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Paul D. Lampe

Researcher at Fred Hutchinson Cancer Research Center

Publications -  141
Citations -  6411

Paul D. Lampe is an academic researcher from Fred Hutchinson Cancer Research Center. The author has contributed to research in topics: Connexin & Phosphorylation. The author has an hindex of 42, co-authored 141 publications receiving 5504 citations. Previous affiliations of Paul D. Lampe include University of Washington.

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Connexin 43 is an emerging therapeutic target in ischemia/reperfusion injury, cardioprotection and neuroprotection.

TL;DR: Using knockout/knockin technology as well as pharmacological approaches, one of the connexins, namely connexin 43, has been identified to be important for cardiac and brain ischemia/reperfusion injuries aswell as protection from it.
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Connexins in Cardiovascular and Neurovascular Health and Disease: Pharmacological Implications

TL;DR: It is concluded that peptide-based investigations have raised several new opportunities for interfering with connexins and their channels that may soon allow preservation of gap junction communication, inhibition of hemichannel opening, and mitigation of inflammatory signaling.
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Cellular Interaction of Integrin α3β1 with Laminin 5 Promotes Gap Junctional Communication

TL;DR: It is suggested that adhesion of epithelial cells to laminin 5 in the basement membrane via α3β1 promotes GJIC that integrates individual cells into synchronized epiboles that integrates the individual motile cells into a synchronized colony.
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Phosphorylation at S365 is a gatekeeper event that changes the structure of Cx43 and prevents down-regulation by PKC

TL;DR: It is shown that Cx43 is phosphorylated on S365 in cultured cells and heart tissue and can serve a “gatekeeper” function that may represent a mechanism to protect cells from ischemia and phorbol ester-induced down-regulation of channel conductance.
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Key connexin 43 phosphorylation events regulate the gap junction life cycle.

TL;DR: These reagents show that phosphorylation at S364 and/or S365 is involved in forming the P1 isoform, an event that apparently regulates trafficking to or within the plasma membrane, and has begun to sort out the critical signaling pathways that regulate gap junction function.