Oct 24, 2024 · A C3 complement blood test gives your healthcare provider information about your immune system. It shows how parts of your immune system are responding to harmful …

It catalyzes the proteolytic cleavage of C3 into C3a and C3b, generated during activation through the classical pathway as well as the lectin pathway. C3a is an anaphylotoxin and the precursor of some cytokines such as ASP, and C3b serves as an opsonizing agent.

Jan 15, 2021 · C3a is used as an inflammatory marker. High levels indicate specific immune- or inflammation-related health problems. C3a levels will be high in Lyme disease but remain low in “mold illnesses”. Keep reading to learn more about high and low C3a levels, their causes and health effects. What is C3a?

C3a is a 77 residue anaphylatoxin that binds to the C3a receptor (C3aR), a class A G protein-coupled receptor. It plays a large role in the immune response. C3a molecules induce responses through the GPCR C3a receptor.

C3 convertase can be used to refer to the form produced in the alternative pathway (C3bBb) or the classical and lectin pathways (C4bC2b, formerly C4b2a). Once formed, both C3 convertases will catalyze the proteolytic cleavage of C3 into C3a and C3b (hence the name "C3-convertase").

Apr 15, 2015 · The complement activation product C3a is often described as a proinflammatory mediator, alongside its downstream cousin, C5a. However, emerging studies show that C3a has several anti-inflammatory facets in vivo.

Learn how Complement Levels (C3, C4) tests diagnose autoimmune diseases, monitor immune health, and uncover causes of low complement levels.

From an evolutionary standpoint, the emerging roles of C3 and C3-derived effectors (e.g. C3a) in early vertebrate development, as exemplified by elegant studies of tissue morphogenesis and patterning in both amphibian and mammalian embryogenesis, might reflect a primordial and species-transcending function of C3 that has been conserved ...

Although the mature native C3 protein consists of 13 distinct structural domains (Fig. 1A), a series of proteolytic reactions leads to removal of either small peptide segments (e.g. C3f) or entire domains (e.g. C3a) themselves.

Bound C3b and C3d possess stable sites that are capable of binding to specific receptors present on a limited variety of cells. We propose that all known physiologically occurring fragments of C3 arise by enzymatic cleavage of the alpha-chain: C3a, C3b, C3c, and C3d.