Magainin

The magainins are a class of antimicrobial peptides found in the African clawed frog (Xenopus laevis).^[1] They were discovered by Dr. Michael Zasloff and first reported in 1987.^[2]

Discovery

Zasloff was using the oocytes of Xenopus to study the nuclear transport and processing of tRNA. After removal of the ovaries of these frogs, He would suture the abdominal wounds and return the frogs to the aquarium he maintained in his laboratory. One day, many years into this research, he was struck by the remarkable manner in which these frogs healed. Wounds closed in the non-sterile tanks without any evidence of infection or visible inflammation. This "eureka" moment, his appreciating this "mysterious" process of healing, suggested to him that some mechanism had to exist by which these frogs fought off the microbes within the tank. He hypothesized that some form of antimicrobial agent was being expressed on the skin. Within several months these agents were isolated, chemically identified as peptides, and synthesized in the laboratory.

Their discovery represented the first example of an antimicrobial peptide produced in the skin of an animal, and complemented prior studies by Hans Boman of Sweden in the Cecropia moth, and Robert Lehrer (US) in rabbit white blood cells (defensins), supporting the widespread existence of antimicrobial peptides throughout nature. Thousands of antimicrobial peptides, similar to magainin, have been found throughout the plant and animal kingdoms. Many exhibit broad-spectrum antimicrobial activity, and can inhibit growth of numerous species of bacteria and fungi, as well as induce osmotic lysis of protozoa. These antimicrobial peptides are components of the "innate immune system" of animals and provide an important first line of antimicrobial defense.

An expert review of antimicrobial peptides, covering their diversity and mechanism of action, has been published.^[3]

References

↑ Magainins at the US National Library of Medicine Medical Subject Headings (MeSH)
↑ Zasloff M (1987). "Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor". Proc. Natl. Acad. Sci. USA. 84 (15): 5449–5453. doi:10.1073/pnas.84.15.5449. PMC 298875. PMID 3299384.
↑ Zasloff, Michael (2002). "Antimicrobial peptides of multicellular organisms". Nature. 415 (6870): 389–395. doi:10.1038/415389a. PMID 11807545.

Protein: cell membrane proteins (other than Cell surface receptor, enzymes, and cytoskeleton)

Arrestin	SAG ARRB1 ARRB2 ARR3

Membrane-spanning 4A	MS4A1 MS4A2 MS4A3 MS4A4A MS4A4E MS4A5 MS4A6A MS4A6E MS4A7 MS4A8B MS4A9 MS4A10 MS4A12 MS4A13 MS4A14 MS4A15 MS4A18

Myelin	Myelin basic protein PMP2 Myelin proteolipid protein PLP1 Myelin oligodendrocyte glycoprotein Myelin-associated glycoprotein Myelin protein zero

Pulmonary surfactant	Pulmonary surfactant-associated protein B Pulmonary surfactant-associated protein C

Tetraspanin	TSPAN1 TSPAN2 TSPAN3 TSPAN4 TSPAN5 TSPAN6 TSPAN7 TSPAN8 TSPAN9 TSPAN10 TSPAN11 TSPAN12 TSPAN13 TSPAN14 TSPAN15 TSPAN16 TSPAN17 TSPAN18 TSPAN19 TSPAN20 TSPAN21 TSPAN22 TSPAN23 TSPAN24 TSPAN25 TSPAN26 TSPAN27 TSPAN28 TSPAN29 TSPAN30 TSPAN31 TSPAN32 TSPAN33 TSPAN34

Other/ungrouped	Calnexin LDL-receptor-related protein-associated protein Neurofibromin 2 Presenilin PSEN1 PSEN2 HFE Phospholipid transfer proteins Dysferlin STRC OTOF

see also other cell membrane protein disorders

Pore-forming toxins (TC 1C)

Antimicrobial cationic peptides	Cathelicidin Defensin Dermcidin Histatin (HTN1, HTN3)

Other, human	Perforin

Other, nonhuman	Cecropin Diphtheria toxin Dermaseptin Magainin Melittin Nisin Pneumolysin

This article is issued from Wikipedia - version of the 11/22/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.