Collectins--soluble proteins containing collagenous regions and lectin domains--and their roles in innate immunity
- PMID: 7987210
- PMCID: PMC2142914
- DOI: 10.1002/pro.5560030801
Collectins--soluble proteins containing collagenous regions and lectin domains--and their roles in innate immunity
Abstract
The collectins are a group of mammalian lectins containing collagen-like regions. They include mannan binding protein, bovine conglutinin, lung surfactant protein A, lung surfactant protein D, and a newly discovered bovine protein named collectin-43. These proteins share a very similar modular domain composition and overall 3-dimensional structure. They also appear to play similar biological roles in the preimmune defense against micro-organisms in both serum and lung surfactant. The close evolutionary relationship between the collectins is further emphasized by a common pattern of exons in their genomic structures and the presence of a gene cluster on chromosome 10 in humans that contains the genes known for the human collectins. Studies on the structure/function relationships within the collectins could provide insight into the properties of a growing number of proteins also containing collagenous regions such as C1q, the hibernation protein, the alpha- and beta-ficolins, as well as the membrane acetylcholinesterase and the macrophage scavenger receptor.
Similar articles
-
Collectins and collectin receptors in innate immunity.APMIS Suppl. 2000;100:1-59. APMIS Suppl. 2000. PMID: 11021254 Review.
-
Structure and function of collectins: humoral C-type lectins with collagenous regions.Behring Inst Mitt. 1993 Dec;(93):224-35. Behring Inst Mitt. 1993. PMID: 8172571 Review.
-
Structural aspects of collectins and receptors for collectins.Immunobiology. 1998 Aug;199(2):165-89. doi: 10.1016/S0171-2985(98)80025-9. Immunobiology. 1998. PMID: 9777404 Review.
-
The genomics of soluble proteins with collagenous domains: C1q, MBL, SP-A, SP-D, conglutinin, and CL-43.Behring Inst Mitt. 1993 Dec;(93):81-6. Behring Inst Mitt. 1993. PMID: 8172588 Review.
-
Similarity in structure between C1q and the collectins as judged by electron microscopy.Behring Inst Mitt. 1993 Dec;(93):6-16. Behring Inst Mitt. 1993. PMID: 8172586 Review.
Cited by
-
M-ficolin is expressed on monocytes and is a lectin binding to N-acetyl-D-glucosamine and mediates monocyte adhesion and phagocytosis of Escherichia coli.Immunology. 2000 Oct;101(2):225-32. doi: 10.1046/j.1365-2567.2000.00099.x. Immunology. 2000. PMID: 11012776 Free PMC article.
-
Surfactant protein A (SP-A) binds to phosphatidylserine and competes with annexin V binding on late apoptotic cells.Protein Cell. 2010 Feb;1(2):188-97. doi: 10.1007/s13238-010-0024-z. Epub 2010 Feb 6. Protein Cell. 2010. PMID: 21203987 Free PMC article.
-
The alpha-helical neck region of human lung surfactant protein D is essential for the binding of the carbohydrate recognition domains to lipopolysaccharides and phospholipids.Biochem J. 1996 Sep 1;318 ( Pt 2)(Pt 2):505-11. doi: 10.1042/bj3180505. Biochem J. 1996. PMID: 8809039 Free PMC article.
-
Collectins: Innate Immune Pattern Recognition Molecules.Adv Exp Med Biol. 2020;1204:75-127. doi: 10.1007/978-981-15-1580-4_4. Adv Exp Med Biol. 2020. PMID: 32152944 Free PMC article. Review.
-
Structure, genetics and function of the pulmonary associated surfactant proteins A and D: The extra-pulmonary role of these C type lectins.Ann Anat. 2017 May;211:184-201. doi: 10.1016/j.aanat.2017.03.002. Epub 2017 Mar 27. Ann Anat. 2017. PMID: 28351530 Free PMC article. Review.
References
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources