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Fibrinogen is made and secreted into the blood primarily by liver hepatocyte cells. Endothelium cells are also reported to make small amounts of fibrinogen, but this fibrinogen has not been fully characterized; blood platelets and their precursors, bone marrow megakaryocytes, while once thought to make fibrinogen, are now known to take up and store but not make the glycoprotein.
Fibrinogen beta chain, also known as FGB, is a gene found in humans and most other vertebrates with a similar system of blood coagulation. The protein encoded by this gene is the beta component of fibrinogen , a blood-borne glycoprotein composed of three pairs of nonidentical polypeptide chains.
The modular structure of fibronectin and its binding domains. Fibronectin is a high-molecular weight (~500-~600 kDa) [5] glycoprotein of the extracellular matrix that binds to membrane-spanning receptor proteins called integrins. [6]
Its soluble precursor, fibrinogen, was thus named by Rudolf Virchow (1821–1902), and isolated chemically by Prosper Sylvain Denis (1799–1863). Alexander Schmidt suggested that the conversion from fibrinogen to fibrin is the result of an enzymatic process, and labeled the hypothetical enzyme "thrombin" and its precursor "prothrombin".
2243 14161 Ensembl ENSG00000171560 ENSMUSG00000028001 UniProt P02671 E9PV24 RefSeq (mRNA) NM_000508 NM_021871 NM_001111048 NM_010196 RefSeq (protein) NP_000499 NP_068657 NP_001104518 NP_034326 Location (UCSC) Chr 4: 154.58 – 154.59 Mb Chr 3: 82.93 – 82.94 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Fibrinogen alpha chain is a protein that in humans is encoded by the FGA gene ...
Fibrinogen gamma chain, also known as fibrinogen gamma gene (FGG), is a human gene found on chromosome 3. [ 5 ] The protein encoded by this gene is the gamma component of fibrinogen, a blood-borne glycoprotein composed of three pairs of nonidentical polypeptide chains.
Circulating fibrinogen is a glycoprotein made of two trimers each of which is composed of three ... impaired secretion, defective calcium binding, defective ...
Fibrin is formed after thrombin cleavage of fibrinopeptide A (FPA) from fibrinogen Aalpha-chains, thus initiating fibrin polymerization. Double-stranded fibrils form through end-to-middle domain (D:E) associations, and concomitant lateral fibril associations and branching create a clot network.