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Home > Mathematics and Science Textbooks > Biology, life sciences > Structural and Functional Studies of Pro-Nerve Growth Factor
Structural and Functional Studies of Pro-Nerve Growth Factor

Structural and Functional Studies of Pro-Nerve Growth Factor


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About the Book

Precursor of NGF (proNGF) mediates cell death in several neuronal cell types by forming an apoptotic complex with NGF receptor p75 and a new pro-neurotrophin receptor---sortilin. Processing at three dibasic sites in the pro domain of proNGF leads to mature NGF. Site 3 (nearest to mature NGF) is at the junction of the pro and mature domains and has been identified as the site important for processing of proNGF to mature NGF. In this study, we determined that mutating site 3 renders proNGF only partially resistant to proteases and results in a heterogeneous protein composition consisting of proNGF, mature NGF and intermediately processed proNGF molecules. Mutating the other two sites, in addition to site 3, resulted in essentially all proNGF and hence a more suitable molecule for cellular and biophysical studies. Using this stable proNGF, proNGF123, we investigated the interactions of proNGF with TrkA, p75, and sortilin receptors' extracellular domains (ECDs). Using SPR and co-immunoprecipitation of purified receptor ECDs with ligands, we found that proNGF-TrkA interaction is 30 fold weaker than NGF-TrkA interaction even though the dissociation of proNGF from TrkA is slower than NGF. The NGF-p75 and NGF-sortilin interactions are weaker than the proNGF interactions with p75 and sortilin. Further, we also found that proNGF is capable of reducing NGF induced TrkA phosphorylation and even more drastically the downstream p42/p44 MAP kinase activation. We conclude that proNGF may be able to cause this reduction in pro-survival signals by additive effects of two mechanisms---(1) direct binding to TrkA and (2) sequestering p75 from augmenting TrkA mediated survival signals. Hence, this study led to generation of a stable proNGF molecule and evaluated proNGF-receptor interaction kinetics and the mechanism of proNGF induced apoptosis in finer detail.


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Product Details
  • ISBN-13: 9781243454645
  • Publisher: Proquest, Umi Dissertation Publishing
  • Publisher Imprint: Proquest, Umi Dissertation Publishing
  • Height: 254 mm
  • Weight: 213 gr
  • ISBN-10: 1243454644
  • Publisher Date: 01 Sep 2011
  • Binding: Paperback
  • Spine Width: 6 mm
  • Width: 203 mm


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