Collectin

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Collectins are soluble pattern recognition receptors (PRRs) belonging to the superfamily of collagen containing C-type lectins.

Eight collectins have been identified including mannan-binding lectin (MBL), surfactant protein A (SP-A), surfactant protein D (SP-D), collectin liver 1 (CL-L1), collectin placenta 1 (CL-P1), conglutinin, collectin of 43 kDa (CL-43) and collectin of 46 kDa (CL-46).

These molecules have been implicated as major modulators of the innate immune system where they have a key role in the first line of defense against invading microorganisms.

Functionally, collectins are usually trimers with the number of trimeric units differing among the collectin family.

[edit] Structural domains

The collectin monomers comprise four structural domains;

  • a cysteine-rich domain at the N-terminus.
  • a collagen domain.
  • a coiled-coil neck domain .
  • a C-type lectin domain that is also called a carbohydrate recognition domain (CRD). Collectins selectively bind to specific complex carbohydrates of microbes using their CRDs.[1]

[edit] Responses

The binding of collectins to microbes causes several immune related responses.

  • They cause the formation of aggregates of the microorganisms, opsonize the microorganisms to increase their phagocytosis and some upregulate of the activity of other PRRs such as the mannose receptor.
  • Some collectins (e.g. MBL) activate of the lectin pathway of the complement system to increase membrane permeability of microorganisms and cause the destruction of that microbe.[1]

[edit] References

  1. ^ a b van de Wetering et al. Collectins: Players of the innate immune system. Eur. J. Biochem. 271, 1229-1249 (2004)
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