Reptilian MPR 300 is also the IGF-IIR

Cloning, sequencing and functional characterization of the IGF-II binding domain

Yadavalli Sivaramakrishna, Praveen kumar Amancha, Nadimpalli Siva Kumar

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

The mammalian cation-independent mannose 6-phosphate/insulin-like growth factor (IGF)-II receptor binds IGF-II with high affinity. Ligands transported by the MPR 300/IGF-IIR include IGF-II and mannose 6-phosphate-modified proteins. By targeting IGF-II to lysosomal degradation, it plays a key role in the maintenance of correct IGF-II levels in the circulation and in target tissues. Although, from our studies we found homologous receptor in calotes but its functional significance was not known. We present here the first report on the calotes MPR 300/IGF-IIR binds IGF-II with Kd of 12.02 nM; these findings provide new and strong evidence that MPR 300/IGF-IIR in Calotes versicolor binds IGFII with high affinity.

Original languageEnglish (US)
Pages (from-to)435-440
Number of pages6
JournalInternational Journal of Biological Macromolecules
Volume44
Issue number5
DOIs
StatePublished - Jun 1 2009

Fingerprint

Insulin-Like Growth Factor II
Cloning
Somatomedins
Organism Cloning
Phosphates
IGF Type 2 Receptor
Cations
Maintenance
Tissue
Ligands
Degradation

Keywords

  • Cation-independent mannose 6-phosphate receptor
  • Evolution
  • IGF-II binding
  • M6P/IGF-II receptor
  • Reptiles (calotes)

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Cite this

Reptilian MPR 300 is also the IGF-IIR : Cloning, sequencing and functional characterization of the IGF-II binding domain. / Sivaramakrishna, Yadavalli; Amancha, Praveen kumar; Siva Kumar, Nadimpalli.

In: International Journal of Biological Macromolecules, Vol. 44, No. 5, 01.06.2009, p. 435-440.

Research output: Contribution to journalArticle

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