| First Author | Nguyen AD | Year | 2013 |
| Journal | J Biol Chem | Volume | 288 |
| Issue | 12 | Pages | 8627-35 |
| PubMed ID | 23364791 | Mgi Jnum | J:203514 |
| Mgi Id | MGI:5527141 | Doi | 10.1074/jbc.M112.441949 |
| Citation | Nguyen AD, et al. (2013) Secreted progranulin is a homodimer and is not a component of high density lipoproteins (HDL). J Biol Chem 288(12):8627-35 |
| abstractText | Progranulin is a secreted glycoprotein, and the GRN gene is mutated in some cases of frontotemporal dementia. Progranulin has also been implicated in cell growth, wound healing, inflammation, and cancer. We investigated the molecular nature of secreted progranulin and provide evidence that progranulin exists as a homodimer. Although recombinant progranulin has a molecular mass of approximately 85 kDa by SDS-PAGE, it elutes in fractions corresponding to approximately 170-180 kDa by gel-filtration chromatography. Additionally, recombinant progranulin can be intermolecularly cross-linked, yielding a complex corresponding to a dimer ( approximately 180 kDa), and progranulins containing different epitope tags physically interact. In plasma, progranulin similarly forms complexes of approximately 180-190 kDa. Although progranulin partially co-fractionated with high density lipoproteins (HDL) by gel-filtration chromatography, we found no evidence that progranulin in mouse or human plasma is a component of HDL either by ultracentrifugation or by lipid binding assays. We conclude that circulating progranulin exists as a dimer and is not likely a component of HDL. |
