN3 in the ER is reinforced by the identification of a protein interaction between SUN3 and the ER membrane-bound transcription factor maMYB. (brookes.ac.uk)
- The results highlight the importance of mid-SUNs as functional components of the ER and outer nuclear membrane. (brookes.ac.uk)
- Nasopharyngeal carcinoma (NPC) is notorious for the metastases, which are in close association with Epstein-Barr virus-encoded latent membrane protein 1 (LMP1). (scielo.br)
Mitogen-activa1
- Identification of a novel inhibitor of mitogen-activated protein kinase kinase. (rndsystems.com)
Lamins1
- Such structures are nuclear lamina, which consist of proteins termed lamins which can be also found in the nuclear matrix. (wikipedia.org)
Metabolism1
- The protein encoded by this gene is a Krebs tricarboxylic acid cycle enzyme that catalyzes the synthesis of citrate from oxaloacetate and acetyl coenzyme A. The enzyme is found in nearly all cells capable of oxidative metabolism. (thermofisher.com)
MRNA and protein expression3
- Here, we show that in primary human femoral head osteoarthritic and normal bovine chondrocytes, TWHF partially or completely inhibited mRNA and protein expression of tumor necrosis factor-α, interleukin (IL)-1, and IL-17-inducible MMP-3 and MMP-13. (aspetjournals.org)
- From experimentally validated target genes of these 86 miRNAs, pan-sensitive and pan-resistant genes with concordant mRNA and protein expression associated with in-vitro drug response to 19 NCCN-recommended breast cancer drugs were selected. (cdc.gov)
- The mRNA and protein expression of the 26 genes was associated with sensitivity or resistance to 18 NCCN-recommended drugs for treating breast cancer. (cdc.gov)
Kinase4
- Giordano G, Sanchez-Perez AM, Montoliu C, Berezney R, Malyavantham K, Costa LG, Calvete JJ, Felipo V. Activation of NMDA receptors induces protein kinase A-mediated phosphorylation and degradation of matrin 3. (medlineplus.gov)
- Mechanistic studies revealed no impact on the activation of extracellular signal-regulated kinase, p38, and c-Jun N-terminal kinase mitogen-activated protein kinases. (aspetjournals.org)
- Protein kinase C regulates human pluripotent stem cell self-renewal. (rndsystems.com)
- Specificity and mechanism of action of some commonly used protein kinase inhibitors. (rndsystems.com)
Genes1
- Alvarez JD, Yasui DH, Niida H, Joh T, Loh DY, Kohwi-Shigematsu T. The MAR-binding protein SATB1 orchestrates temporal and spatial expression of multiple genes during T-cell development. (bdbiosciences.com)
Structural3
- The complexity of NuMat is an indicator of diverse structural and functional significance of its proteins. (wikipedia.org)
- The nuclear matrix is a network of proteins that provides structural support for the nucleus and aids in several important nuclear functions. (medlineplus.gov)
- Lamin A/C proteins have key roles in nuclear structural integrity and chromosomal stability. (mdpi.com)
Sequences4
- Here, applying a different approach, we were able to "visualize" some of the skeletal proteins recognizing and specifically binding MAR‐sequences. (nebraska.edu)
- Histone H1 and nuclear actin are shown to be not only important components of the matrix, but to be involved in a highly efficient interaction with MAR‐sequences as well. (nebraska.edu)
- 3411. P.C. Park, U. De Boni, 'A specific conformation of the territory of chromosome 17 locates ERBB-2 sequences to a DNase-hypersensitive domain at the nuclear periphery,' Chromosoma 107(May 1998):87-95. (nanomedicine.com)
- The matching is com- plicated by the fact that there are protein modifications and the sequence databases store the unmodified sequences. (lu.se)
Antibody8
- While the antibody to the nucleolar isoform of DNA topoisomerase II gave a fluorescent pattern that was well-maintained until the late phases of apoptosis, the other three nuclear antigens showed marked modifications in their distribution. (nih.gov)
- E) Immunogold labeling of the nuclear tubules by using an antibody against the matrix protein. (cdc.gov)
- The 14/SATB1 monoclonal antibody specifically binds to the special AT-rich sequence binding protein 1 that is encoded by the SATB1 (SATB homeobox 1) gene. (bdbiosciences.com)
- Both methods yield antibody in solution that is free of most other soluble proteins, lipids, etc. (bdbiosciences.com)
- NDP52 antibody detects NDP52 protein at autophagosome by immunofluorescent analysis. (genetex.com)
- Immunoprecipitation of NDP52 protein from Jurkat whole cell extracts using 5 μg of NDP52 antibody (GTX115378). (genetex.com)
- NDP52 antibody detects NDP52 protein by western blot analysis. (genetex.com)
- Product Description google Mouse anti-Ectoderm-heural cortex protein 1 (ENC-1) Monoclonal Antibody (Unconjugated), suitable for WB, ELISA. (biosensis.com)
Attachment regions3
- S/MARs (scaffold/matrix attachment regions), the DNA regions that are known to attach genomic DNA to variety of nuclear proteins, show an ever increasing spectrum of established biological activities. (wikipedia.org)
- Specific genomic DNA segments that interact with the nuclear matrix are called scaffold or matrix attachment regions (SARs or MARs). (bdbiosciences.com)
- Above all, this is enabled by the so-called 'mass binding phenomenon' by which scaffold/matrix-attachment regions (S/MARs) reversibly associate with ubiquitous factors. (nih.gov)
Extracellular matrix8
- Here we show that changes in the composition of the extracellular matrix during this week can affect cardiomyocyte growth and differentiation in mice. (nature.com)
- We identify agrin, a component of neonatal extracellular matrix, as required for the full regenerative capacity of neonatal mouse hearts. (nature.com)
- Together, our results uncover a new inducer of mammalian heart regeneration and highlight fundamental roles of the extracellular matrix in cardiac repair. (nature.com)
- Henry, M. D. & Campbell, K. P. Dystroglycan: an extracellular matrix receptor linked to the cytoskeleton. (nature.com)
- We examined the correlation between nuclear deformation and cell functions such as cell proliferation, transfection and extracellular matrix protein type I collagen production. (cdc.gov)
- Fibrosis generally occurs due to dysregulation of mechanisms that control the usual extracellular matrix (ECM) turnover 11 . (bvsalud.org)
- IPF is characterized by damaged distal lung epithelium with excessive tissue scarring and extracellular matrix remodeling. (lu.se)
- Interestingly, we found epithelial YT signaling to be actively involved in extracellular matrix remodeling in the fibrotic lung epithelium through modulation of lysyl oxidase expression, a collagen crosslinking enzyme. (lu.se)
Tumor4
- The nuclear matrix composition on human cells has been proven to be cell type and tumor specific. (wikipedia.org)
- It has been clearly demonstrated that the nuclear matrix composition in a tumor is different from its normal counterparts. (wikipedia.org)
- The purpose of this study was to systematically review the effects of bladder tumor antigen (BTA) stat and nuclear matrix protein (NMP) 22 as a screening method in an asymptomatic population. (researchsquare.com)
- It also analyzes the strengths and weaknesses of screening methods and associated results using two non-invasive screening methods for bladder cancer-bladder tumor antigen (BTA) stat and nuclear matrix protein 22 (NMP 22)-in an asymptomatic population and in patients with suspicion of or a history of BC. (researchsquare.com)
Ribonucleoprotein2
- I. Partial separation into matrix protein fibrils and a residual ribonucleoprotein fraction. (rupress.org)
- Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ribonucleoprotein C and other RNA-binding proteins. (embl.de)
Electron3
- Moreover, the ultrastructural localization of both 125- and 160-kDa proteins was investigated by electron microscope immunocytochemistry with gold-conjugated secondary antibodies. (nih.gov)
- 3406. H. Ris, 'High-resolution field-emission scanning electron microscopy of nuclear pore complex,' Scanning 19(August 1997):368-375. (nanomedicine.com)
- A viral etiology, such as measles, has been proposed because nuclear inclusions in diseased osteoclasts that are similar to those seen in paramyxovirus-infected cells have been seen on electron microscopy. (msdmanuals.com)
Pore complex2
- 3405. D. Stoffler, B. Fahrenkrog, U. Aebi, 'The nuclear pore complex: From molecular architecture to functional dynamics,' Curr. (nanomedicine.com)
- 3407. S.A. Rutherford, M.W. Goldberg, T.D. Allen, 'Three-dimensional visualization of the route of protein import: the role of nuclear pore complex substructures,' Exp. (nanomedicine.com)
Mitochondrial matrix1
- This protein is nuclear encoded and transported into the mitochondrial matrix, where the mature form is found. (thermofisher.com)
Nucleus9
- In biology, the nuclear matrix is the network of fibres found throughout the inside of a cell nucleus after a specific method of chemical extraction. (wikipedia.org)
- According to some sources, most, if not all proteins found in nuclear matrix are the aggregates of proteins of structures that can be found in the nucleus of living cells. (wikipedia.org)
- The MATR3 gene provides instructions for making a protein called matrin 3, which is found in the nucleus of the cell as part of the nuclear matrix. (medlineplus.gov)
- The effect of the S85C mutation on the function of the matrin 3 protein is unknown, although one study indicates that the mutation may change the location of the protein in the nucleus. (medlineplus.gov)
- The fate of dsRNA in the nucleus: a p54(nrb)-containing complex mediates the nuclear retention of promiscuously A-to-I edited RNAs. (medlineplus.gov)
- ND10 bodies are nuclear domains appearing immunohistochemically as ten dots per nucleus. (genetex.com)
- ND10 proteins are removed from the nucleus by herpes simplex virus-1 infection and may have a role in viral life cycles. (genetex.com)
- Further, we demonstrated that cell proliferation, transfection, and type I collagen production were strongly associated with the nuclear volume, indicating that the nucleus serves as a critical mechanosensor for cell regulation. (cdc.gov)
- Our study delineated the relationships between focal adhesions, nucleus and cell function and highlighted that the nanotopography could regulate cell phenotype and function by modulating nuclear deformation. (cdc.gov)
Microscopy1
- I'm using cell and molecular biology techniques, biochemistry as well as microscopy to characterise the plant SUN proteins. (brookes.ac.uk)
Apoptosis4
- In this study we focused our attention on the behavior of four nuclear matrix proteins during the various stages of apoptosis in the HL-60 cell line exposed to the DNA topoisomerase I inhibitor, camptothecin. (nih.gov)
- Indirect immunofluorescence experiments were performed to follow these nuclear matrix antigens during apoptosis. (nih.gov)
- DEATH domain, found in proteins involved in cell death (apoptosis). (embl-heidelberg.de)
- TRAIL, also called Apo2L, is a cytotoxic protein that induces apoptosis of many transformed cell lines but not of normal tissues, even though its death domain-containing receptor, DR4, is expressed on both cell types. (embl-heidelberg.de)
Chaperones1
- The mitochondria have their own chaperones and proteolytic enzymes that remove damaged or unfolded proteins [ 18 - 20 ]. (hindawi.com)
Fatty acids2
- Important cytoprotective mechanisms activated by oxidative inflammatory conditions are mediated by nitrated fatty acids that covalently modify proteins to limit inflammation and oxidant stress. (aspetjournals.org)
- Palmitoylation refers back to the modification of the cysteine thiols in proteins by fatty acids, mostly palmitic acid, via 'thioester bond' formation. (yeastevolution.com)
Actin1
- ENC-1 is an actin-binding protein involved in the regulation of neuronal process formation and in differentiation of neural crest cells. (biosensis.com)
Genome3
- Toward this objective, ChIP-Seq data of 14 S/MAR binding proteins were analyzed and the binding site coordinates of these proteins were used to prepare a non-redundant S/MAR dataset of human genome. (researchgate.net)
- The aim of the project is to build a laboratory focused on the study of functionally important complexes of biomacromolecules, namely those of nucleic acids and proteins, which form so called genome architecture (telomeres, centromeres, A study of the genetic heterochromatin blocks, complexes of nuclear matrix, nucleosomes). (muni.cz)
- Previous studies have indicated that KIN17 is involved in global genome repair, DNA replication, transcription and regulation of the cell cycle as part of a multi-protein complex. (spandidos-publications.com)
Antibodies3
- Evidence is presented that proteins recognized by the anti‐HMG antibodies also participate in Mar‐interactions. (nebraska.edu)
- BTA works by using antibodies to identify concentrations of complement factor H-related proteins in urine that were raised as a result of BC. (researchsquare.com)
- Apart from being an acidic medium containing an assortment of antimicrobial molecules including antibodies (IgA and IgG), mucins, β-defensins, secretory leucocyte protease inhibitor (SLPI), neutrophil gelatinase-associated lipocalin (NGAL), surfactant protein etc. (frontiersin.org)
Fingerprint1
- We describe a statistical measure, Mass Distance Fingerprint, for automatic de novo detection of predominant peptide mass distances, i.e., putative protein mod- ifications. (lu.se)
Fluorescent1
- This methodology is predicated on metabolic labeling of a clickable analog of palmitic acid by parasitic cells, adopted by CuAAC (Copper-catalyzed Alkyne-Azide Cycloaddition response) Click on Chemistry to render palmitoylated proteins fluorescent. (yeastevolution.com)
Genetic2
- Along with the nuclear lamina, it supposedly aids in organizing the genetic information within the cell. (wikipedia.org)
- Some studies indicate that matrin 3 binds and stabilizes a type of RNA called messenger RNA (mRNA), which provides the genetic blueprint for proteins. (medlineplus.gov)
Lamina1
- During mitosis, the lamina matrix is reversibly disassembled as the lamin proteins are phosphorylated. (nih.gov)
Proteome2
- The proteostasis network (PN) is an assembly of distinct dynamic molecular pathways that control the functionality of the proteome (proteome homeodynamics) during protein synthesis, folding, trafficking, and degradation. (hindawi.com)
- Ageing leads to a gradual dysfunction of the proteostasis network and thus to proteome instability due to accumulation of damaged and/or misfolded proteins [ 2 ]. (hindawi.com)
Adapter1
- It is a substrate-specific adapter of an E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target protein. (biosensis.com)
Gene expression1
- There is evidence that the nuclear matrix is involved in regulation of gene expression in Arabidopsis thaliana. (wikipedia.org)
Synthesis1
- Abrin, like the similar plant toxin ricin, causes toxicity by inhibiting the formation (synthesis) of proteins in the cells of the exposed individual. (cdc.gov)
Amino acids1
- BLM encodes 1417 amino acids that code for a protein in the nuclear matrix of growing cells, which is a member of the RecQ family of helicases. (medscape.com)
Transcription1
- Instead, TWHF partially inhibited DNA binding capacity of cytokine-stimulated activating protein-1 (AP-1) and nuclear factor-κB (NF-κB) transcription factors. (aspetjournals.org)
Chromosomal1
- Nuclear architecture and the induction of chromosomal aberrations,' Mutat. (nanomedicine.com)
Ankyrin1
- Other DD-containing proteins, such as ankyrin, MyD88 and pelle, are probably not directly involved in cell death signalling. (embl-heidelberg.de)
Mediators1
- 3409. V.C. Cordes, H.R. Rackwitz, S. Reidenbach, 'Mediators of nuclear protein import target karyophilic proteins to pore complexes of cytoplasmic annulate lamellae,' Exp. (nanomedicine.com)
Cysteine1
- This mutation, known as Ser85Cys (or S85C), replaces the amino acid serine with the amino acid cysteine at position 85 of the protein. (medlineplus.gov)
Apoptotic1
- Alpha-helical domain present in a variety of proteins with apoptotic functions. (embl-heidelberg.de)
Hepatocellular carcinoma1
- Sp2 promotes invasion and metastasis of hepatocellular carcinoma by targeting TRIB3 protein. (nih.gov)
19951
- dration of globular proteins (Baker, 1995). (lu.se)
Recombinant1
- Recombinant protein encompassing a sequence within the center region of human NDP52. (genetex.com)
Highly conserved1
- The lamin family of proteins make up the matrix and are highly conserved in evolution. (nih.gov)
Inflammation2
- The major pathologic manifestations of rheumatoid arthritis (RA) and osteoarthritis (OA) are joint inflammation and articular cartilage resorption by proinflammatory cytokine-stimulated matrix metalloproteinases (MMPs) and aggrecanases. (aspetjournals.org)
- Underlying pathogenic mechanisms in chronic kidney disease (CKD) include chronic inflammation, oxidant stress, and matrix remodeling associated with dysregulated nuclear factor- κ B, nuclear factor- κ B, and SMAD signaling pathways, respectively. (aspetjournals.org)
Regulation1
- KIN17, which is known as a DNA and RNA binding protein, is highly expressed in numerous types of human cancers and was discovered to participate in several vital cell behaviors, including DNA replication, damage repair, regulation of cell cycle and RNA processing. (spandidos-publications.com)
Magnetic1
- Here we report the nuclear magnetic resonance (NMR) structure of the 145 residue long p75ICD. (embl-heidelberg.de)
Serum1
- Source of all serum proteins is from USDA inspected abattoirs located in the United States. (bdbiosciences.com)
Nucleotide1
- Moreover, speci®c hy- found in narrow minor groove regions in a variety dration patterns seem to play a role in nucleotide sequence recognition by proteins (Otwinowski of oligonucleotide duplexes (Prive et al. (lu.se)
Endoplasmic reticulum1
- Previous higher plant studies have associated them with functions at the nuclear envelope and the endoplasmic reticulum (ER). (brookes.ac.uk)
Cell9
- Lamin B2 contributes to the proliferation of bladder cancer cells via activating the expression of cell division cycle‑associated protein 3. (nih.gov)
- Other studies suggest that the matrin 3 protein may be involved in cell survival. (medlineplus.gov)
- 3418. P. Loidl, A. Eberharter, 'Nuclear matrix and the cell cycle,' Int. Rev. Cytol. (nanomedicine.com)
- 3419. M.A. Mancini, D. He, I.I. Ouspenski, B.R. Brinkley, 'Dynamic continuity of nuclear and mitotic matrix proteins in the cell cycle,' J. Cell Biochem. (nanomedicine.com)
- This includes finding out what other proteins the SUNs bind to and what functions they have during cell division. (brookes.ac.uk)
- Nanotopographical modulation of cell function through nuclear deformation. (cdc.gov)
- We, herein, engineered nanotopographies of various shapes (gratings and pillars) and dimensions (feature size, spacing and height), and thoroughly investigated cell spreading, focal adhesion organization and nuclear deformation of human primary fibroblasts as the model cell grown on the nanotopographies. (cdc.gov)
- These approaches promise to enable researchers to assess, on a large scale, both expression level and functional state of the proteins that carry out most functions in a cell. (lu.se)
- The success of proteomics experiments, such as studies of protein function and cell signaling pathways, ultimately de- pends on how well the protein content in samples is identified and annotated. (lu.se)
Regions1
- 3408. N. Pante, U. Aebi, 'Sequential binding of import ligands to distinct nucleopore regions during their nuclear import,' Science 273(20 September 1996):1729-1732. (nanomedicine.com)