Insulin binding sites on the nuclear envelope: potential relationship to mRNA metabolism

Goldfine, Ira D.; Purrello, Francesco; Clawson, Gary A.; Vigneri, Riccardo

doi:10.1002/jcb.240200104

Cited by 28 publications

(6 citation statements)

References 47 publications

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“…The previously observed inhibition of pituitary GH mRNA levels induced by IGF-I (10) may have been due to other posttranscriptional events, including an increase in GH mRNA degradation, processing, or transport (34). The half-life of GH mRNA in GH cells has been reported to range from 40 to 56 h (30), while in other studies a shorter half-life has been reported (31).…”

Section: Methodsmentioning

confidence: 91%

Insulinlike growth factor I regulation of growth hormone gene transcription in primary rat pituitary cells.

Yamashita¹,

Melmed²

1987

J. Clin. Invest.

136

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Section: Methodsmentioning

confidence: 91%

Insulinlike growth factor I regulation of growth hormone gene transcription in primary rat pituitary cells.

Yamashita¹,

Melmed²

1987

J. Clin. Invest.

136

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“…More controversially, studies going back several decades have suggested that IR are found in cell nuclei (Goldfine et al, 1982; Podlecki et al, 1987; Smith et al, 1997). There is also evidence for insulin/IGF-1 induced nuclear localization of IRSs (Sun et al, 2003; Wu et al, 2003; Chen et al, 2005).…”

Section: Receptor Traffickingmentioning

confidence: 99%

Molecular Basis of Signaling Specificity of Insulin and IGF Receptors: Neglected Corners and Recent Advances

2012

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Insulin and insulin-like growth factor (IGF) receptors utilize common phosphoinositide 3-kinase/Akt and Ras/extracellular signal-regulated kinase signaling pathways to mediate a broad spectrum of “metabolic” and “mitogenic” responses. Specificity of insulin and IGF action in vivo must in part reflect expression of receptors and responsive pathways in different tissues but it is widely assumed that it is also determined by the ligand binding and signaling mechanisms of the receptors. This review focuses on receptor-proximal events in insulin/IGF signaling and examines their contribution to specificity of downstream responses. Insulin and IGF receptors may differ subtly in the efficiency with which they recruit their major substrates (IRS-1 and IRS-2 and Shc) and this could influence effectiveness of signaling to “metabolic” and “mitogenic” responses. Other substrates (Grb2-associated binder, downstream of kinases, SH2Bs, Crk), scaffolds (RACK1, β-arrestins, cytohesins), and pathways (non-receptor tyrosine kinases, phosphoinositide kinases, reactive oxygen species) have been less widely studied. Some of these components appear to be specifically involved in “metabolic” or “mitogenic” signaling but it has not been shown that this reflects receptor-preferential interaction. Very few receptor-specific interactions have been characterized, and their roles in signaling are unclear. Signaling specificity might also be imparted by differences in intracellular trafficking or feedback regulation of receptors, but few studies have directly addressed this possibility. Although published data are not wholly conclusive, no evidence has yet emerged for signaling mechanisms that are specifically engaged by insulin receptors but not IGF receptors or vice versa, and there is only limited evidence for differential activation of signaling mechanisms that are common to both receptors. Cellular context, rather than intrinsic receptor activity, therefore appears to be the major determinant of whether responses to insulin and IGFs are perceived as “metabolic” or “mitogenic.”

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“…Similarly, intracellular insulin can stimulate nuclear membrane receptors and result in the generation of second messengers. 17,28 Intracellular angiotensin II has also been shown to interact with intracellular receptors and generate second messengers. 34,35 These observations suggest that in some cases, the intracellular action of a hormone can modulate or amplify a signal at the cell surface, because the intracellular hormone is seen to release the same (or similar) second messengers as binding of hormone to cell-surface receptors.…”

mentioning

confidence: 99%

“…sengers, eg, insulin 17,27,28 ; (4) binding to nucleolar components, eg, FGF, PTHrP, angiogenin 13,18,20 ; and (5) binding to chromatin, eg, angiotensin II, PTHrP, nerve growth factor (NGF), EGF, and PDGF. 3,12,18,21,29 Given these observations, it appears important to determine the actions of intracellular hormones, whether they are synthesized intracellularly or internalized.…”

mentioning

confidence: 99%

The Nature of Intracrine Peptide Hormone Action

Ré

1999

Hypertension

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Abstract-Current theory holds that peptide hormone action results from hormone binding to cell-surface receptors, with the generation of intracellular second messengers. However, a growing body of evidence suggests that intracellular peptide hormone, either internalized or synthesized in situ, can exert physiologically relevant effects. These effects are diverse and poorly understood. I propose that such intracrine action can serve to modulate cellular function over time and thereby play a role in biological memory of various sorts, in the maintenance of hormonal responsiveness, and in cellular differentiation. (Hypertension. 1999;34:534-538.)Key Words: intracrine Ⅲ peptides Ⅲ nucleus Ⅲ memory Ⅲ differentiation O ur laboratory introduced the term "intracrine" in 1984 to describe the actions of a peptide hormone within its cell of synthesis. 1 This concept was later explicitly expanded to include the intracellular action of internalized peptide hormones. 2 These formulations were based on our studies of the actions of intracellular angiotensin II. [1][2][3][4][5][6][7][8][9][10][11] Subsequently, evidence supporting intracrine action has been developed for a large number of peptide hormones and factors (for example, insulin, growth hormone, prolactin, nerve growth factor, interferon-␥, fibroblast growth factor [FGF], Tat protein, platelet-derived growth factor [PDGF], epidermal growth factor [EGF], parathyroid hormone-related protein [PTHrP], endogenous opiates, angiogenin, among others). [12][13][14][15][16][17][18][19][20][21][22][23][24] Although the intracellular actions of steroid hormones and their receptors have been studied intensively, the implications, if any, of intracrine peptide hormone action for normal or abnormal cellular physiology remain unclear. 23 Indeed, the default view appears to be that if such intracellular binding/action of peptide hormones exists at all, it represents a vestigial or unimportant aspect of biology.This view, however, is beginning to change as evidence mounts for the binding of a large number of peptide hormones to nuclei and other intracellular structures and for biological change associated with that binding. It would therefore appear useful at this time to reconsider the possible implications of intracrine peptide action.By way of review, one can note that peptide hormones have been reported to act intracellularly in the following ways: (1) binding to receptors in the endoplasmic reticulum soon after synthesis and generating second messengers, eg, PDGF-B/v-sis 24,25 ; (2) binding to intravesicular receptors after internalization, with subsequent generation of second messengers, eg, EGF in the absence of its membraneanchoring domain 26 ; (3) binding to receptors on the nuclear membrane, with the subsequent generation of second messengers, eg, insulin 17,27,28 ; (4) binding to nucleolar components, eg, FGF, PTHrP, angiogenin 13,18,20 ; and (5) binding to chromatin, eg, angiotensin II, PTHrP, nerve growth factor (NGF), EGF, and PDGF. 3,12,18,21,29 Given these observations,...

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Insulin binding sites on the nuclear envelope: potential relationship to mRNA metabolism

Cited by 28 publications

References 47 publications

Insulinlike growth factor I regulation of growth hormone gene transcription in primary rat pituitary cells.

Insulinlike growth factor I regulation of growth hormone gene transcription in primary rat pituitary cells.

Molecular Basis of Signaling Specificity of Insulin and IGF Receptors: Neglected Corners and Recent Advances

The Nature of Intracrine Peptide Hormone Action

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