为烈性传染病

人类是霍乱弧菌的唯一易感者

经消化道传播

病后可获得短暂免疫力

免疫力主要是SIgA的作用

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男年满55岁，女职员年满55岁

男年满60岁，女职员年满50岁

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The Ras protein is a member of a large family of small GTP-binding proteins, often called monomeric GTPases to distinguish them from the trimeric G proteins. Ras resembles the α subunit of a G protein and functions as a molecular switch in much the same way.

It cycles between two distinct conformational states—active when GTP is bound and inactive when GDP is bound. Interaction with an activating protein called Ras-GEF encourages Ras to exchange its GDP for GTP, thus switching Ras to its activated state; after a delay, Ras is switched off by a GAP called Ras-GAP, which promotes the hydrolysis of its bound GTP to GDP.

In its active state, Ras initiates a phosphorylation cascade in which a series of serine/threonine kinases phosphorylate and activate one another in sequence, like an intracellular game of dominoes. This relay system, which carries the signal from the plasma membrane to the nucleus, includes a three-kinase module called the MAP-kinase signaling module, in honor of the final enzyme in the chain, the mitogen-activated protein kinase, or MAP kinase.

In this pathway, MAP kinase is phosphorylated and activated by an enzyme called, logically enough, MAP kinase kinase. This protein is itself switched on by a MAP kinase kinase kinase (which is activated by Ras). At the end of the MAP-kinase cascade, MAP kinase phosphorylates various effector proteins, including certain transcription regulators, altering their ability to control gene transcription. The resulting change in the pattern of gene expression may stimulate cell proliferation, promote cell survival, or induce cell differentiation: the precise outcome will depend on which other genes are active in the cell and what other signals the cell receives.

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An extracellular survival signal, such as IGF, activates an RTK, which recruits and activates PI 3-kinase. PI 3-kinase then phosphorylates an inositol phospholipid that is embedded in the cytosolic side of the plasma membrane.

The resulting phosphorylated inositol phospholipid attracts intracellular signaling proteins that have a special domain that recognizes it.

One of these signaling proteins, Akt, is a protein kinase that is activated at the membrane by phosphorylation mediated by two other protein kinases (here called protein kinases 1 and 2); protein kinase 1 is also recruited by the phosphorylated lipid docking sites.

Once activated, Akt is released from the plasma membrane and phosphorylates various downstream proteins on specific serines and threonines.

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