A family of structurally-related angiogenic proteins of approximately 70 kDa in size. They have high specificity for members of the TIE RECEPTOR FAMILY.
An angiopoietin that is closely related to ANGIOPOIETIN-1. It binds to the TIE-2 RECEPTOR without receptor stimulation and antagonizes the effect of ANGIOPOIETIN-1. However its antagonistic effect may be limited to cell receptors that occur within the vasculature. Angiopoietin-2 may therefore play a role in down-regulation of BLOOD VESSEL branching and sprouting.
The first to be discovered member of the angiopoietin family. It may play a role in increasing the sprouting and branching of BLOOD VESSELS. Angiopoietin-1 specifically binds to and stimulates the TIE-2 RECEPTOR. Several isoforms of angiopoietin-1 occur due to ALTERNATIVE SPLICING of its mRNA.
A TIE receptor tyrosine kinase that is found almost exclusively on ENDOTHELIAL CELLS. It is required for both normal embryonic vascular development (NEOVASCULARIZATION, PHYSIOLOGIC) and tumor angiogenesis (NEOVASCULARIZATION, PATHOLOGIC).
A TIE receptor found predominantly on ENDOTHELIAL CELLS. It is considered essential for vascular development and can form a heterodimer with the TIE-2 RECEPTOR. The TIE-1 receptor may play a role in regulating BLOOD VESSEL stability and maturation.
A family of structurally-related tyrosine kinase receptors that are expressed predominantly in ENDOTHELIAL CELLS and are essential for development of BLOOD VESSELS (NEOVASCULARIZATION, PHYSIOLOGIC). The name derives from the fact that they are tyrosine kinases that contain Ig and EGF domains.
The original member of the family of endothelial cell growth factors referred to as VASCULAR ENDOTHELIAL GROWTH FACTORS. Vascular endothelial growth factor-A was originally isolated from tumor cells and referred to as "tumor angiogenesis factor" and "vascular permeability factor". Although expressed at high levels in certain tumor-derived cells it is produced by a wide variety of cell types. In addition to stimulating vascular growth and vascular permeability it may play a role in stimulating VASODILATION via NITRIC OXIDE-dependent pathways. Alternative splicing of the mRNA for vascular endothelial growth factor A results in several isoforms of the protein being produced.
The development of new BLOOD VESSELS during the restoration of BLOOD CIRCULATION during the healing process.
Agents that induce or stimulate PHYSIOLOGIC ANGIOGENESIS or PATHOLOGIC ANGIOGENESIS.
A family of angiogenic proteins that are closely-related to VASCULAR ENDOTHELIAL GROWTH FACTOR A. They play an important role in the growth and differentiation of vascular as well as lymphatic endothelial cells.
A pathologic process consisting of the proliferation of blood vessels in abnormal tissues or in abnormal positions.
These growth factors are soluble mitogens secreted by a variety of organs. The factors are a mixture of two single chain polypeptides which have affinity to heparin. Their molecular weight are organ and species dependent. They have mitogenic and chemotactic effects and can stimulate endothelial cells to grow and synthesize DNA. The factors are related to both the basic and acidic FIBROBLAST GROWTH FACTORS but have different amino acid sequences.
A class of cellular receptors that have an intrinsic PROTEIN-TYROSINE KINASE activity.
Soluble protein factors generated by activated lymphocytes that affect other cells, primarily those involved in cellular immunity.
Glycoproteins found on the membrane or surface of cells.
Regulatory proteins and peptides that are signaling molecules involved in the process of PARACRINE COMMUNICATION. They are generally considered factors that are expressed by one cell and are responded to by receptors on another nearby cell. They are distinguished from HORMONES in that their actions are local rather than distal.
Any of the tubular vessels conveying the blood (arteries, arterioles, capillaries, venules, and veins).
Highly specialized EPITHELIAL CELLS that line the HEART; BLOOD VESSELS; and lymph vessels, forming the ENDOTHELIUM. They are polygonal in shape and joined together by TIGHT JUNCTIONS. The tight junctions allow for variable permeability to specific macromolecules that are transported across the endothelial layer.
Single pavement layer of cells which line the luminal surface of the entire vascular system and regulate the transport of macromolecules and blood components.
Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.
A 180-kDa VEGF receptor found primarily in endothelial cells that is essential for vasculogenesis and vascular maintenance. It is also known as Flt-1 (fms-like tyrosine kinase receptor-1). A soluble, alternatively spliced isoform of the receptor may serve as a binding protein that regulates the availability of various ligands for VEGF receptor binding and signal transduction.
RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.
A variation of the PCR technique in which cDNA is made from RNA via reverse transcription. The resultant cDNA is then amplified using standard PCR protocols.
Histochemical localization of immunoreactive substances using labeled antibodies as reagents.
The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.
Products of proto-oncogenes. Normally they do not have oncogenic or transforming properties, but are involved in the regulation or differentiation of cell growth. They often have protein kinase activity.
Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.
Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.
A heterogeneous group of sporadic or hereditary carcinoma derived from cells of the KIDNEYS. There are several subtypes including the clear cells, the papillary, the chromophobe, the collecting duct, the spindle cells (sarcomatoid), or mixed cell-type carcinoma.
Tumors or cancers of the KIDNEY.
An adenocarcinoma characterized by the presence of varying combinations of clear and hobnail-shaped tumor cells. There are three predominant patterns described as tubulocystic, solid, and papillary. These tumors, usually located in the female reproductive organs, have been seen more frequently in young women since 1970 as a result of the association with intrauterine exposure to diethylstilbestrol. (From Holland et al., Cancer Medicine, 3d ed)

Molecular cloning and characterization of a novel angiopoietin family protein, angiopoietin-3. (1/298)

Using homology-based PCR, we have isolated cDNA encoding a novel member (491 amino acids) of the angiopoietin (Ang) family from human adult heart cDNA and have designated it angiopoietin-3 (Ang3). The NH2-terminal and COOH-terminal portions of Ang-3 contain the characteristic coiled-coil domain and fibrinogen-like domain that are conserved in other known Angs. Ang3 has a highly hydrophobic region at the N-terminus (approximately 21 amino acids) that is typical of a signal sequence for protein secretion. Ang3 mRNA is most abundant in adrenal gland, placenta, thyroid gland, heart and small intestine in human adult tissues. Additionally, Ang3 is a secretory protein, but is not a mitogen in endothelial cells.  (+info)

Angiopoietins 3 and 4: diverging gene counterparts in mice and humans. (2/298)

The angiopoietins have recently joined the members of the vascular endothelial growth factor family as the only known growth factors largely specific for vascular endothelium. The angiopoietins include a naturally occurring agonist, angiopoietin-1, as well as a naturally occurring antagonist, angiopoietin-2, both of which act by means of the Tie2 receptor. We now report our attempts to use homology-based cloning approaches to identify new members of the angiopoietin family. These efforts have led to the identification of two new angiopoietins, angiopoietin-3 in mouse and angiopoietin-4 in human; we have also identified several more distantly related sequences that do not seem to be true angiopoietins, in that they do not bind to the Tie receptors. Although angiopoietin-3 and angiopoietin-4 are strikingly more structurally diverged from each other than are the mouse and human versions of angiopoietin-1 and angiopoietin-2, they appear to represent the mouse and human counterparts of the same gene locus, as revealed in our chromosomal localization studies of all of the angiopoietins in mouse and human. The structural divergence of angiopoietin-3 and angiopoietin-4 appears to underlie diverging functions of these counterparts. Angiopoietin-3 and angiopoietin-4 have very different distributions in their respective species, and angiopoietin-3 appears to act as an antagonist, whereas angiopoietin-4 appears to function as an agonist.  (+info)

Angiopoietin-3, a novel member of the angiopoietin family. (3/298)

A cDNA clone encoding angiopoietin-3 protein (Ang3), a novel member of the angiopoietin family, was identified. Ang3 cDNA was cloned from a human aorta cDNA library. Ang3 is a 503 amino acid protein having 45.1% and 44.7% identity with human angiopoietin-1 and human angiopoietin-2, respectively. Ang3 mRNA is expressed in lung and cultured human umbilical vein endothelial cells (HUVECs). Ang3 mRNA expression in HUVECs was slightly decreased by vascular endothelial cell growth factor treatment, suggesting that the regulation of Ang3 mRNA expression is different from that of Ang2.  (+info)

Molecular cloning, expression, and characterization of angiopoietin-related protein. angiopoietin-related protein induces endothelial cell sprouting. (4/298)

Using degenerate polymerase chain reaction, we isolated a cDNA encoding a novel 493-amino acid protein from human and mouse adult heart cDNAs and have designated it angiopoietin-related protein-2 (ARP2). The NH(2)-terminal and COOH-terminal portions of ARP2 contain the characteristic coiled-coil domain and fibrinogen-like domain that are conserved in angiopoietins. ARP2 has two consensus glycosylation sites and a highly hydrophobic region at the NH(2) terminus that is typical of a secretory signal sequence. Recombinant ARP2 expressed in COS cells is secreted and glycosylated. In human adult tissues, ARP2 mRNA is most abundant in heart, small intestine, spleen, and stomach. In rat embryos, ARP2 mRNA is most abundant in the blood vessels and skeletal muscles. Endothelial and vascular smooth muscle cells also contain ARP2 mRNA. Recombinant ARP2 protein induces sprouting in vascular endothelial cells but does not bind to the Tie1 or Tie2 receptor. These results suggest that ARP2 may exert a function on endothelial cells through autocrine or paracrine action.  (+info)

Hepatic expression, synthesis and secretion of a novel fibrinogen/angiopoietin-related protein that prevents endothelial-cell apoptosis. (5/298)

Using degenerate PCR we isolated a cDNA encoding a novel 406- and 410-amino acid protein from human and mouse embryonic cDNAs and have designated it 'hepatic fibrinogen/angiopoietin-related protein' (HFARP). The N-terminal and C-terminal portions of HFARP contain the characteristic coiled-coil domains and fibrinogen-like domains that are conserved in angiopoietins. In human and mouse tissues, HFARP mRNA is specifically expressed in the liver. HFARP mRNA and protein are mainly present in the hepatocytes. HFARP has a highly hydrophobic region at the N-terminus that is typical of a secretory signal sequence and one consensus glycosylation site. Recombinant HFARP expressed in COS-7 cells is secreted and glycosylated. HFARP protein is present not only in the hepatocytes, but also in the circulating blood. Recombinant HFARP acts as an apoptosis survival factor for vascular endothelial cells, but does not bind to Tie1 or Tie2 (endothelial-cell tyrosine kinase receptors). These results suggest that HFARP may exert a protective function on endothelial cells through an endocrine action.  (+info)

Expression of Tie1, Tie2, and angiopoietins 1, 2, and 4 in Kaposi's sarcoma and cutaneous angiosarcoma. (6/298)

The angiopoietins are recently described growth factors for vascular endothelium. The Tie1 and Tie2 receptors are expressed by endothelium. Acquired immune deficiency syndrome (AIDS)-associated Kaposi's sarcoma (KS) and cutaneous angiosarcoma are malignancies of endothelial origin. KS involves primarily the skin and mucosal surfaces and is common in AIDS patients. In an effort to determine whether the angiopoietins and Tie receptors play a role in the pathobiology of angiosarcoma and KS, we studied the expression of angiopoietin-1, angiopoietin-2, angiopoietin-4, Tie1, and Tie2 mRNAs in biopsies of KS from 12 AIDS patients, in biopsies of cutaneous angiosarcoma from two patients, and in control biopsies of normal skin from three volunteers by in situ hybridization. Strong expression of angiopoietin-2, Tie1, and Tie2 mRNAs was detected in the tumor cells of KS and cutaneous angiosarcomas, in contrast to the focal low-level expression in normal skin biopsies. Focal low-level expression of angiopoietin-1 was seen in KS, cutaneous angiosarcomas, and in normal skin. Focal low-level expression of angiopoietin-4 was identified in a minority of KS lesions. These findings suggest that the angiopoietins and Tie receptors may play an important role in the pathobiology of KS and cutaneous angiosarcoma and identify additional potential targets for therapeutic intervention in these vascular malignancies.  (+info)

Characterization of the fasting-induced adipose factor FIAF, a novel peroxisome proliferator-activated receptor target gene. (7/298)

Fasting is associated with significant changes in nutrient metabolism, many of which are governed by transcription factors that regulate the expression of rate-limiting enzymes. One factor that plays an important role in the metabolic response to fasting is the peroxisome proliferator-activated receptor alpha (PPARalpha). To gain more insight into the role of PPARalpha during fasting, and into the regulation of metabolism during fasting in general, a search for unknown PPARalpha target genes was performed. Using subtractive hybridization (SABRE) comparing liver mRNA from wild-type and PPARalpha null mice, we isolated a novel PPARalpha target gene, encoding the secreted protein FIAF (for fasting induced adipose factor), that belongs to the family of fibrinogen/angiopoietin-like proteins. FIAF is predominantly expressed in adipose tissue and is strongly up-regulated by fasting in white adipose tissue and liver. Moreover, FIAF mRNA is decreased in white adipose tissue of PPARgamma +/- mice. FIAF protein can be detected in various tissues and in blood plasma, suggesting that FIAF has an endocrine function. Its plasma abundance is increased by fasting and decreased by chronic high fat feeding. The data suggest that FIAF represents a novel endocrine signal involved in the regulation of metabolism, especially under fasting conditions.  (+info)

Peroxisome proliferator-activated receptor gamma target gene encoding a novel angiopoietin-related protein associated with adipose differentiation. (8/298)

The nuclear receptor peroxisome proliferator-activated receptor gamma regulates adipose differentiation and systemic insulin signaling via ligand-dependent transcriptional activation of target genes. However, the identities of the biologically relevant target genes are largely unknown. Here we describe the isolation and characterization of a novel target gene induced by PPARgamma ligands, termed PGAR (for PPARgamma angiopoietin related), which encodes a novel member of the angiopoietin family of secreted proteins. The transcriptional induction of PGAR follows a rapid time course typical of immediate-early genes and occurs in the absence of protein synthesis. The expression of PGAR is predominantly localized to adipose tissues and placenta and is consistently elevated in genetic models of obesity. Hormone-dependent adipocyte differentiation coincides with a dramatic early induction of the PGAR transcript. Alterations in nutrition and leptin administration are found to modulate the PGAR expression in vivo. Taken together, these data suggest a possible role for PGAR in the regulation of systemic lipid metabolism or glucose homeostasis.  (+info)

Angiopoietins are a family of growth factors that play crucial roles in the development and maintenance of blood vessels. They bind to the Tie2 receptor tyrosine kinase, which is primarily expressed on vascular endothelial cells. The interaction between angiopoietins and Tie2 regulates various aspects of vascular biology, including vasculogenesis, angiogenesis, and vascular stability.

There are four main members in the angiopoietin family: Ang1, Ang2, Ang3 (also known as Ang4 in humans), and Ang4 (also known as Ang5 in mice). Among these, Ang1 and Ang2 have been studied most extensively.

Ang1 is produced by perivascular cells, such as smooth muscle cells and pericytes, and it acts as a stabilizing factor for blood vessels. It promotes vascular maturation and quiescence by enhancing endothelial cell survival, reducing vascular permeability, and increasing the association between endothelial cells and mural cells (pericytes or smooth muscle cells).

Ang2, on the other hand, is produced mainly by endothelial cells and has context-dependent functions. During embryonic development, Ang2 acts as a pro-angiogenic factor in conjunction with vascular endothelial growth factor (VEGF) to promote the formation of new blood vessels. However, in adult tissues, Ang2 is upregulated during pathological conditions like inflammation and tumor growth, where it destabilizes existing vasculature by antagonizing Ang1's effects on Tie2 signaling. This leads to increased vascular permeability, inflammation, and the initiation of angiogenesis.

In summary, angiopoietins are essential regulators of blood vessel development and homeostasis, with distinct functions for different family members in promoting or inhibiting various aspects of vascular biology.

Angiopoietin-2 (Ang-2) is a protein that is involved in the regulation of blood vessel formation and maintenance. It is a member of the angiopoietin family, which includes Ang-1, Ang-2, Ang-3, and Ang-4. These proteins bind to the Tie receptor tyrosine kinases (Tie1 and Tie2) on the surface of endothelial cells, which line the interior of blood vessels.

Ang-2 is primarily produced by endothelial cells and has context-dependent roles in angiogenesis, which is the growth of new blood vessels from pre-existing ones. In general, Ang-2 is thought to act as an antagonist of Ang-1, which promotes vessel stability and maturation.

Ang-2 can destabilize existing blood vessels by binding to Tie2 receptors and blocking the stabilizing effects of Ang-1. This can lead to increased vascular permeability and inflammation. However, in the presence of pro-angiogenic factors such as VEGF (vascular endothelial growth factor), Ang-2 can also promote the formation of new blood vessels by stimulating endothelial cell migration and proliferation.

Abnormal regulation of Ang-2 has been implicated in various diseases, including cancer, diabetic retinopathy, and age-related macular degeneration. In these conditions, increased levels of Ang-2 can contribute to the development of abnormal blood vessels, which can lead to tissue damage and loss of function.

Angiopoietin-1 (ANG-1) is a protein that plays a crucial role in the development and maintenance of blood vessels. It is a member of the angiopoietin family, which includes several growth factors involved in the regulation of angiogenesis, the formation of new blood vessels from pre-existing ones.

ANG-1 primarily binds to the Tie2 receptor, which is predominantly expressed on vascular endothelial cells. The ANG-1/Tie2 signaling pathway promotes vascular stability, integrity, and maturation by enhancing endothelial cell survival, migration, and adhesion. It also inhibits vascular leakage and inflammation, contributing to the overall homeostasis of the vasculature.

In addition to its role in physiological conditions, ANG-1 has been implicated in various pathological processes such as tumor angiogenesis, ischemia, and fibrosis. Modulation of the ANG-1/Tie2 signaling pathway has emerged as a potential therapeutic strategy for treating several diseases associated with abnormal vascular function.

TEC (Tyrosine kinase with Immunoglobulin-like and EGF homology domains-2) or TIE-2 is a type of receptor tyrosine kinase that plays a crucial role in the regulation of angiogenesis, lymphangiogenesis, and vascular maintenance. It is primarily expressed on the surface of endothelial cells, which line the interior surface of blood vessels.

The TIE-2 receptor binds to its ligand, angiopoietin-1 (Ang1), promoting vessel stability and quiescence by reducing endothelial cell permeability and enhancing their survival. Angiopoietin-2 (Ang2) can also bind to the TIE-2 receptor but with lower affinity than Ang1, acting as a context-dependent agonist or antagonist. In the presence of VEGF (Vascular Endothelial Growth Factor), Ang2 functions as an antagonist, inducing vascular instability and increasing endothelial cell permeability, which contributes to angiogenesis during development and in pathological conditions like tumor growth, inflammation, and ischemia.

Abnormal TIE-2 signaling has been implicated in several diseases, including cancer, atherosclerosis, and diabetic retinopathy. Targeting the TIE-2 signaling pathway presents an attractive therapeutic strategy for treating these conditions.

To my knowledge, there is no widely recognized medical definition for a "TIE-1 receptor" in the context of general medicine or clinical practice. The term "TIE-1" refers to a type of gene and its corresponding protein that are part of the angiopoietin/TIE signaling pathway, which plays crucial roles in blood vessel development and maintenance. However, this is more of a research concept and is not typically mentioned in medical textbooks or clinical practice guidelines.

Therefore, I would recommend consulting relevant scientific literature or consulting with a basic science or molecular biology expert for a more detailed and accurate definition of "TIE-1 receptor" and its functions.

Tie receptors (also known as Tyrosine Kinase with Immunoglobulin-like and EGF-like domains) are a family of transmembrane receptors that play crucial roles in regulating various cellular processes, including cell survival, proliferation, differentiation, and migration. They are composed of an extracellular domain containing immunoglobulin-like and EGF-like motifs, a single transmembrane region, and an intracellular tyrosine kinase domain. Upon ligand binding, Tie receptors undergo dimerization and autophosphorylation, leading to the activation of downstream signaling pathways that control vascular development, angiogenesis, and maintenance of vascular integrity. There are two main members of this family: Tie1 and Tie2 (also known as Tek). While Tie2 is widely expressed in endothelial cells and has well-established ligands (Angiopoietin-1 and -2), Tie1 is predominantly found in endothelial cells and its function and ligand remain less clear. Dysregulation of Tie receptors has been implicated in various vascular disorders, such as tumor angiogenesis and vascular leakage.

Vascular Endothelial Growth Factor A (VEGFA) is a specific isoform of the vascular endothelial growth factor (VEGF) family. It is a well-characterized signaling protein that plays a crucial role in angiogenesis, the process of new blood vessel formation from pre-existing vessels. VEGFA stimulates the proliferation and migration of endothelial cells, which line the interior surface of blood vessels, thereby contributing to the growth and development of new vasculature. This protein is essential for physiological processes such as embryonic development and wound healing, but it has also been implicated in various pathological conditions, including cancer, age-related macular degeneration, and diabetic retinopathy. The regulation of VEGFA expression and activity is critical to maintaining proper vascular function and homeostasis.

Physiologic neovascularization is the natural and controlled formation of new blood vessels in the body, which occurs as a part of normal growth and development, as well as in response to tissue repair and wound healing. This process involves the activation of endothelial cells, which line the interior surface of blood vessels, and their migration, proliferation, and tube formation to create new capillaries. Physiologic neovascularization is tightly regulated by a balance of pro-angiogenic and anti-angiogenic factors, ensuring that it occurs only when and where it is needed. It plays crucial roles in various physiological processes, such as embryonic development, tissue regeneration, and wound healing.

Angiogenesis inducing agents are substances or drugs that stimulate the growth of new blood vessels, a process known as angiogenesis. This process is essential for the growth and development of tissues and organs in the body, including wound healing and the formation of blood vessels in the placenta during pregnancy. However, abnormal angiogenesis can also contribute to various diseases, such as cancer, diabetic retinopathy, and age-related macular degeneration.

Angiogenesis inducing agents are being studied for their potential therapeutic benefits in a variety of medical conditions. For example, they may be used to promote wound healing or tissue repair after injury or surgery. In cancer treatment, angiogenesis inhibitors are often used to block the growth of new blood vessels and prevent tumors from growing and spreading. However, angiogenesis inducing agents can have the opposite effect and may potentially be used to enhance the delivery of drugs to tumors or improve the effectiveness of other cancer treatments.

Examples of angiogenesis inducing agents include certain growth factors, such as vascular endothelial growth factor (VEGF), fibroblast growth factor (FGF), and platelet-derived growth factor (PDGF). These substances can be administered as drugs to stimulate angiogenesis in specific contexts. Other substances, such as hypoxia-inducible factors (HIFs) and prostaglandins, can also induce angiogenesis under certain conditions.

Vascular Endothelial Growth Factors (VEGFs) are a family of signaling proteins that stimulate the growth and development of new blood vessels, a process known as angiogenesis. They play crucial roles in both physiological and pathological conditions, such as embryonic development, wound healing, and tumor growth. Specifically, VEGFs bind to specific receptors on the surface of endothelial cells, which line the interior surface of blood vessels, triggering a cascade of intracellular signaling events that promote cell proliferation, migration, and survival. Dysregulation of VEGF signaling has been implicated in various diseases, including cancer, age-related macular degeneration, and diabetic retinopathy.

Pathologic neovascularization is the abnormal growth of new blood vessels in previously avascular tissue or excessive growth within existing vasculature, which occurs as a result of hypoxia, inflammation, or angiogenic stimuli. These newly formed vessels are often disorganized, fragile, and lack proper vessel hierarchy, leading to impaired blood flow and increased vascular permeability. Pathologic neovascularization can be observed in various diseases such as cancer, diabetic retinopathy, age-related macular degeneration, and chronic inflammation. This process contributes to disease progression by promoting tumor growth, metastasis, and edema formation, ultimately leading to tissue damage and organ dysfunction.

Endothelial growth factors (ECGFs or EGFs) are a group of signaling proteins that stimulate the growth, proliferation, and survival of endothelial cells, which line the interior surface of blood vessels. These growth factors play crucial roles in various physiological processes, including angiogenesis (the formation of new blood vessels), wound healing, and vascular development during embryogenesis.

One of the most well-studied EGFs is the vascular endothelial growth factor (VEGF) family, which consists of several members like VEGFA, VEGFB, VEGFC, VEGFD, and placental growth factor (PlGF). These factors bind to specific receptors on the surface of endothelial cells, leading to a cascade of intracellular signaling events that ultimately result in cell proliferation, migration, and survival.

Other EGFs include fibroblast growth factors (FGFs), hepatocyte growth factor (HGF), platelet-derived growth factor (PDGF), and transforming growth factor-beta (TGF-β). Dysregulation of endothelial growth factors has been implicated in various pathological conditions, such as cancer, diabetic retinopathy, age-related macular degeneration, and cardiovascular diseases. Therefore, understanding the functions and regulation of EGFs is essential for developing novel therapeutic strategies to treat these disorders.

Receptor Protein-Tyrosine Kinases (RTKs) are a type of transmembrane receptors found on the cell surface that play a crucial role in signal transduction and regulation of various cellular processes, including cell growth, differentiation, metabolism, and survival. They are called "tyrosine kinases" because they possess an intrinsic enzymatic activity that catalyzes the transfer of a phosphate group from ATP to tyrosine residues on target proteins, thereby modulating their function.

RTKs are composed of three main domains: an extracellular domain that binds to specific ligands (growth factors, hormones, or cytokines), a transmembrane domain that spans the cell membrane, and an intracellular domain with tyrosine kinase activity. Upon ligand binding, RTKs undergo conformational changes that lead to their dimerization or oligomerization, which in turn activates their tyrosine kinase activity. Activated RTKs then phosphorylate specific tyrosine residues on downstream signaling proteins, initiating a cascade of intracellular signaling events that ultimately result in the appropriate cellular response.

Dysregulation of RTK signaling has been implicated in various human diseases, including cancer, diabetes, and developmental disorders. As such, RTKs are important targets for therapeutic intervention in these conditions.

Lymphokines are a type of cytokines that are produced and released by activated lymphocytes, a type of white blood cell, in response to an antigenic stimulation. They play a crucial role in the regulation of immune responses and inflammation. Lymphokines can mediate various biological activities such as chemotaxis, activation, proliferation, and differentiation of different immune cells including lymphocytes, monocytes, macrophages, and eosinophils. Examples of lymphokines include interleukins (ILs), interferons (IFNs), tumor necrosis factor (TNF), and colony-stimulating factors (CSFs).

Membrane glycoproteins are proteins that contain oligosaccharide chains (glycans) covalently attached to their polypeptide backbone. They are integral components of biological membranes, spanning the lipid bilayer and playing crucial roles in various cellular processes.

The glycosylation of these proteins occurs in the endoplasmic reticulum (ER) and Golgi apparatus during protein folding and trafficking. The attached glycans can vary in structure, length, and composition, which contributes to the diversity of membrane glycoproteins.

Membrane glycoproteins can be classified into two main types based on their orientation within the lipid bilayer:

1. Type I (N-linked): These glycoproteins have a single transmembrane domain and an extracellular N-terminus, where the oligosaccharides are predominantly attached via asparagine residues (Asn-X-Ser/Thr sequon).
2. Type II (C-linked): These glycoproteins possess two transmembrane domains and an intracellular C-terminus, with the oligosaccharides linked to tryptophan residues via a mannose moiety.

Membrane glycoproteins are involved in various cellular functions, such as:

* Cell adhesion and recognition
* Receptor-mediated signal transduction
* Enzymatic catalysis
* Transport of molecules across membranes
* Cell-cell communication
* Immunological responses

Some examples of membrane glycoproteins include cell surface receptors (e.g., growth factor receptors, cytokine receptors), adhesion molecules (e.g., integrins, cadherins), and transporters (e.g., ion channels, ABC transporters).

Intercellular signaling peptides and proteins are molecules that mediate communication and interaction between different cells in living organisms. They play crucial roles in various biological processes, including cell growth, differentiation, migration, and apoptosis (programmed cell death). These signals can be released into the extracellular space, where they bind to specific receptors on the target cell's surface, triggering intracellular signaling cascades that ultimately lead to a response.

Peptides are short chains of amino acids, while proteins are larger molecules made up of one or more polypeptide chains. Both can function as intercellular signaling molecules by acting as ligands for cell surface receptors or by being cleaved from larger precursor proteins and released into the extracellular space. Examples of intercellular signaling peptides and proteins include growth factors, cytokines, chemokines, hormones, neurotransmitters, and their respective receptors.

These molecules contribute to maintaining homeostasis within an organism by coordinating cellular activities across tissues and organs. Dysregulation of intercellular signaling pathways has been implicated in various diseases, such as cancer, autoimmune disorders, and neurodegenerative conditions. Therefore, understanding the mechanisms underlying intercellular signaling is essential for developing targeted therapies to treat these disorders.

Blood vessels are the part of the circulatory system that transport blood throughout the body. They form a network of tubes that carry blood to and from the heart, lungs, and other organs. The main types of blood vessels are arteries, veins, and capillaries. Arteries carry oxygenated blood away from the heart to the rest of the body, while veins return deoxygenated blood back to the heart. Capillaries connect arteries and veins and facilitate the exchange of oxygen, nutrients, and waste materials between the blood and the body's tissues.

Endothelial cells are the type of cells that line the inner surface of blood vessels, lymphatic vessels, and heart chambers. They play a crucial role in maintaining vascular homeostasis by controlling vasomotor tone, coagulation, platelet activation, and inflammation. Endothelial cells also regulate the transport of molecules between the blood and surrounding tissues, and contribute to the maintenance of the structural integrity of the vasculature. They are flat, elongated cells with a unique morphology that allows them to form a continuous, nonthrombogenic lining inside the vessels. Endothelial cells can be isolated from various tissues and cultured in vitro for research purposes.

The endothelium is a thin layer of simple squamous epithelial cells that lines the interior surface of blood vessels, lymphatic vessels, and heart chambers. The vascular endothelium, specifically, refers to the endothelial cells that line the blood vessels. These cells play a crucial role in maintaining vascular homeostasis by regulating vasomotor tone, coagulation, platelet activation, inflammation, and permeability of the vessel wall. They also contribute to the growth and repair of the vascular system and are involved in various pathological processes such as atherosclerosis, hypertension, and diabetes.

Proteins are complex, large molecules that play critical roles in the body's functions. They are made up of amino acids, which are organic compounds that are the building blocks of proteins. Proteins are required for the structure, function, and regulation of the body's tissues and organs. They are essential for the growth, repair, and maintenance of body tissues, and they play a crucial role in many biological processes, including metabolism, immune response, and cellular signaling. Proteins can be classified into different types based on their structure and function, such as enzymes, hormones, antibodies, and structural proteins. They are found in various foods, especially animal-derived products like meat, dairy, and eggs, as well as plant-based sources like beans, nuts, and grains.

Vascular Endothelial Growth Factor Receptor-1 (VEGFR-1), also known as Flt-1 (Fms-like tyrosine kinase-1), is a receptor tyrosine kinase that plays a crucial role in the regulation of angiogenesis, vasculogenesis, and lymphangiogenesis. It is primarily expressed on vascular endothelial cells, hematopoietic stem cells, and monocytes/macrophages. VEGFR-1 binds to several ligands, including Vascular Endothelial Growth Factor-A (VEGF-A), VEGF-B, and Placental Growth Factor (PlGF). The binding of these ligands to VEGFR-1 triggers intracellular signaling cascades that modulate various cellular responses, such as proliferation, migration, survival, and vascular permeability. While VEGFR-1 is known to have a role in promoting angiogenesis under certain conditions, it primarily acts as a negative regulator of angiogenesis by sequestering VEGF-A, preventing its binding to the more proangiogenic VEGFR-2 receptor. Dysregulation of VEGFR-1 signaling has been implicated in various pathological conditions, including cancer, inflammation, and vascular diseases.

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

Reverse Transcriptase Polymerase Chain Reaction (RT-PCR) is a laboratory technique used in molecular biology to amplify and detect specific DNA sequences. This technique is particularly useful for the detection and quantification of RNA viruses, as well as for the analysis of gene expression.

The process involves two main steps: reverse transcription and polymerase chain reaction (PCR). In the first step, reverse transcriptase enzyme is used to convert RNA into complementary DNA (cDNA) by reading the template provided by the RNA molecule. This cDNA then serves as a template for the PCR amplification step.

In the second step, the PCR reaction uses two primers that flank the target DNA sequence and a thermostable polymerase enzyme to repeatedly copy the targeted cDNA sequence. The reaction mixture is heated and cooled in cycles, allowing the primers to anneal to the template, and the polymerase to extend the new strand. This results in exponential amplification of the target DNA sequence, making it possible to detect even small amounts of RNA or cDNA.

RT-PCR is a sensitive and specific technique that has many applications in medical research and diagnostics, including the detection of viruses such as HIV, hepatitis C virus, and SARS-CoV-2 (the virus that causes COVID-19). It can also be used to study gene expression, identify genetic mutations, and diagnose genetic disorders.

Immunohistochemistry (IHC) is a technique used in pathology and laboratory medicine to identify specific proteins or antigens in tissue sections. It combines the principles of immunology and histology to detect the presence and location of these target molecules within cells and tissues. This technique utilizes antibodies that are specific to the protein or antigen of interest, which are then tagged with a detection system such as a chromogen or fluorophore. The stained tissue sections can be examined under a microscope, allowing for the visualization and analysis of the distribution and expression patterns of the target molecule in the context of the tissue architecture. Immunohistochemistry is widely used in diagnostic pathology to help identify various diseases, including cancer, infectious diseases, and immune-mediated disorders.

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

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

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

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

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

Examples of proto-oncogene proteins include:

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

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

"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.

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.

Carcinoma, renal cell (also known as renal cell carcinoma or RCC) is a type of cancer that originates in the lining of the tubules of the kidney. These tubules are small structures within the kidney that help filter waste and fluids from the blood to form urine.

Renal cell carcinoma is the most common type of kidney cancer in adults, accounting for about 80-85% of all cases. It can affect people of any age, but it is more commonly diagnosed in those over the age of 50.

There are several subtypes of renal cell carcinoma, including clear cell, papillary, chromophobe, and collecting duct carcinomas, among others. Each subtype has a different appearance under the microscope and may have a different prognosis and response to treatment.

Symptoms of renal cell carcinoma can vary but may include blood in the urine, flank pain, a lump or mass in the abdomen, unexplained weight loss, fatigue, and fever. Treatment options for renal cell carcinoma depend on the stage and grade of the cancer, as well as the patient's overall health and preferences. Treatment may include surgery, radiation therapy, chemotherapy, immunotherapy, or targeted therapy.

Kidney neoplasms refer to abnormal growths or tumors in the kidney tissues that can be benign (non-cancerous) or malignant (cancerous). These growths can originate from various types of kidney cells, including the renal tubules, glomeruli, and the renal pelvis.

Malignant kidney neoplasms are also known as kidney cancers, with renal cell carcinoma being the most common type. Benign kidney neoplasms include renal adenomas, oncocytomas, and angiomyolipomas. While benign neoplasms are generally not life-threatening, they can still cause problems if they grow large enough to compromise kidney function or if they undergo malignant transformation.

Early detection and appropriate management of kidney neoplasms are crucial for improving patient outcomes and overall prognosis. Regular medical check-ups, imaging studies, and urinalysis can help in the early identification of these growths, allowing for timely intervention and treatment.

Adenocarcinoma, clear cell is a type of cancer that begins in the glandular cells lining various organs and appears "clear" under the microscope due to its characteristic appearance. These cells produce and release mucus or other fluids. This type of cancer can occur in several parts of the body including the lungs, breasts, ovaries, prostate, and kidneys. Clear cell adenocarcinoma is most commonly found in the ovary and accounts for around 5-10% of all ovarian cancers. It is also associated with endometriosis, a condition where tissue similar to the lining of the uterus grows outside the uterine cavity.

Clear cell adenocarcinoma has unique features that distinguish it from other types of cancer. The cells are often large and have distinct borders, giving them a "clear" appearance under the microscope due to their high lipid or glycogen content. This type of cancer tends to be more aggressive than some other forms of adenocarcinoma and may have a poorer prognosis, particularly if it has spread beyond its original site.

Treatment for clear cell adenocarcinoma typically involves surgery to remove the tumor, followed by chemotherapy or radiation therapy to kill any remaining cancer cells. The specific treatment plan will depend on several factors, including the location and stage of the cancer, as well as the patient's overall health and medical history.

... -1 and angiopoietin-2 can form dimers, trimers, and tetramers. Angiopoietin-1 has the ability to form higher order ... is demonstrated by an increased ratio of angiopoietin-2 and angiopoietin-1 in blood serum. To be specific, angiopoietin levels ... Angiopoietin-1 encodes a 498 amino acid polypeptide with a molecular weight of 57 kDa whereas angiopoietin-2 encodes a 496 ... Angiopoietin-2 has been proposed as a biomarker in different cancer types. Angiopoietin-2 expression levels are proportional to ...
The angiopoietin receptors are receptors that bind angiopoietin. TIE-1 and TIE-2 comprise the cell-surface receptors that bind ... The angiopoietins are protein growth factors required for the formation of blood vessels (angiogenesis). The angiopoietins are ... In humans, three angiopoietins have been identified: Ang1, Ang2, and Ang4 (Ang 3 is the mouse ortholog of human Ang4). Ang1 and ... But it is clear that at least Tie-2 is capable of physiologic activation as a result of binding the angiopoietins.[citation ...
... is a type of angiopoietin and is encoded by the gene ANGPT1. Angiopoietins are proteins with important roles in ... increased angiopoietin-2, and an elevated ratio of angiopoietin-2/angiopoietin-1 in the placenta. This suggests that ... Dunk C, Shams M, Nijjar S (2000). "Angiopoietin-1 and angiopoietin-2 activate trophoblast Tie-2 to promote growth and migration ... Cheung AH, Stewart RJ, Marsden PA (1998). "Endothelial Tie2/Tek ligands angiopoietin-1 (ANGPT1) and angiopoietin-2 (ANGPT2): ...
The Angiopoietin-like proteins are proteins structurally like the angiopoietins but which do not bind to the angiopoietin ... Angiopoietin-related protein 1, gene ANGPTL1 Angiopoietin-related protein 2, gene ANGPTL2 Angiopoietin-related protein 3, gene ... Angiopoietin-related protein 7, gene ANGPTL7 Angiopoietin-related protein 8, gene ANGPTL8, also known as lipasin because of its ... gene ANGPTL4 Angiopoietin-related protein 5, gene ANGPTL5, mainly expressed in adult human heart. Angiopoietin-related protein ...
Angiopoietin-1, angiopoietin-2, and angiopoietin-4 participate in the formation of blood vessels. The protein encoded by this ... Angiopoietin-related protein 1 also known as angiopoietin-3 (ANG-3) is a protein that in humans is encoded by the ANGPTL1 gene ... 2005). "Biological characterization of angiopoietin-3 and angiopoietin-4". FASEB J. 18 (11): 1200-8. doi:10.1096/fj.03-1466com ... 1999). "Molecular cloning, expression, and characterization of angiopoietin-related protein. angiopoietin-related protein ...
... is a protein that in humans is encoded by the ANGPTL7 gene. It is one of the 8 angiopoietin-like ... "Entrez Gene: ANGPTL7 angiopoietin-like 7". Angiopoietin-like proteins: a comprehensive look Tanigawa, Yosuke; Wainberg, Michael ... Peek R, Kammerer RA, Frank S, Otte-Holler I, Westphal JR (Jan 2002). "The angiopoietin-like factor cornea-derived transcript 6 ...
Angiopoietin-1, angiopoietin-2, and angiopoietin-4 participate in the formation of blood vessels. ANGPTL2 protein is a secreted ... Angiopoietin-related protein 2 also known as angiopoietin-like protein 2 is a protein that in humans is encoded by the ANGPTL2 ... and characterization of angiopoietin-related protein. angiopoietin-related protein induces endothelial cell sprouting". J Biol ... Angiopoietins are members of the vascular endothelial growth factor family and the only known growth factors largely specific ...
Activation of the Tie2 receptor by the ligand Angiopoietin 2. This has been shown in vitro and in vivo. Activation of the ... Activation of the signaling pathway by Delta4, Angiopoietin 2, insulin, or a combination of the three and a JAK inhibitor ... Angiopoietin 2). Hes3, in turn, by regulating the expression of Shh and potentially other factors, can also exert an effect on ... Angiopoietin 2, insulin, or a combined treatment consisting of all three factors and an inhibitor of JAK) induce the increase ...
Angiopoietin-4 is a protein that in humans is encoded by the ANGPT4 gene. Angiopoietins are proteins with important roles in ... 2005). "Biological characterization of angiopoietin-3 and angiopoietin-4". FASEB J. 18 (11): 1200-8. doi:10.1096/fj.03-1466com ... "Genomic structures of the human angiopoietins show polymorphism in angiopoietin-2". Cytogenet. Cell Genet. 94 (3-4): 147-54. ... "Entrez Gene: ANGPT4 angiopoietin 4". Human ANGPT4 genome location and ANGPT4 gene details page in the UCSC Genome Browser. ...
Angiopoietin-like 3, also known as ANGPTL3, is a protein that in humans is encoded by the ANGPTL3 gene. The protein encoded by ... "Entrez Gene: ANGPTL3 angiopoietin-like 3". Conklin D, Gilbertson D, Taft DW, Maurer MF, Whitmore TE, Smith DL, et al. (December ... The FBN-like domain in angiopoietin-like 3 protein was shown to bind alpha-5/beta-3 integrins, and this binding induced ... Kaplan R, Zhang T, Hernandez M, Gan FX, Wright SD, Waters MG, Cai TQ (January 2003). "Regulation of the angiopoietin-like ...
It targets the protein angiopoietin 2. As of May 2017[update], it is in Phase II clinical trials for the treatment of diabetic ... Hussain RM, Neiweem AE, Kansara V, Harris A, Ciulla TA (October 2019). "Tie-2/Angiopoietin pathway modulation as a therapeutic ... "Anti-vasculaR Endothelial Growth Factor plUs Anti-angiopoietin 2 in Fixed comBination therapY: Evaluation for the Treatment of ...
Her doctoral research looked at the role of angiopoietins in astrocytoma angiogenesis. After earning her doctorate Zadeh moved ... Zadeh, Gelareh (2007). Role of angiopoietins and Tie2/TEK in astrocytoma angiogenesis (Thesis). OCLC 234132296. "Dr. Gelareh ...
Three dimensional structure of none of the members of Angiopoietin like proteins (ANGPTLs) is available up until now.[when?] ... "Atypical angiopoietin-like protein that regulates ANGPTL3". Proceedings of the National Academy of Sciences of the United ... is a novel but atypical member of the angiopoietin-like protein family". Biochemical and Biophysical Research Communications. ... "Visualizing the regulatory role of Angiopoietin-like protein 8 (ANGPTL8) in glucose and lipid metabolic pathways". Genomics. ...
January 2003). "Angiopoietin-1 and angiopoietin-2 share the same binding domains in the Tie-2 receptor involving the first Ig- ... angiopoietin-1 and angiopoietin-2, modulate VEGF-induced postnatal neovascularization". Circulation Research. 83 (3): 233-40. ... Angiopoietin-1 receptor also known as CD202B (cluster of differentiation 202B) is a protein that in humans is encoded by the ... Master Z, Jones N, Tran J, Jones J, Kerbel RS, Dumont DJ (November 2001). "Dok-R plays a pivotal role in angiopoietin-1- ...
Hata K, Udagawa J, Fujiwaki R, Nakayama K, Otani H, Miyazaki K (2002). "Expression of angiopoietin-1, angiopoietin-2, and Tie2 ... Xu Y, Yu Q (September 2001). "Angiopoietin-1, unlike angiopoietin-2, is incorporated into the extracellular matrix via its ... Cheung AH, Stewart RJ, Marsden PA (March 1998). "Endothelial Tie2/Tek ligands angiopoietin-1 (ANGPT1) and angiopoietin-2 ( ... "Angiopoietin-1 and angiopoietin-2 share the same binding domains in the Tie-2 receptor involving the first Ig-like loop and the ...
The angiopoietins, Ang1 and Ang2, are required for the formation of mature blood vessels, as demonstrated by mouse knock out ... Thurston G (October 2003). "Role of Angiopoietins and Tie receptor tyrosine kinases in angiogenesis and lymphangiogenesis". ...
... binds to the angiopoietin-like protein 3 (ANGPTL3). ANGPTL3 slows the function of certain enzymes that break down ...
Li JJ, Huang YQ, Basch R, Karpatkin S (February 2001). "Thrombin induces the release of angiopoietin-1 from platelets". ... Angiopoietin-1) and cytokines including the EMT inducer TGF-β. The release of TGF-β by platelets in blood vessels near primary ...
July 2007). "Lipid-lowering effects of anti-angiopoietin-like 4 antibody recapitulate the lipid phenotype found in angiopoietin ... Angiopoietin-like 4 is a protein that in humans is encoded by the ANGPTL4 gene. Alternatively spliced transcript variants ... July 2017). "Angiopoietin-like 4 induces a β-catenin-mediated upregulation of ID3 in fibroblasts to reduce scar collagen ... June 2015). "Angiopoietin-like 4 is a potent angiogenic factor and a novel therapeutic target for patients with proliferative ...
Angiopoietin 2 can act as an antagonist to Tie-2, destabilizing the endothelial cells, which results in less endothelial cell ... Angiopoietin 1 and Tie-2 signaling is essential for maturation and stabilization of endothelial cells. Platelet-derived growth ... Similar to the inhibition of the PDGF pathway, angiopoietin 2 reduces levels of pericytes, leading to diabetic retinopathy. ... "Angiopoietin-2, a natural antagonist for Tie2 that disrupts in vivo angiogenesis". Science. 277 (5322): 55-60. doi:10.1126/ ...
Chugh, S; Macé, C; Clement, L; Del Nogal, A; Marshall, C (2014). "Angiopoietin-like 4 based therapeutics for proteinuria and ...
"Attenuated angiopoietin-Tie2 signaling regresses Schlemm's canal integrity and induces glaucoma". Journal of Clinical ...
... and angiopoietins, that play the key roles in the blood vessel formation. National Science Contest for Elementary School ... "Requisite role of angiopoietin-1, a ligand for the TIE2 receptor, during embryonic angiogenesis". Cell. 87 (7): 1171-1180. doi: ... "Angiopoietin-2, a Natural Antagonist for Tie2 That Disrupts in vivo Angiogenesis". Science. 277 (5322): 55-60. doi:10.1126/ ...
Zeng L, Dai J, Ying K (2003). "Identification of a novel human angiopoietin-like gene expressed mainly in heart". J. Hum. Genet ...
Mammoto T, Parikh SM, Mammoto A, Gallagher D, Chan B, Mostoslavsky G, Ingber DE, Sukhatme VP (Aug 2007). "Angiopoietin-1 ...
He later showed that inhibition of the Tie2-ligand Angiopoietin 2 induces tumor regression and inhibits metastasis by ... He also identified expression of Angiopoietin 2 as an adaptive resistance mechanism upon anti-angiogenic treatment by VEGF ... "Role of Angiopoietin-2 in Adaptive Tumor Resistance to VEGF Signaling Blockade". Cell Reports. 8 (3): 696-706. doi:10.1016/j. ... "Dual angiopoietin-2 and VEGFA inhibition elicits antitumor immunity that is enhanced by PD-1 checkpoint blockade". Science ...
Regulation by Hypoxia and Angiopoietin-2". Cancer Research. 67 (18): 8429-8432. doi:10.1158/0008-5472.CAN-07-1684. ISSN 0008- ...
Mediators that promote angiogenesis are angiopoietin and vascular endothelial growth factor (VEGF). Prostaglandin E2 promotes ...
Makinde T, Murphy RF, Agrawal DK (2007). "Immunomodulatory role of vascular endothelial growth factor and angiopoietin-1 in ... The expression of angiopoietin-2 in the absence of VEGF leads to endothelial cell death and vascular regression. Conversely, a ...
2003). "Identification of a novel human angiopoietin-like gene expressed mainly in heart". J. Hum. Genet. 48 (3): 159-62. doi: ...
Angiopoietin-1 and angiopoietin-2 can form dimers, trimers, and tetramers. Angiopoietin-1 has the ability to form higher order ... is demonstrated by an increased ratio of angiopoietin-2 and angiopoietin-1 in blood serum. To be specific, angiopoietin levels ... Angiopoietin-1 encodes a 498 amino acid polypeptide with a molecular weight of 57 kDa whereas angiopoietin-2 encodes a 496 ... Angiopoietin-2 has been proposed as a biomarker in different cancer types. Angiopoietin-2 expression levels are proportional to ...
Angiopoietin-2 (Ang2), a ligand of the endothelial Tie2 tyrosine kinase, is involved in vascular inflammation and leakage in ... Angiopoietin-2 blockade ameliorates autoimmune neuroinflammation by inhibiting leukocyte recruitment into the CNS. ... Angiopoietin-2 blockade ameliorates autoimmune neuroinflammation by inhibiting leukocyte recruitment into the CNS. ...
... (ANG2) is a 56.9 kDa glycosylated growth factor that is specific for endothelial cells (ECs). ANG2 is expressed ... TIE2-Angiopoietin pathway has shown promising results in some pre-clinical and clinical trials, including studies on recurrent ... During angiogenesis, ANG2 exerts its effects via the angiopoietin-1/TIE2 receptor signaling system on endothelial cells. ...
AGPT2, ANG2, Angiopoietin-2. Background. Angiopoietin-2 (ANG 2, or ANGPT2), is a member of the ANG family, which plays an ... Recombinant Human Angiopoietin-2 / AGPT2 Protein (His Tag) Beta LifeScience SKU/CAT #: BLPSN-0198 ... Recombinant Human Angiopoietin-2 / AGPT2 Protein (His Tag) Beta LifeScience SKU/CAT #: BLPSN-0198 ... Inquire the Recombinant Human Angiopoietin-2 / AGPT2 Protein (His Tag) by filling out the form below. Well get back to you ...
Angiopoietin-like 8 (Angptl8) controls adipocyte lipolysis and phospholipid composition. Chemistry and Physics of Lipids 207 (B ... Abbreviation Angptl8, angiopoietin-like 8; FA, fatty acid; LD, lipid droplet; LPL, lipoprotein lipase; NEFA, non-esterified FA ... Angiopoietin-like 8 (Angptl8) inhibits lipolysis in the circulation together with Angplt3 and controls post-prandial fat ...
To determine the significance and regulation of the angiopoietin (Ang) pathway in highly vascular human renal cell carcinomas ( ... Adult, Aged, Aged, 80 and over, Angiogenesis Inducing Agents, Angiopoietin-1, Angiopoietin-2, Angiopoietins, Carcinoma, Renal ... Expression of the angiopoietins and their receptor Tie2 in human renal clear cell carcinomas; regulation by the von Hippel- ... Expression of the angiopoietins and their receptor Tie2 in human renal clear cell carcinomas; regulation by the von Hippel- ...
Home » Human ANGPTL2(Angiopoietin Like Protein 2) ELISA Kit,ELISA KIT, E-EL-H6034-96T, Human ... Product Tag - Human ANGPTL2(Angiopoietin Like Protein 2) ELISA Kit,ELISA KIT, E-EL-H6034-96T, Human. ...
Angiopoietin-1 (Ang-1) is a key regulator of angiogenesis and endothelial activation and has been studied as an objective ... Brief Report: Higher Levels of Angiopoietin-1 Are Associated With Early and Sustained Viral Suppression in Children Living With ...
Angiopoietin-2 as a marker of endothelial activation is a good predictor factor for intensive care unit admission of COVID-19 ... In those patients, soluble E-selectin and angiopoietin-2 were significantly increased (p value at 0.009 and 0.003, respectively ... ROC curve analysis identified an Angiopoietin-2 cut-off of 5000 pg/mL as the best predictor for ICU outcome (Se = 80.1%, Sp = ... CRP or D-dimers.Angiopoietin-2 is a relevant predictive factor for ICU direct admission in COVID-19 patients. This result ...
A clinicopathological correlation of the expression of the angiopoietin-Tie-2 receptor pathway in the brain of adults with ... A clinicopathological correlation of the expression of the angiopoietin-Tie-2 receptor pathway in the brain of adults with ...
上海金畔生物科技有限公司提供Cali-Bio CB500316.10ug Recombinant Human Angiopoietin-2,ANG 2重组人血管生成素-2 10ug,欢迎访问官网了解更多产品信息和订购 ... Cali-Bio CB500316.10ug Recombinant Human Angiopoietin-2,ANG 2重组人血管生成素-2 10ug. 发表于. 2024年3月29日. 由Amresco中国 ... Cali-Bio CB500316.10ug Recombinant Human Angiopoietin-2,ANG 2重组人血
The Angiopoietin-2/Angiopoietin-1 ratio increases early in burn patients and predicts mortality.. Heuberger, Dorothea; Wendel- ... Our aim was to analyze the Angiopoietin-2/Angiopoietin-1 ratio (Angpt-2/Angpt-1 ratio) over the first two days in critically ... Angiopoietin-2 (Angpt-2) is involved in the pathogenesis of the capillary leak syndrome in sepsis and has been shown to be ...
Le Cras, T.D.; Mobberley-Schuman, P.S.; Broering, M.; Fei, L.; Trenor, C.C., 3rd; Adams, D.M. Angiopoietins as serum biomarkers ...
Angiopoietins as Potential Targets in Management of Retinal Disease. Clin Ophthalmol. 2021. 15:3747-3755. [QxMD MEDLINE Link]. ...
angiopoietin 2. IEP. RGD. PMID:18342145. RGD:2314190. NCBI chr16:71,088,364...71,138,805 Ensembl chr16:71,088,364...71,138,804 ...
P. Zhu, M. J. Tan, R. L. Huang et al., "Angiopoietin-like 4 protein elevates the prosurvival intracellular O2-:H2O2 ratio and ... Elevated expression of angiopoietin-like 4 (ANGPTL4) is widespread in tumors and its role in anoikis resistance has been ...
"Roles of angiopoietins and VEGFs during normal and pathologic angiogenesis". Dan Dumont, Sunnybrook Health Science Center, ...
KRAS mutation-driven angiopoietin 2 bestows anti-VEGF resistance in epithelial carcinomas. Hosaka K, Andersson P, Wu J, He X, ...
Angiopoietins, growth factors, and vascular morphology in early arthritis. Ursula Fearon, Konstantina Griosios, Alexander ...
The levels of HIF-1α, angiopoietin-2 (Ang-2), and vascular endothelial growth factor (VEGF) expression in a cohort of chronic ... AFP: Alpha-fetoprotein; Ang-2:Angiopoietin-2; CH:Chronic hepatitis; ELISA:Enzyme -linked immunosorbent assay; EMT:Epithelial- ...
Evinacumab-dgnb is in a class of medications called angiopoietin-like protein 3 (ANGPTL3) inhibitor monoclonal antibodies. It ...
... hereditary angioedema with angiopoietin-1 gene; HAE-PLG, hereditary angioedema with plasminogen gene. ...
Differential expression of angiopoietin-2 and vascular endothelial growth factor in androgen-independent prostate cancer models ...
Structural basis for angiopoietin-1 mediated signaling initiation. 4k24. Structure of anti-uPAR Fab ATN-658 in complex with ... Angiopoietin-2/Tie2 Complex Crystal Structure. 2i9a. Crystal structure of the free aminoterminal fragment of urokinase type ...
A clinical trial has also been initiated for CTX310, targeting angiopoietin-related protein 3 (ANGPTL3). ...
Apolipoprotein CIII and Angiopoietin-like Protein 8 are Elevated in Lipodystrophy and Decrease after Metreleptin.. Lightbourne ... Metreleptin therapy lowers plasma angiopoietin-like protein 3 in patients with generalized lipodystrophy.. Muniyappa R, Abel BS ...
Angiopoietin-2 is a Tie-2 receptor ligand that is selectively released from WPB secretory granules. We identify a critical role ... Synaptotagmin-Like Protein 2a Regulates Angiogenic Lumen Formation via Weibel-Palade Body Apical Secretion of Angiopoietin-2 ... This disrupts the release of angiopoietin-2 and blocks Tie-2 signaling necessary for proper lumen formation. ... Furthermore, we provide evidence that WPB-housed angiopoietin-2 is required for vascular lumen formation. ...
... carnosine treatment prevented retinal vascular damage via normalization of the increased angiopoietin-2 and VEGF levels in ...
The angiocrine effects of IGF2 on placental microvasculature expansion are mediated, in part, through IGF2R and angiopoietin- ...

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