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Activation key verbace pro 0.9.2 activated partial thromboplastin

Registration key aPTSC - Clinical: Activated Partial Thromboplastin Time

Two-dimensional MXene/cobalt nanowire heterojunction for https://eldiesel21.ru/download/?file=103. Haveestimated, based onthe activated partial thromboplastin time (APTT) test, that a maximum plasma concentration of 9.5 jig ml-' LAM S5 is achievable before there is a significant effect on the coagulation system (Hoffman et al, 1995a). The report is directed to arm report readers with conclusive judgment on the potential of mentioned factors that propel growth in.

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Activated Partial Thromboplastin Test Market Growth – Owned. See more ideas about coumadin diet, vitamin k, warfarin diet. The activated partial thromboplastin time (APTT) was employed to analyze the anticoagulant effect of DE-CMs, and this value was measured using a commercially available kit (Nanjing Herb Source Bio-Tech, China) (Stangier, 2020; Andreas et al, 2020) containing sodium citrate anticoagulant (109 mM), kaolin-kephalin solution and CaCl 2 solution (25 mM).

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O'Brien S R, Teresa, Sellers T, Meyer D (1995) Artifactual Prolongation of the Activated Partial Thromboplastin Time Associated With Hemoconcentration in Dogs. To study and analyze the global Activated Partial Thromboplastin market size by key regions/countries, type and application, history data from 2020 to 2020, and forecast to 2020. The APTT assay depends on the phospholipid (a partial thromboplastin), contact activator (eg.

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The term 'Activated Partial Thromboplastin Time (APTT)' derives from the original form of the test (devised in ) in which only the phospholipid concentration of the test was controlled (as opposed to the phospholipid and the surface activator concentrations) and the name 'partial thromboplastin' was applied at the time to phospholipid. The global activated partial thromboplastin time test market was dominated by Europe, it was registered for majority of the activated partial thromboplastin market share, which was 30.0% in 2020. Activated Partial Thromboplastin Time Is a Better Trending click resources.

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Activated Partial Thromboplastin Time (APTT) Test & APTT https://eldiesel21.ru/download/?file=108. The Identification and Synthesis of Activated Plasma. Platelets are counted as part of a CBC, or complete blood count.

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H&O What is the partial thromboplastin time (PTT) test? Blood Chemical Test The following test was performed using collected blood from abdominal aorta at the same time with blood collection for heamtological examination. A client receiving a continuous intravenous (IV) infusion of heparin for the treatment of pulmonary embolism has an activated partial thromboplastin time (aPTT) level of 40 seconds.

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By definition, arterial blood gas (ABG) analysis shows. PCL-b-PHFBA nanofibrous membranes showed.

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Verbace pro 0.9.2 activated partial thromboplastin. APTT; PTT; Activated partial thromboplastin time. In particular, this report presents the global revenue market share of key companies in Activated Partial Thromboplastin business, shared in Chapter 3. This report presents.

Activated Partial Thromboplastin Time (aPTT)

Intrinsic pathway coagulation factor profile, aPTT, partial thromboplastin time, PTT, blood coagulation tests. On this website you will find: The full contents of the print textbook ("Book Chapters"), with over 150 bonus web-only chapters and dozens of additional images throughout. Patients: Thirty patients receiving continuous-infusion intravenous heparin.

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Prothrombin fragment F1+2. No tablet should be ingested if it is broken, cracked, or otherwise not intact. Pune, New York, USA, November 17 2020 (Wiredrelease) Research Dive: The global activated partial thromboplastin time test market forecast will surpass $601.2 million by the end of 2020, at a CAGR of 6.8%, and has been rising from $353.0 million in 2020, according to Activated Partial Thromboplastin.

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Plasma Thromboplastin Antecedent (PTA) or antihemophilic factor C. Activated by thrombin in extrinsic pathway to increase production of thrombin inside fibrin clot. The Global Activated Partial Thromboplastin Test Market Growth 2020 - This report provides market size, growth, trends, statistics, price & top players share along with the driver opportunities and analysis by region for the forecast period up to 2020. Additional sources were identified from the reference lists of these articles.

Annexin A8 (ANXA8) regulates proliferation of porcine

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Association between activated partial thromboplastin time. Recent references from PubMed and VetMedResource; Watts J (2020) The use of bipolar electrosurgical forceps for haemostasis in open surgical ovariectomy of bitches and queens and castration of dogs. This APTT screening test is also used to ensure whether the right dose of heparin is being used.

ACE2 down-regulation and its effects on the body. Hypokalemia, inflammation, fibrosis, oxidative stress, and clotting?

I've spent the past few months studying this virus and its effects in-depth. We know that SARS-CoV-2 uses ACE2 as its entry receptor, and we know that it down-regulates this receptor and results in an over-abundance of Angiotensin II. We know this because the severe and critical patients almost invariably present with hypokalemia, low blood potassium. The action of excessive Angiotensin II on AT1 receptors is the cause. It makes you secrete more aldosterone and excrete more potassium.
https://www.diabetesresearchclinicalpractice.com/article/S0168-8227(20)30382-X/fulltext
That got me thinking, what else does Angiotensin II do?
I started digging around and I found a paper with a handy-dandy table:
https://www.nature.com/articles/1002101
https://www.nature.com/articles/1002101/tables/1
Let's go down the list, shall we?
Nuclear factor kappa-light-chain-enhancer of activated B cells, or NF-κB. Highly pro-inflammatory initiator of cytokine release. Unregulated NF-κB is implicated in asthma, rheumatoid arthritis, inflammatory bowel disease, and multiple sclerosis. Autoimmune diseases.
https://en.wikipedia.org/wiki/NF-%CE%BAB
NF-κB (nuclear factor kappa-light-chain-enhancer of activated B cells) is a protein complex that controls transcription of DNA, cytokine production and cell survival. NF-κB is found in almost all animal cell types and is involved in cellular responses to stimuli such as stress, cytokines, free radicals, heavy metals, ultraviolet irradiation, oxidized LDL, and bacterial or viral antigens.[1][2][3][4][5] NF-κB plays a key role in regulating the immune response to infection. Incorrect regulation of NF-κB has been linked to cancer, inflammatory and autoimmune diseases, septic shock, viral infection, and improper immune development. NF-κB has also been implicated in processes of synaptic plasticity and memory.[6][7][8][9][10][11]
Inhibitor of κB. Sounds like it counters the action of NF-κB, right? Wrong. It regulates and enhances it.
https://en.wikipedia.org/wiki/I%CE%BAB_kinase
IκB kinase activity is essential for activation of members of the nuclear factor-kB (NF-κB) family of transcription factors, which play a fundamental role in lymphocyte immunoregulation.[6][8] Activation of the canonical, or classical, NF-κB pathway begins in response to stimulation by various pro-inflammatory stimuli, including lipopolysaccharide (LPS) expressed on the surface of pathogens, or the release of pro-inflammatory cytokines such as tumor necrosis factor (TNF) or interleukin-1 (IL-1). Following immune cell stimulation, a signal transduction cascade leads to the activation of the IKK complex, an event characterized by the binding of NEMO to the homologous kinase subunits IKK-α and IKK-β. The IKK complex phosphorylates serine residues (S32 and S36) within the amino-terminal domain of inhibitor of NF-κB (IκBα) upon activation, consequently leading to its ubiquitination and subsequent degradation by the proteasome.[5] Degradation of IκBα releases the prototypical p50-p65 dimer for translocation to the nucleus, where it binds to κB sites and directs NF-κB-dependent transcriptional activity.[8] NF-κB target genes can be differentiated by their different functional roles within lymphocyte immunoregulation and include positive cell-cycle regulators, anti-apoptotic and survival factors, and pro-inflammatory genes. Collectively, activation of these immunoregulatory factors promotes lymphocyte proliferation, differentiation, growth, and survival.[9]
Nicotinamide adenine dinucleotide phosphate oxidase, or NADPH oxidase. Catalyzes production of superoxide free radicals to kill invaders.
https://en.wikipedia.org/wiki/NADPH_oxidase
Superoxides are crucial in killing foreign bacteria in the human body. Consequently, under-activity can lead to an increased susceptibility to organisms such as catalase-positive microbes, and over-activity can lead to oxidative stress and cell damage. Excessive production of ROS in vascular cells causes many forms of cardiovascular disease including hypertension, atherosclerosis, myocardial infarction, and ischemic stroke.[11] Atherosclerosis is caused by the accumulation of macrophages containing cholesterol (foam cells) in artery walls (in the intima). ROS produced by NADPH oxidase activate an enzyme that makes the macrophages adhere to the artery wall (by polymerizing actin fibers). This process is counterbalanced by NADPH oxidase inhibitors, and by antioxidants. An imbalance in favor of ROS produces atherosclerosis. In vitro studies have found that the NADPH oxidase inhibitors apocynin and diphenyleneiodonium, along with the antioxidants N-acetyl-cysteine and resveratrol, depolymerized the actin, broke the adhesions, and allowed foam cells to migrate out of the intima.[12][13] One study suggests a role for NADPH oxidase in ketamine-induced loss of neuronal parvalbumin and GAD67 expression.[14] Similar loss is observed in schizophrenia, and the results may point at the NADPH oxidase as a possible player in the pathophysiology of the disease.[15] Nitro blue tetrazolium is used in a diagnostic test, in particular, for chronic granulomatous disease, a disease in which there is a defect in NADPH oxidase; therefore, the phagocyte is unable to make the reactive oxygen species or radicals required for bacterial killing, resulting in bacteria thriving within the phagocyte. The higher the blue score the better the cell is at producing reactive oxygen species. It has also been shown that NADPH oxidase plays a role in the mechanism that induces the formation of sFlt-1, a protein that deactivates certain proangiogenic factors that play a role in the development of the placenta, by facilitating the formation of reactive oxygen species, which are suspected intermediaries in sFlt-1 formation. These effects are in part responsible for inducing pre-eclampsia in pregnant women[16]
Neutrophil cytosol factor 1, also known as p47phox. Activates the aforementioned NADPH oxidase.
https://en.wikipedia.org/wiki/Neutrophil_cytosolic_factor_1
The protein encoded by this gene is a 47 kDa cytosolic subunit of neutrophil NADPH oxidase. This oxidase is a multicomponent enzyme that is activated to produce superoxide anion. Mutations in this gene have been associated with chronic granulomatous disease.[5] Genetic variability in the NCF1 gene has been found to be related to a higher chance of getting autoimmune diseases such as Sjögren's syndrome, rheumatoid arthritis and lupus erythematosus.[6]
Tumor necrosis factor alpha, or TNF-α. Hilariously inflammatory and cytotoxic. Implicated in some autoimmune diseases. Having too much of it can actually cause cancer, which makes perfect sense, given that systemic inflammation basically rolls the dice as your body regenerates the damage, and if it messes up the cell replication, whoops, cancer.
https://en.wikipedia.org/wiki/Tumor_necrosis_factor_alpha
Tumor necrosis factor (TNF, cachexin, or cachectin; once named as tumor necrosis factor alpha or TNFα) is a cell signaling protein (cytokine) involved in systemic inflammation and is one of the cytokines that make up the acute phase reaction. It is produced chiefly by activated macrophages, although it can be produced by many other cell types such as CD4+ lymphocytes, NK cells, neutrophils, mast cells, eosinophils, and neurons.[5] TNF is a member of the TNF superfamily, consisting of various transmembrane proteins with a homologous TNF domain. The primary role of TNF is in the regulation of immune cells. TNF, being an endogenous pyrogen, is able to induce fever, apoptotic cell death, cachexia, inflammation and to inhibit tumorigenesis and viral replication and respond to sepsis via IL1- & IL6-producing cells. Dysregulation of TNF production has been implicated in a variety of human diseases including Alzheimer's disease,[6] cancer,[7] major depression,[8] psoriasis[9] and inflammatory bowel disease (IBD).[10] Though controversial, studies of depression and IBD are currently being linked to increased levels of TNF.[11][12] Recombinant TNF is used as an immunostimulant under the INN tasonermin. TNF can be produced ectopically in the setting of malignancy and parallels parathyroid hormone both in causing secondary hypercalcemia and in the cancers with which excessive production is associated.[/quote]
Interleukin-6, or IL-6. A highly inflammatory cytokine produced as a response to infection and stress.
https://en.wikipedia.org/wiki/Interleukin_6
IL-6 is an important mediator of fever and of the acute phase response. It is capable of crossing the blood-brain barrier[8] and initiating synthesis of PGE2 in the hypothalamus, thereby changing the body's temperature setpoint. In muscle and fatty tissue, IL-6 stimulates energy mobilization that leads to increased body temperature. IL-6 can be secreted by macrophages in response to specific microbial molecules, referred to as pathogen-associated molecular patterns (PAMPs). These PAMPs bind to an important group of detection molecules of the innate immune system, called pattern recognition receptors (PRRs), including Toll-like receptors (TLRs). These are present on the cell surface and intracellular compartments and induce intracellular signaling cascades that give rise to inflammatory cytokine production. IL-6 is found in many supplemental cloning media such as briclone. Inhibitors of IL-6 (including estrogen) are used to treat postmenopausal osteoporosis. IL-6 is also produced by adipocytes and is thought to be a reason why obese individuals have higher endogeneous levels of CRP.[9] Intranasally administered IL-6 has been shown to improve sleep-associated consolidation of emotional memories.[10] IL-6 is responsible for stimulating acute phase protein synthesis, as well as the production of neutrophils in the bone marrow. It supports the growth of B cells and is antagonistic to regulatory T cells. When psychologically stressed, the human body produces stress hormones like cortisol, which are able to trigger interleukin-6 release into the circulation.[11]
Chemokine ligand 2, also known as MCP1. A cytokine that recruits monocytes, memory T cells, and dendritic cells to a site of inflammation. Implicated in autoimmune diseases like rheumatoid arthritis and idiopathic pulmonary fibrosis.
The chemokine (C-C motif) ligand 2 (CCL2) is also referred to as monocyte chemoattractant protein 1 (MCP1) and small inducible cytokine A2. CCL2 is a small cytokine that belongs to the CC chemokine family. CCL2 recruits monocytes, memory T cells, and dendritic cells to the sites of inflammation produced by either tissue injury or infection.[3][4][/quote]
I did a little Googling on the side and found this. Wow!
https://www.sciencedirect.com/science/article/abs/pii/0046817794901171?via%3Dihub
Macrophages play a crucial role in the pathogenesis of idiopathic pulmonary fibrosis (IPF). To examine the mechanisms for increased monocyte/macrophage recruitment in IPF and nonIPF interstitial lung diseases (nonIPF) the localization of monocyte chemoattractant protein-1 (MCP-1) was investigated in 14 cases of IPF, seven cases of nonIPF, and seven normal control lungs (CTRL) by immunohistochemistry using a specific anti-MCP-1 monoclonal antibody, F9. By double immunohistochemical staining using F9 and one of the cell type specific antibodies significant differences in the staining pattern of MCP-1 were observed between IPF and nonIPF. In IPF MCP-1 was observed in cuboidal and flattened metaplastic epithelial cells, alveolar macrophages, and vascular endothelial cells. In contrast, no epithelial cells were stained for MCP-1 in nonIPF cases, although alveolar macrophages and vascular endothelial cells were labeled. Northern hybridization analysis of selected cases showed marked expression of MCP-1 messenger RNA (mRNA) in IPF and nonIPF compared with CTRL. These findings suggest that the MCP-1 production in IPF and nonIPF plays an important role in the recruitment of monocyte/macrophages. Monocyte chemoattractant protein-1 production by epithelial cells in IPF may be caused by the metaplastic nature of the epithelial cells and may be one of the key factors inducing the irreversible progression of IPF.[/quote]
So, uncontrolled MCP1 expression can help scar the lungs by promoting monocyte activity. Interesting. Let's continue going down the list.
Intercellular adhesion molecule-1, or ICAM-1. Helps leukocytes enter the endothelium. Acts like a maintenance access hatch for the lining of blood vessels.
https://en.wikipedia.org/wiki/ICAM-1
The protein encoded by this gene is a type of intercellular adhesion molecule continuously present in low concentrations in the membranes of leukocytes and endothelial cells. Upon cytokine stimulation, the concentrations greatly increase. ICAM-1 can be induced by interleukin-1 (IL-1) and tumor necrosis factor (TNF) and is expressed by the vascular endothelium, macrophages, and lymphocytes. ICAM-1 is a ligand for LFA-1 (integrin), a receptor found on leukocytes.[9] When activated, leukocytes bind to endothelial cells via ICAM-1/LFA-1 and then transmigrate into tissues.[10] LFA-1 has also been found in a soluble form,[11] which seems to bind and block ICAM-1.[12] ICAM-1 is an endothelial- and leukocyte-associated transmembrane protein long known for its importance in stabilizing cell-cell interactions and facilitating leukocyte endothelial transmigration. More recently, ICAM-1 has been characterized as a site for the cellular entry of human rhinovirus.[13] Because of these associations with immune responses, it has been hypothesized that ICAM-1 could function in signal transduction. ICAM-1 ligation produces proinflammatory effects such as inflammatory leukocyte recruitment by signaling through cascades involving a number of kinases, including the kinase p56lyn.
Vascular cell adhesion molecule-1, or VCAM-1. Has a very similar function to ICAM-1. Whereas ICAM-1 facilitates the transmigration of leukocytes through the endothelium, VCAM-1 facilitates the adhesion to it.
https://en.wikipedia.org/wiki/VCAM-1
The VCAM-1 protein mediates the adhesion of lymphocytes, monocytes, eosinophils, and basophils to vascular endothelium. It also functions in leukocyte-endothelial cell signal transduction, and it may play a role in the development of atherosclerosis and rheumatoid arthritis. Upregulation of VCAM-1 in endothelial cells by cytokines occurs as a result of increased gene transcription (e.g., in response to Tumor necrosis factor-alpha (TNF-α) and Interleukin-1 (IL-1)) and through stabilization of Messenger RNA (mRNA) (e.g., Interleukin-4 (IL-4)). The promoter region of the VCAM-1 gene contains functional tandem NF-κB (nuclear factor-kappa B) sites. The sustained expression of VCAM-1 lasts over 24 hours. Primarily, the VCAM-1 protein is an endothelial ligand for VLA-4 (Very Late Antigen-4 or integrin α4β1) of the β1 subfamily of integrins. VCAM-1 expression has also been observed in other cell types (e.g., smooth muscle cells). It has also been shown to interact with EZR[7] and Moesin.[7] CD106 also exists on the surface of some subpopulations of mesenchymal stem cells(MSC).[8]
Reactive oxygen species, or ROS. A major component of the oxidative stress response. Helps nuke pathogens out of existence.
https://en.wikipedia.org/wiki/Reactive_oxygen_species
In the mammalian host, ROS is induced as an antimicrobial defense. To highlight the importance of this defense, individuals with chronic granulomatous disease who have deficiencies in generating ROS, are highly susceptible to infection by a broad range of microbes including Salmonella enterica, Staphylococcus aureus, Serratia marcescens, and Aspergillus spp. Studies on the homeostasis of the Drosophila melanogaster’s intestines have shown the production of ROS as a key component of the immune response in the gut of the fly. ROS acts both as a bactericide, damaging the bacterial DNA, RNA and proteins, as well as a signalling molecule that induces repair mechanisms of the epithelium.[19] The uracil released by microorganism triggers the production and activity of Duox, the ROS-producing enzyme in the intestine. Duox activity is induced according to the level of uracil in the gut; under basal conditions, it is down-regulated by the protein kinase MkP3. The tight regulation of Duox avoids excessive production of ROS and facilitates differentiation between benign and damage-inducing microorganisms in the gut.[20] The exact manner in which ROS defends the host from invading microbe is not fully understood. One of the more likely modes of defense is damage to microbial DNA. Studies using Salmonella demonstrated that DNA repair mechanisms were required to resist killing by ROS. More recently, a role for ROS in antiviral defense mechanisms has been demonstrated via Rig-like helicase-1 and mitochondrial antiviral signaling protein. Increased levels of ROS potentiate signaling through this mitochondria-associated antiviral receptor to activate interferon regulatory factor (IRF)-3, IRF-7, and nuclear factor kappa B (NF-κB), resulting in an antiviral state.[21] Respiratory epithelial cells were recently demonstrated to induce mitrochondrial ROS in response to influenza infection. This induction of ROS led to the induction of type III interferon and the induction of an antiviral state, limiting viral replication.[22] In host defense against mycobacteria, ROS play a role, although direct killing is likely not the key mechanism; rather, ROS likely affect ROS-dependent signalling controls, such as cytokine production, autophagy, and granuloma formation.[23] Reactive oxygen species are also implicated in activation, anergy and apoptosis of T cells.[24]
Superoxide. Same function as above, pretty much.
https://en.wikipedia.org/wiki/Superoxide
Superoxide and hydroperoxyl (HO2) are often discussed interchangeably, although superoxide predominates at physiological pHs. Both superoxide and hydroperoxyl are classified as reactive oxygen species.[3] It is generated by the immune system to kill invading microorganisms. In phagocytes, superoxide is produced in large quantities by the enzyme NADPH oxidase for use in oxygen-dependent killing mechanisms of invading pathogens. Mutations in the gene coding for the NADPH oxidase cause an immunodeficiency syndrome called chronic granulomatous disease, characterized by extreme susceptibility to infection, especially catalase-positive organisms. In turn, micro-organisms genetically engineered to lack the superoxide-scavenging enzyme superoxide dismutase (SOD) lose virulence. Superoxide is also deleterious when produced as a byproduct of mitochondrial respiration (most notably by Complex I and Complex III), as well as several other enzymes, for example xanthine oxidase[9], which can catalyze the transfer of electrons directly to molecular oxygen under strongly reducing conditions.
Tissue factor, or CD142. A highly pro-thrombotic agent. Promotes clotting.
https://en.wikipedia.org/wiki/Tissue_factor
Tissue factor, also called platelet tissue factor, factor III, or CD142, is a protein encoded by the F3 gene, present in subendothelial tissue and leukocytes. Its role in the clotting process is the initiation of thrombin formation from the zymogen prothrombin. Thromboplastin defines the cascade that leads to the activation of factor X—the tissue factor pathway. In doing so, it has replaced the previously named extrinsic pathway in order to eliminate ambiguity. The F3 gene encodes coagulation factor III, which is a cell surface glycoprotein. This factor enables cells to initiate the blood coagulation cascades, and it functions as the high-affinity receptor for the coagulation factor VII. The resulting complex provides a catalytic event that is responsible for initiation of the coagulation protease cascades by specific limited proteolysis. Unlike the other cofactors of these protease cascades, which circulate as nonfunctional precursors, this factor is a potent initiator that is fully functional when expressed on cell surfaces. There are three distinct domains of this factor: extracellular, transmembrane, and cytoplasmic. This protein is the only one in the coagulation pathway for which a congenital deficiency has not been described.[5] In addition to the membrane-bound tissue factor, soluble form of tissue factor was also found which results from alternatively spliced tissue factor mRNA transcripts, in which exon 5 is absent and exon 4 is spliced directly to exon 6.[6][7]
Plasminogen activator inhibitor-1, or PAI-1. Again, a highly pro-thrombotic agent that promotes clotting and prevents clots from breaking down. I'm starting to see a pattern, here.
https://en.wikipedia.org/wiki/Plasminogen_activator_inhibitor-1
PAI-1's main function entails the inhibition of urokinase plasminogen activator (uPA), an enzyme responsible for the cleavage of plasminogen to form plasmin. Plasmin mediates the degradation of the extracellular matrix either by itself or in conjunction with matrix metalloproteinases. In this scenario, PAI-1 inhibits uPA via active site binding, preventing the formation of plasmin. Additional inhibition is mediated by PAI-1 binding to the uPA/uPA receptor complex, resulting in the latter's degradation.[6] Thus, PAI can be said to inhibit the serine proteases tPA and uPA/urokinase, and hence is an inhibitor of fibrinolysis, the physiological process that degrades blood clots. In addition, PAI-1 inhibits the activity of matrix metalloproteinases, which play a crucial role in invasion of malignant cells through the basal lamina.
Activator protein-1, or AP-1. A regulator of gene expression, cell proliferation, and apoptosis (or programmed cell death). This guy is the janitor of human skin cells, basically.
https://en.wikipedia.org/wiki/AP-1_transcription_factor
AP-1 transcription factor has been shown to have a hand in a wide range of cellular processes, including cell growth, differentiation, and apoptosis. AP-1 activity is often regulated via post-translational modifications, DNA binding dimer composition, and interaction with various binding partners. AP-1 transcription factors are also associated with numerous physiological functions especially in determination of organisms’ life span and tissue regeneration. Below are some of the other important functions and biological roles AP-1 transcription factors have been shown to be involved in. The AP-1 transcription factor has been shown to play numerous roles in cell growth and proliferation. In particular, c-Fos and c-Jun seem to be major players in these processes. C-jun has been shown to be essential for fibroblast proliferation,[13] and levels of both AP-1 subunits have been shown to be expressed above basal levels during cell division.[14] C-fos has also been shown to increase in expression in response to the introduction of growth factors in the cell, further supporting its suggested involvement in the cell cycle. The growth factors TGF alpha, TGF beta, and IL2 have all been shown to stimulate c-Fos, and thereby stimulate cellular proliferation via AP-1 activation.[10] AP-1 transcription is deeply involved in the modulation of gene expression. Changes in cellular gene expression in the initiation of DNA synthesis and the formation of differentiated derivatives can lead to cellular differentiation.[10] AP-1 has been shown to be involved in cell differentiation in several systems. For example, by forming stable heterodimers with c-Jun, the bZIP region of c-Fos increases the binding of c-Jun to target genes whose activation is involved in the differentiation of chicken embryo fibroblasts (CEF).[15] AP-1 transcription factor is associated with a broad range of apoptosis related interactions. AP-1 activity is induced by numerous extracellular matrix and genotoxic agents, suggesting involvement in programmed cell death.[2] Many of these stimuli activate the c-Jun N-terminal kinases (JNKs) leading to the phosphorylation of Jun proteins and enhanced transcriptional activity of AP-1 dependent genes.[2] Increases in the levels of Jun and Fos proteins and JNK activity have been reported in scenarios in which cells undergo apoptosis. For example, inactivated c-Jun-ER cells show a normal morphology, while c-Jun-ER activated cells have been shown to be apoptotic.[16][/quote]
Matrix metalloproteinase, or MMP. Helps degrade ECMs.
https://en.wikipedia.org/wiki/Matrix_metallopeptidase
The MMPs play an important role in tissue remodeling associated with various physiological or pathological processes such as morphogenesis, angiogenesis, tissue repair, cirrhosis, arthritis, and metastasis. MMP-2 and MMP-9 are thought to be important in metastasis. MMP-1 is thought to be important in rheumatoid arthritis and osteoarthritis. Recent data suggests active role of MMPs in the pathogenesis of Aortic Aneurysm. Excess MMPs degrade the structural proteins of the aortic wall. Disregulation of the balance between MMPs and TIMPs is also a characteristic of acute and chronic cardiovascular diseases.[16]
C-reactive protein, or CRP. Secreted by the liver in response to IL-6, mostly to help the body clean up cellular junk. This is the guy who roams the battlefield and collects the dog tags.
https://en.wikipedia.org/wiki/C-reactive_protein
CRP binds to the phosphocholine expressed on the surface of dead or dying cells and some bacteria. This activates the complement system, promoting phagocytosis by macrophages, which clears necrotic and apoptotic cells and bacteria.[13] This so-called acute phase response occurs as a result of increasing concentrations of IL-6, which is produced by macrophages[6] as well as adipocytes[7] in response to a wide range of acute and chronic inflammatory conditions such as bacterial, viral, or fungal infections; rheumatic and other inflammatory diseases; malignancy; and tissue injury and necrosis. These conditions cause release of interleukin-6 and other cytokines that trigger the synthesis of CRP and fibrinogen by the liver. CRP binds to phosphocholine on micro-organisms. It is thought to assist in complement binding to foreign and damaged cells and enhances phagocytosis by macrophages (opsonin-mediated phagocytosis), which express a receptor for CRP. It plays a role in innate immunity as an early defence system against infections.[13]
Serum amyloid A, or SAA. No, not Single Action Army. Moves cholesterol around, recruits immune cells to respond to inflammation like a 911 dispatcher, and induces enzymes to degrade the ECM.
https://en.wikipedia.org/wiki/Serum_amyloid_A
Acute-phase serum amyloid A proteins (A-SAAs) are secreted during the acute phase of inflammation. These proteins have several roles, including the transport of cholesterol to the liver for secretion into the bile, the recruitment of immune cells to inflammatory sites, and the induction of enzymes that degrade extracellular matrix. A-SAAs are implicated in several chronic inflammatory diseases, such as amyloidosis, atherosclerosis, and rheumatoid arthritis.[2] Three acute-phase SAA isoforms have been reported in mice, called SAA1, SAA2, and SAA3. During inflammation, SAA1 and SAA2 are expressed and induced principally in the liver, whereas SAA3 is induced in many distinct tissues. SAA1 and SAA2 genes are regulated in liver cells by the proinflammatory cytokines IL-1, IL-6, and TNF-α. Both SAA1 and SAA2 are induced up to a 1000-fold in mice under acute inflammatory conditions following exposure to bacterial lipopolysaccharide (LPS).[2] Three A-SAA genes have also been identified in humans,[3] although the third gene, SAA3, is believed to represent a pseudogene that does not generate messenger RNA or protein.[4] Molecular weights of the human proteins are estimated at 11.7 kDa for SAA1[5] and 12.8 kDa for SAA4.[6] Serum amyloid A (SAA) is also an acute phase marker that responds rapidly. Similar to CRP, levels of acute-phase SAA increase within hours after inflammatory stimulus, and the magnitude of increase may be greater than that of CRP. Relatively trivial inflammatory stimuli can lead to SAA responses. It has been suggested that SAA levels correlate better with disease activity in early inflammatory joint disease than do ESR and CRP. Although largely produced by hepatocytes, more recent studies show that SAA is produced by adipocytes as well, and its serum concentration is associated with body mass index.[7]
That's quite the list.
Wow, you know what all this sounds to me like a recipe for? Major clotting, fibrosis, oxidative stress, and cytokine storms.
You know what COVID-19 patients have? Major clotting, fibrosis, oxidative stress, and cytokine storms.
https://www.nejm.org/doi/full/10.1056/NEJMc2007575
We describe a patient with Covid-19 and clinically significant coagulopathy, antiphospholipid antibodies, and multiple infarcts. He was one of three patients with these findings in an intensive care unit designated for patients with Covid-19. This unit, which was managed by a multidisciplinary team from Peking Union Medical College Hospital in the Sino–French New City Branch of Tongji Hospital in Wuhan, China, was set up on an emergency basis to accept the most critically ill patients during the outbreak of Covid-19. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection was confirmed in all the patients by reverse-transcriptase–polymerase-chain-reaction (RT-PCR) assay or serologic testing.
https://www.dw.com/en/covid-19-recovered-patients-have-partially-reduced-lung-function/a-52859671
Further investigations of the recovered COVID-19 patients must now be conducted to show whether they have developed pulmonary fibrosis — scarring in the lungs. Over time, the scar tissue can destroy the normal lung and make it hard for oxygen to get into the blood. Low oxygen levels (and the stiff scar tissue itself) can cause shortness of breath, particularly during physical exertion. Lung fibrosis cannot be cured because the scarred changes in the lung tissue do not regress. But the progression of pulmonary fibrosis can be delayed and sometimes even stopped if detected in time.
https://www.preprints.org/manuscript/202003.0346/v1/download
Dysregulation of immune responses following hyper-inflammation and cytokine storm, may lead to multiple organ failure, pulmonary tissue damage, and reduced lung capacity which is well-known in patients with COVID-19 infection (34, 36). Present data in COVID-19 infected patients showed a significantly increased level of plasma pro-inflammatory cytokines including MCP1, MIP1α, MIP1β, IL1-β, IL1RA, IL7, IL8, IL9, IL10, IP10, PDGFB basic FGF2, GCSF, GMCSF, IFNγ, TNFα, and VEGFA (37). In conclusion, viral infection initiates a detrimental cycle of oxidative stress-mediated functions including PARP and PARG activity, ADP ribose increase, TRPM2 activity, apoptosis and/or necrosis (parthanatos) (38) and inflammatory and vasodilator agents Preprints (www.preprints.org) | NOT PEER-REVIEWED | Posted: 23 March 2020 doi:10.20944/preprints202003.0346.v1 release. Together, all these mechanisms result in endothelial dysfunction and extravasation of immune cells in alveolar space and finally a ground glass pattern in chest X ray. The trapped immune cells release large amounts of cytokines which leads to systemic inflammatory response syndrome (SIRS), a figure usually seen in septic shock and other cause of acute respiratory distress syndrome (ARDS) like paraquat (1,10-dimethyl-4,40- bipyridinium dichloride; PQ ) poisoning (39)(Fig 1).
Now, some have suspected that the use of ARBs, or angiotensin receptor blockers, may be harmful because it may up-regulate ACE2 and enhance viral entry. However, individuals with high blood pressure who continued taking ARBs during a COVID-19 infection displayed reduced illness and reduced mortality:
https://www.thecardiologyadvisor.com/home/topics/hypertension/treating-hypertension-and-covid-19-with-ace-inhibitors-or-arbs-may-improve-clinical-outcomes/
The median number of days from symptom onset to hospital admission and discharge were 2.0 and 16.5, respectively in the non-ACEI/ARB group, and 3.0 and 20.0, respectively in the ACEI/ARB group. The median heart rates were 90.5 bpm and 80.0 bpm in the non-ACEI/ARB and ACEI/ARB groups, respectively, and the median respiratory rate was 20.0 in both groups. There was a greater percentage of patients treated with non-ACEI/ARB vs ACEI/ARB categorized as exhibiting a severe case of COVID-19 during hospitalization (48% vs 23.5%, respectively; 1 vs 0 death, respectively). Levels of C-reactive protein and lactate dehydrogenase, as well as counts of white blood cells, neutrophils, and platelets were comparable between the 2 groups, and absolute numbers of CD3+ and CD8+ (but not CD4+) T-cells were higher in the ACEI/ARB vs non-ACEI/ARB group (P =.02 and P =.01, respectively). Levels of interleukin-6 (IL-6) had a lower, nonsignificant trend in the ACEI/ARB group, and the peak viral load was lower in the ACEI/ARB vs non-ACEI/ARB group during hospitalization (P =.03), but not at hospital admission. “[W]e found that ACEI/ARB therapy attenuated the inflammatory response, potentially through the inhibition of IL-6 levels, which is consistent with the findings that ACEI and ARB therapy alleviated [lipopolysaccharide]-induced pneumonic injury,6” noted the study authors. “This study also suggests that ACEI/ARB therapy had a beneficial effect on the immune system by avoiding peripheral T cell depletion…[W]e hypothesize that RAS inhibitors do not directly inhibit viral replication; rather, they play an indirect antiviral role by regulating immune function and inhibiting inflammatory responses.”
IL-6 and TNF-α are major inflammatory markers in COVID-19 infection. Patients often have major coagulopathy and endothelial dysfunction driven perhaps by severe endotheliitis and the release of endogenous pro-thrombotic agents. They have fibrosis and scarring of the parenchyma of the lungs, and they have oxidative damage to the tissues. Sometimes, the inflammation caused by the cytokine release syndrome is so severe, it progresses to hemorrhagic necrosis of brain, heart, lung, and kidney tissues.
In conclusion, we need studies and clinical trials to test and see if Losartan and other ARBs have a beneficial effect in reducing COVID-19-associated inflammation.
submitted by THASF to CoronavirusFOS

Haemostatic Alterations after Sildenafil and Tramadol Administration in Rats | Journal of Advances in Medicine and Medical Research

Haemostatic parameters constitute measurable indices in the haemostatic system used to assess the functionality of the coagulation system of an individual to establish a state of health or disorder. This study evaluated haemostatic parameter such as platelets count, mean platelet volume (MPV), platelets distribution width (PDW), prothrombin time (PT) and activated partial thromboplastin time (APTT) in 22 Male Albino Rats grouped and orally treated daily for three weeks with Sildenafil (4 mg/200 g.bwt), Tramadol(6 mg/200 g.bwt) and Sildenafil/Tramadol combination (4+6 mg/220 g.bwt). Rats were sacrificed by cardiac puncture and 5 mls of blood collected for the analysis of the parameters using Sysmex haematology analyser and Agape Diagnostic reagents kits. Results obtained shows a statistically significant increase in platelet count, PT and APTT compared with control across the various groups (p<0.05). A statistically significant decrease was observed in MPV, PDW in Sildenafil+tramadol group, significant decrease in platelets distribution width for Tramadol group when compared with control (p<0.05). No significant difference was observed in the mean platelets volume and platelet distribution width in Sildenafil group. A comparison of Sildenafil+tramadol and Sildenafil groups shows no statistically significant difference in all the parameters analysed. There was also no significant difference in the mean platelets count, PDW, PT and APTT when Sildenafil+tramadol and Tramadol groups were compared (p<0.05). However, a statistically significant increase was seen in platelets count when Sildenafil+tramadol and tramadol were compared (p<0.05). Sildenafil and tramadol causes significant increase in platelets count, prolonged PT and APTT following single/combined daily administration in rats. Further research on these parameters, assessment of liver function, and measurement of intrinsic and extrinsic pathway coagulation factors in human taking this medication is recommended.
Please read full article –https://www.journaljammr.com/index.php/JAMM
Keywords: Haemostatic, sildenafil, tramadol, prothrombin, thromboplastin
submitted by sciencedomain to u/sciencedomain

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