Characterization of mannose 6-phosphate receptors (MPRs) from opossum liver: opossum cation-independent MPR binds insulin-like growth factor-II.

Dahms, Nancy M.; Brzycki-Wessell, Mary A.; Ramanujam, Kalathur S.; Seetharam, Bellur

doi:10.1210/endo.133.2.8344189

Cited by 29 publications

(24 citation statements)

References 32 publications

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“…It is widely hypothesized that IGF2-IGF2R binding is unique to therian mammals (marsupials and placentals) due to sexual conflict in regulating paternal IGF2 during placental and embryo development (10,(18)(19)(20)(21).…”

Section: Significancementioning

confidence: 99%

“…This hypothesis of mammalian-specific function was bolstered by early studies showing that IGF2R does not effectively bind IGF2 in chicken (18,21,41), Xenopus (18), or monotremes (10), and IGF2R has lower affinity for IGF2 in marsupials compared with placental mammals (19,20). However, more sensitive assays have indicated that IGF2R-IGF2 binding occurs in chicken, trout, and garden lizards (42,65,66), which counters the claim that measurable IGF2-IGF2R binding is confined to mammals.…”

Section: Members Of Iis/tor Network Are Outliers In Evolutionary Ratementioning

confidence: 99%

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Rapid molecular evolution across amniotes of the IIS/TOR network

McGaugh

Bronikowski

Kuo

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

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The insulin/insulin-like signaling and target of rapamycin (IIS/TOR) network regulates lifespan and reproduction, as well as metabolic diseases, cancer, and aging. Despite its vital role in health, comparative analyses of IIS/TOR have been limited to invertebrates and mammals. We conducted an extensive evolutionary analysis of the IIS/TOR network across 66 amniotes with 18 newly generated transcriptomes from nonavian reptiles and additional available genomes/transcriptomes. We uncovered rapid and extensive molecular evolution between reptiles (including birds) and mammals: (i) the IIS/TOR network, including the critical nodes insulin receptor substrate (IRS) and phosphatidylinositol 3-kinase (PI3K), exhibit divergent evolutionary rates between reptiles and mammals; (ii) compared with a proxy for the rest of the genome, genes of the IIS/TOR extracellular network exhibit exceptionally fast evolutionary rates; and (iii) signatures of positive selection and coevolution of the extracellular network suggest reptile-and mammal-specific interactions between members of the network. In reptiles, positively selected sites cluster on the binding surfaces of insulin-like growth factor 1 (IGF1), IGF1 receptor (IGF1R), and insulin receptor (INSR); whereas in mammals, positively selected sites clustered on the IGF2 binding surface, suggesting that these hormone-receptor binding affinities are targets of positive selection. Further, contrary to reports that IGF2R binds IGF2 only in marsupial and placental mammals, we found positively selected sites clustered on the hormone binding surface of reptile IGF2R that suggest that IGF2R binds to IGF hormones in diverse taxa and may have evolved in reptiles. These data suggest that key IIS/TOR paralogs have sub-or neofunctionalized between mammals and reptiles and that this network may underlie fundamental life history and physiological differences between these amniote sister clades.insulin signaling | insulin growth factor | molecular evolution | rapamycin T he last 20 y has provided overwhelming support that the insulin-and insulin-like signaling/target of rapamycin (IIS/TOR) molecular network responds to stress and nutrients and underlies a wide range of physiological functions (1); cancer, metabolic syndrome, and diabetes (2); and the timing of life events (e.g., growth, maturation, reproduction, and aging) (3). The vertebrate IIS/TOR network consists of peptide hormones, binding proteins that regulate hormone bioavailability, and cell membrane receptors (hereafter, extracellular proteins of the IIS/TOR network) that induce an intracellular signaling cascade (hereafter, intracellular proteins of the IIS/TOR network) to stimulate cell proliferation, survival, and metabolism (Fig. S1). The core intracellular signal transduction genes in this network are largely conserved across deep phylogenetic time (4, 5). In contrast, genes encoding the IIS/TOR extracellular network have diverged in the vertebrate lineage (6-8) and may have variable roles among taxa (9, 10). Despite its central rol...

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Section: Significancementioning

confidence: 99%

Section: Members Of Iis/tor Network Are Outliers In Evolutionary Ratementioning

confidence: 99%

Rapid molecular evolution across amniotes of the IIS/TOR network

McGaugh

Bronikowski

Kuo

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

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“…The IGFR-2 protein is encoded by an imprinted gene that diverged relatively recently (coincident with marsupialization and the evolution of the placenta) from the mannose-6-phosphate transporter -a very old gene which can be traced phylogenetically all the way back to yeast (Morgan et al 1987, MacDonald et al 1988, Clairmont & Czech 1989, Dahms et al 1993, Yandell et al 1999, Killian et al 2001b, Whyte & Munro 2001. Despite this wealth of knowledge, we know very little about how IGFR-2 is regulated.…”

Section: Introductionmentioning

confidence: 99%

The cellular repressor of E1A-stimulated genes mediates glucocorticoid-induced loss of the type-2 IGF receptor in ileal epithelial cells

Gordon

Paxton²,

Fox³

2005

Journal of Endocrinology

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Glucocorticoids induce hypertrophy of the neonatal ileal mucosa but the molecular mechanisms behind this growth induction remain poorly understood. Ileal epithelial cells (IECs) are dependent upon IGF-II for proliferation both in vivo and in culture. The type-2 IGF receptor (IGFR-2) is a lysosomal transport protein that attenuates IGF-IIdriven growth and is highly abundant in the ileum. The cellular repressor of E1A-stimulated genes (CREG) is a secreted phosphoglycoprotein that affects cell fate via ligand binding with IGFR-2, although the mechanism by which it does so is unknown. We hypothesized that glucocorticoids might facilitate IGF-mediated hypertrophy through CREG-mediated degradation of IGFR-2. To test this hypothesis, confluent rat IECs (IEC-18) were cultured for 72 h with or without dexamethasone (DEX) and harvested for Western blot, immunocytochemistry, gene array and CREG immunoneutralization experiments.IGFR-2 and CREG immunohistochemistry were also performed in archived ileal specimens from control and DEX-exposed newborn mice and extremely premature infants to investigate in vivo and clinical relevance. DEX exposure was found to diminish IGFR-2 immunolocalization in cultured rat IECs, newborn mouse ileal mucosa and human neonatal ileal mucosa. Gene array data indicated that IGFR-2 expression was unchanged with DEX treatment, suggesting a mechanism of protein degradation. CREG immunolocalization and abundance was found to be increased by DEX and immunoneutralization of CREG resulted in the abolition of IGFR-2 degradation. We have concluded that CREG is a secreted mediator by which DEX induces degradation of IGFR-2 and speculate that this is a fundamental mechanism of mucosal growth induction.

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“…The IGF-II/CI-MPR was purified from bovine liver by phosphomannan-Sepharose affinity chromatography as described in Dahms et al (1993). Competition for binding with 125 I-hIGF-II to bIGF-II/ CI-MPR was again expressed as a percentage of the control with no added IGF-II.…”

Section: Methodsmentioning

confidence: 99%

“…Interestingly, the avian and amphibian CI-MPRs lack the binding site for IGF-II but are able to bind mannose 6-phosphate-bearing ligands (Canfield & Kornfeld 1989, Clairmont & Czech 1989. However, the CI-MPR from the opossum, a species that recently diverged from placental mammals, can bind IGF-II, albeit with a 75-fold lower affinity than the bovine receptor (Dahms et al 1993). Thus, the IGF-II binding property of the CI-MPR appears to be have been acquired later in vertebrate evolution and may be limited to mammals.…”

Section: Introductionmentioning

confidence: 99%

Kangaroo IGF-II is structurally and functionally similar to the human [Ser29]-IGF-II variant

Yandell¹,

Francis²,

Wheldrake³

et al. 1999

Journal of Endocrinology

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Kangaroo IGF-II has been purified from western grey kangaroo (Macropus fuliginosus) serum and characterised in a number of in vitro assays. In addition, the complete cDNA sequence of mature IGF-II has been obtained by reverse-transcription polymerase chain reaction. Comparison of the kangaroo IGF-II cDNA sequence with known IGF-II sequences from other species revealed that it is very similar to the human variant, [Ser 29 ]-hIGF-II. Both the variant and kangaroo IGF-II contain an insert of nine nucleotides that encode the amino acids Leu-Pro-Gly at the junction of the B and C domains of the mature protein.The deduced kangaroo IGF-II protein sequence also contains three other amino acid changes that are not observed in human IGF-II. These amino acid differences share similarities with the changes described in many of the IGF-IIs reported for non-mammalian species. Characterisation of human IGF-II, kangaroo IGF-II, chicken IGF-II and [Ser 29 ]-hIGF-II in a number of in vitro assays revealed that all four proteins are functionally very similar. No significant differences were observed in the ability of the IGF-IIs to bind to the bovine IGF-II/cationindependent mannose 6-phosphate receptor or to stimulate protein synthesis in rat L6 myoblasts. However, differences were observed in their abilities to bind to IGF-binding proteins (IGFBPs) present in human serum. Kangaroo, chicken and [Ser 29 ]-hIGF-II had lower apparent affinities for human IGFBPs than did human IGF-II. Thus, it appears that the major circulating form of IGF-II in the kangaroo and a minor form of IGF-II found in human serum are structurally and functionally very similar. This suggests that the splice site that generates both the variant and major form of human IGF-II must have evolved after the divergence of marsupials from placental mammals.

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Characterization of mannose 6-phosphate receptors (MPRs) from opossum liver: opossum cation-independent MPR binds insulin-like growth factor-II.

Cited by 29 publications

References 32 publications

Rapid molecular evolution across amniotes of the IIS/TOR network

Rapid molecular evolution across amniotes of the IIS/TOR network

The cellular repressor of E1A-stimulated genes mediates glucocorticoid-induced loss of the type-2 IGF receptor in ileal epithelial cells

Kangaroo IGF-II is structurally and functionally similar to the human [Ser29]-IGF-II variant

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