Chauhan, Anoop S and Rawat, Pooja and Malhotra, Himanshu and Sheokand, Navdeep and Kumar(1), Manoj and Patidar, Anil and Chaudhary, Surbhi and Jakhar, Priyanka and Raje, Chaaya I and Raje, Manoj (2015) Secreted multifunctional Glyceraldehyde-3-phosphate dehydrogenase sequesters lactoferrin and iron into cells via a non-canonical pathway. Scientific reports, 5. p. 18465. ISSN 2045-2322
Full text not available from this repository. (Request a copy)Abstract
Lactoferrin is a crucial nutritionally important pleiotropic molecule and iron an essential trace metal for all life. The current paradigm is that living organisms have evolved specific membrane anchored receptors along with iron carrier molecules for regulated absorption, transport, storage and mobilization of these vital nutrients. We present evidence for the existence of non-canonical pathway whereby cells actively forage these vital resources from beyond their physical boundaries, by secreting the multifunctional housekeeping enzyme Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) into the extracellular milieu. This effect's an autocrine/paracrine acquisition of target ligand into the cell. Internalization by this route is extensively favoured even by cells that express surface receptors for lactoferrin and involves urokinase plasminogen activator receptor (uPAR). We also demonstrate the operation of this phenomenon during inflammation, as an arm of the innate immune response where lactoferrin denies iron to invading microorganisms by chelating it and then itself being sequestered into surrounding host cells by GAPDH.
| Item Type: | Article |
|---|---|
| Additional Information: | Copyright of this article belongs to NPG. |
| Uncontrolled Keywords: | Glyceraldehyde-3-phosphate |
| Subjects: | Q Science > QR Microbiology |
| Depositing User: | Dr. K.P.S.Sengar |
| Date Deposited: | 29 Jan 2016 07:09 |
| Last Modified: | 01 Mar 2016 06:04 |
| URI: | http://crdd.osdd.net/open/id/eprint/1733 |
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