Akt1 induces extracellular matrix invasion and matrix metalloproteinase-2 activity in mouse mammary epithelial cells.

No abstract is available for this paper.

• Publication year

  2001

• Venue

  Cancer Research

• Publication date

  2001-10-15

• Fields of study

  Biology, Medicine

• Identifiers
  PMID 11606407
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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• Role of AKT1 in 17beta-estradiol- and insulin-like growth factor I (IGF-I)-dependent proliferation and prevention of apoptosis in MCF-7 breast carcinoma cells.

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• PDK1 acquires PDK2 activity in the presence of a synthetic peptide derived from the carboxyl terminus of PRK2.

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• Protein kinase C-α overexpression stimulates Akt activity and suppresses apoptosis induced by interleukin 3 withdrawal

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• CREB Is a Regulatory Target for the Protein Kinase Akt/PKB*

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• Localization of matrix metalloproteinase MMP-2 to the surface of invasive cells by interaction with integrin alpha v beta 3.

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• The proteins encoded by c-akt and v-akt differ in post-translational modification, subcellular localization and oncogenic potential.

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• Binding and localization of M(r) 72,000 matrix metalloproteinase at cell surface invadopodia.

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