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Coagulin information


Coagulin
Identifiers
SymbolCoagulin
PfamPF02035
InterProIPR000275
SCOP2d1aoca_ / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Limulus polyphemus horseshoe crabs use coagulin to form gel clots

Coagulin is a gel-forming protein of hemolymph that hinders the spread of bacterial and fungal invaders by immobilizing them. It is produced in the coagulogen form before being cleaved into the active form through a serine proteinase cascade.[1][2][3] It has been most extensively studied in horseshoe crabs. It has also been produced by other organisms, such as Bacillus coagulans I4 in a plasmid location.[4] In human medicine, coagulation of coagulin is the basis of detection of bacterial endotoxin through the Limulus amebocyte lysate test for parenteral medications.

  1. ^ Srimal S, Miyata T, Kawabata S, Miyata T, Iwanaga S (August 1985). "The complete amino acid sequence of coagulogen isolated from Southeast Asian horseshoe crab, Carcinoscorpius rotundicauda". Journal of Biochemistry. 98 (2): 305–318. doi:10.1093/oxfordjournals.jbchem.a135283. PMID 3905780.
  2. ^ Miyata T, Usui K, Iwanaga S (June 1984). "The amino acid sequence of coagulogen isolated from southeast Asian horseshoe crab, Tachypleus gigas". Journal of Biochemistry. 95 (6): 1793–1801. doi:10.1093/oxfordjournals.jbchem.a134792. PMID 6469947.
  3. ^ Loof TG, Mörgelin M, Johansson L, Oehmcke S, Olin AI, Dickneite G, et al. (September 2011). "Coagulation, an ancestral serine protease cascade, exerts a novel function in early immune defense". Blood. 118 (9): 2589–2598. doi:10.1182/blood-2011-02-337568. PMID 21613262. S2CID 16041445.
  4. ^ Hyronimus B, Le Marrec C, Urdaci MC (July 1998). "Coagulin, a bacteriocin-like inhibitory substance produced by Bacillus coagulans I4". Journal of Applied Microbiology. 85 (1): 42–50. doi:10.1046/j.1365-2672.1998.00466.x. PMID 9721655. S2CID 27449682.

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