June 1, 1997Endocrinology

Insulin Stimulates the Phosphorylation of the 66- and 52-Kilodalton Shc Isoforms by Distinct Pathways1

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Population

Chinese hamster ovary/IR cells and 3T3L1 adipocytes

Design

Preclinical

Authors

AKAimee W. KaoUniversity of California, San Francisco SWSteven B. WatersLos Medanos College SOShuichi OkadaHidaka Hospital

Discussion

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Implication

No immediate clinical implications; leaves open isoform-specific Shc roles in insulin signaling for future human studies.

Structured PICO

Population

Chinese hamster ovary/IR cells and 3T3L1 adipocytes

Intervention

Insulin, anisomycin, osmotic shock, dominant-interfering Ras mutant (N17Ras), MEK inhibitor (PD98059), dominant-interfering MEK mutant, MAP kinase phosphatase (MKP-1)

Outcome

Phosphorylation of 66-kDa and 52-kDa Shc isoforms (serine vs tyrosine phosphorylation)surrogate

Insulin stimulates serine phosphorylation of the 66-kDa Shc isoform via a MEK-dependent pathway, distinct from the tyrosine phosphorylation of the 52-kDa isoform.

Cite This Study

Kao et al. (1997) studied this question.

synapsesocial.com/papers/6a715ccefebe604dd70a08a3 https://doi.org/10.1210/endo.138.6.5203

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Insulin Stimulates the Phosphorylation of the 66- and 52-Kilodalton Shc Isoforms by Distinct Pathways1

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Insulin Stimulates the Phosphorylation of the 66- and 52-Kilodalton Shc Isoforms by Distinct Pathways1

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider