Acute-phase proteins

annular pentameric protein found in blood plasma whose circulating concentrations rise in response to inflammation

Fibrinogen (coagulation factor I) is a glycoprotein complex, produced in the liver, that circulates in the blood of all vertebrates. During tissue and vascular injury, it is converted enzymatically by thrombin to fibrin and then to a fibrin-based blood clot. Fibrin clots function primarily to occlude blood vessels to stop bleeding. Fibrin also binds and reduces the activity of thrombin. This activity, sometimes referred to as antithrombin I, limits clotting. Fibrin also mediates blood platelet and endothelial cell spreading, tissue fibroblast proliferation, capillary tube formation, and angiog

thumb|right|Composition of a fresh thrombus at microscopy, [[HE stain, showing nuclear debris in a background of fibrin and red blood cells.]] thumb|right|Micrograph showing fibrin (dark pink amorphous material) in a blocked [[vein surrounded by extravasated red blood cells (right of image). An artery (left of image) and the amnion (far left of image) is also seen. Placenta in a case of fetal thrombotic vasculopathy. H&E stain.]]

Ferritin is a universal intracellular and extracellular protein that stores iron and releases it in a controlled fashion. The protein is produced by almost all living organisms, including archaea, bacteria, algae, higher plants, and animals. It is the primary intracellular iron-storage protein in both prokaryotes and eukaryotes, keeping iron in a soluble and non-toxic form. In humans, it acts as a buffer against iron deficiency and iron overload.

thumb|360px|alt=Schematic diagram of the blood coagulation and protein C pathways. In the blood coagulation pathway, thrombin acts to convert factor XI to XIa, VIII to VIIIa V to Va, fibrinogen to fibrin. In addition, thrombin promotes platelet activation and aggregation via activation of protease-activated receptors on the cell membrane of the platelet. Thrombin also cross over into the protein C pathway by converting protein C into APC. APC in turn converts factor V into Vi, and VIIIa into VIIIi. Finally APC activates PAR-1 and EPCR.|Role of thrombin in the blood coagulation cascade

mammalian protein found in Homo sapiens

Ceruloplasmin (or caeruloplasmin) is a ferroxidase enzyme that in humans is encoded by the CP gene.

mammalian protein found in Homo sapiens

Plasmin is an important enzyme () present in blood that degrades many blood plasma proteins, including fibrin clots. The degradation of fibrin is termed fibrinolysis. In humans, the plasmin protein (in the zymogen form of plasminogen) is encoded by the PLG gene.

proteins secreted into the blood by hepatocytes in response to trauma, inflammation or disease

thumb|363x363px|Structure of human alpha-1-acid glycoprotein (AGP1) rendered in ChimeraX using PDB ID: 3KQ0 thumb|339x339px|Structure of human alpha-1-acid glycoprotein (AGP2) rendered in ChimeraX using PDB ID: 3APU Orosomucoid (ORM) or alpha-1-acid glycoprotein (α1AGp, AGP or AAG) is an acute phase protein found in plasma. Orosomucoid was discovered over 70 years ago and belongs to the lipocalin protein family. There are two isoforms of AGP, referred to as AGP1 and AGP2. It is an alpha-globulin glycoprotein and is modulated by two polymorphic genes. It is synthesized primarily in hepatocytes

protein-coding gene in the species Homo sapiens

α2-Macroglobulin (α2M) or alpha-2-macroglobulin is a large (720 KDa) plasma protein found in the blood. It is mainly produced by the liver, and also locally synthesized by macrophages, fibroblasts, and adrenocortical cells. In humans it is encoded by the A2M gene.

InterPro Family

protein-coding gene in the species Homo sapiens

protein-coding gene in the species Homo sapiens