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Acute Phase Proteins

Acute Phase Proteins Background

Available Resources for Acute Phase Proteins

With Creative BioMart, you can find a diverse range of products related to acute phase proteins. We offer recombinant proteins that can be used for various research purposes. Additionally, we provide customized services to meet your specific requirements, ensuring that you get the products you need.

In addition to our products and services, we also offer a wealth of resources for your reference. Our resources cover various aspects of acute phase proteins, including the involved pathways, protein functions, interacting proteins, relevant articles, research areas, and other related topics. These resources can be invaluable for researchers looking to deepen their understanding of Acute Phase Proteins and their role in physiological processes.

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About Acute Phase Proteins

Acute phase proteins (APPs) are a group of proteins synthesized by the liver in response to inflammation, infection, tissue injury, or other physiological disruptions. They play a crucial role in the acute phase response, which is a rapid and nonspecific reaction of the body to these stimuli. The acute phase response is a component of the innate immune system and is aimed at restoring homeostasis and initiating the immune defense mechanisms.

During the acute phase response, the levels of certain proteins in the blood change significantly. APPs can be classified into positive acute phase proteins and negative acute phase proteins, depending on whether their concentrations increase or decrease in response to the inflammatory stimulus.

  • Positive acute phase proteins: These proteins show an increase in their synthesis and release during the acute phase response. Examples of positive acute phase proteins include C-reactive protein (CRP), fibrinogen, serum amyloid A (SAA), haptoglobin, alpha-1 antitrypsin, and ferritin. These proteins participate in various physiological processes, such as inflammation modulation, pathogen clearance, tissue repair, and iron sequestration.
  • Negative acute phase proteins: These proteins exhibit a decrease in their synthesis and release during the acute phase response. Albumin and transthyretin (prealbumin) are examples of negative acute-phase proteins. The reduction in their levels is thought to be a result of the body's increased demand for amino acids to synthesize positive acute-phase proteins.

Based on their mode of action, APP classified as below:

  • Protease inhibitors, e.g., alpha 1 antitrypsin, alpha 1 antichymotrypsin.
  • Coagulation proteins, e.g., fibrinogen, prothrombin.
  • Complement proteins, e.g., C2, C3, C4, C5, etc.
  • Transport proteins, e.g., Hp, Cp, hemopexin.
  • Other proteins, e.g., CRP, SAA, SAP, acid glycoprotein (AGP).

The induction and regulation of acute phase proteins are primarily mediated by pro-inflammatory cytokines, such as interleukin-1 (IL-1), interleukin-6 (IL-6), and tumor necrosis factor-alpha (TNF-α). These cytokines are produced by immune cells and other cell types in response to the presence of pathogens, tissue damage, or other inflammatory signals.

The measurement of acute phase proteins, particularly CRP, is commonly used in clinical settings as a marker of inflammation and disease activity. Elevated levels of acute-phase proteins can indicate the presence of infection, inflammation, autoimmune disorders, or certain malignancies.

In summary, acute phase proteins are an important component of the innate immune response. Their altered levels during the acute phase response serve as indicators of inflammation and help to initiate and regulate various processes involved in the body's defense and recovery mechanisms.

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Regulation and Functions of Acute Phase Proteins

The regulation and functions of APPs are tightly linked to the inflammatory response and play crucial roles in various physiological processes. Here are some key aspects of the regulation and functions of APPs:

Regulation of Acute Phase Proteins

  • Cytokines: The synthesis of many APPs is regulated by pro-inflammatory cytokines, such as interleukin-1 (IL-1), interleukin-6 (IL-6), and tumor necrosis factor-alpha (TNF-α). These cytokines are produced by immune cells and other cell types in response to infection, tissue injury, or inflammation, and they stimulate the liver to produce APPs.
  • Signal Transduction Pathways: Cytokines and other signaling molecules activate specific intracellular pathways, such as the Janus kinase-signal transducer and activator of transcription (JAK-STAT) pathway, nuclear factor-kappa B (NF-κB) pathway, and mitogen-activated protein kinase (MAPK) pathway, which regulate the transcription and synthesis of APPs.

Functions of Acute Phase Proteins

The function of positive APPs is regarded as important in optimization and trapping of microorganism and their products, in activating the complement system, binding cellular remnants like nuclear fractions, neutralizing enzymes, scavenging free hemoglobin and radicals, and modulating the host's immune response.

Table 1 Biological activities of selected acute phase proteins (Jain S, et al., 2011)

Acute phase protein Biological activity
Haptoglobin Binds with hemoglobin
Bacteriostatic effect
Stimulation of angiogenesis
Role in lipid metabolism/development of fatty liver in cattle
Immunomodulatory effect
Inhibition of neutrophils respiratory burst activity
C-reactive protein Complement activation and opsonization
Modulation of monocytes and macrophages, cytokine production
Binding of chromatin
Prevention of tissue migration of neutrophils
Serum amyloid A Transport of cholesterol from dying cells to hepatocytes
Inhibitory effect on fever
Inhibitory effect on the oxidative burst of neutrophilic granulocytes
Inhibitory effect on in vitro immune response
Chemotexic effect on monocytes, leukocytes, and T cells
Induction of calcium mobilization by monocytes
Inhibition of platelet activation
  • Inflammation Modulation: APPs, such as C-reactive protein (CRP) and serum amyloid A (SAA), play a role in modulating the inflammatory response. They bind to bacterial cell wall components, damaged tissue, or apoptotic cells, promoting their clearance and limiting the spread of infection or tissue damage.
  • Opsonization and Pathogen Clearance: Some APPs, including CRP and mannose-binding lectin (MBL), act as opsonins. They enhance the recognition and phagocytosis of pathogens by immune cells, such as macrophages and neutrophils, facilitating pathogen clearance.
  • Complement Activation: Certain APPs, like C-reactive protein and serum amyloid P (SAP), can activate the complement system. Complement activation leads to the recruitment and activation of immune cells, direct lysis of pathogens, and enhanced phagocytosis.
  • Tissue Repair and Remodeling: Several APPs, such as fibrinogen, haptoglobin, and alpha-1 antitrypsin, are involved in tissue repair and remodeling processes. They contribute to wound healing, extracellular matrix remodeling, and the regulation of protease activity.
  • Antioxidant Effects: Some APPs, like haptoglobin and ceruloplasmin, possess antioxidant properties. They bind and neutralize free radicals and reactive oxygen species, protecting cells and tissues from oxidative damage.
  • Iron Sequestration: APPs, including ferritin and haptoglobin, participate in iron metabolism. They can sequester iron, limiting its availability to pathogens and reducing its pro-inflammatory effects.
  • Immunomodulation: Certain APPs, such as alpha-1 antitrypsin and antithrombin III, have immunomodulatory functions. They regulate the activity of immune cells, modulate cytokine production, and contribute to immune homeostasis.

The precise functions and regulation of APPs can vary depending on the specific protein and the context of the inflammatory response. However, overall, APPs play important roles in inflammation modulation, pathogen clearance, tissue repair, and immune regulation, contributing to the body's defense mechanisms and recovery from injury or infection.

Acute Phase Protein CRP - Creative BioMart

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References:

  1. Jain S, Gautam V, Naseem S. Acute-phase proteins: As diagnostic tool. J Pharm Bioallied Sci. 2011;3(1):118-127. doi:10.4103/0975-7406.76489
  2. Gruys E, Toussaint MJ, Niewold TA, Koopmans SJ. Acute phase reaction and acute phase proteins. J Zhejiang Univ Sci B. 2005;6(11):1045-1056. doi:10.1631/jzus.2005.B1045
  3. Janciauskiene, S., Welte, T., & Mahadev, R. (2011). Acute Phase Proteins: Structure and Function Relationship. InTech. doi: 10.5772/18121
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