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Cyclic AMP: An adenine nucleotide containing one phosphate group which is esterified to both the 3'- and 5'-positions of the sugar moiety. It is a second messenger and a key intracellular regulator, functioning as a mediator of activity for a number of hormones, including epinephrine, glucagon, and ACTH.

Intracellular Signaling Cascades

JoVE 10721

Intracellular signaling cascades amplify a signal originating extracellularly and directs it to its intended intracellular target resulting in transcription, translation, protein modifications, enzyme activation, cellular metabolism, mitosis, and/or apoptosis.

The most basic of signaling cascades involves the activation of second messengers and the release of kinases. Kinases activate or deactivate proteins and enzymes by adding a phosphate group to them. Phosphatases remove phosphate groups resulting in the deactivation or reactivation of proteins. The cyclic AMP (cAMP) pathway is named for its second messenger, cAMP. This pathway is most often initiated when a ligand binds to a G-coupled protein receptor. The G-protein decouples from the receptor and triggers adenylate cyclase to synthesize cAMP from ATP. For each ligand-receptor interaction, multiple cAMP molecules are generated—amplifying the signal. cAMP activates protein kinase A (PKA). PKA is a tetramer molecule with two regulatory subunits and two active subunits. When four cAMP molecules interact with a PKA molecule, it releases the two active subunits. These PKA subunits phosphorylate target proteins and enzymes. In the case of gene expression, PKA activates CREB, a transcription factor in the nucleus. The steps that precede the intracellular signaling cascade that is the lig

 Core: Biology

What are Second Messengers?

JoVE 10720

Because many receptor binding ligands are hydrophilic, they do not cross the cell membrane and thus their message must be relayed to a second messenger on the inside. There are several second messenger pathways, each with their own way of relaying information. G-protein coupled receptors can activate both phosphoinositol and cyclic AMP (cAMP) second messenger pathways. The phosphoinositol path is active when the receptor induces phospholipase C to hydrolyze the phospholipid, phosphatidylinositol biphosphate (PIP2), into two second messengers: diacylglycerol (DAG) and inositol triphosphate (IP3). DAG remains near the cell membrane and activates protein kinase C (PKC). IP3 translocates to the endoplasmic reticulum (ER) and becomes the opening ligand for calcium ion channels on the ER membrane- releasing calcium into the cytoplasm. In the cAMP pathway, the activated receptor induces adenylate cyclase to produce multiple copies of cAMP from nearby adenosine triphosphate (ATP) molecules. cAMP can stimulate protein kinase A (PKA), open calcium ion channels, and initiate the enzyme- Exchange-protein activated by cAMP (Epac). Similar to cAMP, is cyclic guanosine monophosphate (cGMP). cGMP is synthesized from guanosine triphosphate (GTP) molecules when guanylyl cyclase is activated. As a second messenger, cGMP induces protein kinase G

 Core: Biology

Operons

JoVE 10984

Prokaryotes can control gene expression through operons—DNA sequences consisting of regulatory elements and clustered, functionally related protein-coding genes. Operons use a single promoter sequence to initiate transcription of a gene cluster (i.e., a group of structural genes) into a single mRNA molecule. The terminator sequence ends transcription. An operator sequence, located between the promoter and structural genes, prohibits the operon’s transcriptional activity if bound by a repressor protein. Altogether, the promoter, operator, structural genes, and terminator form the core of an operon. Operons are usually either inducible or repressible. Inducible operons, such as the bacterial lac operon, are normally “off” but will turn “on” in the presence of a small molecule called an inducer (e.g., allolactose). When glucose is absent, but lactose is present, allolactose binds and inactivates the lac operon repressor—allowing the operon to generate enzymes responsible for lactose metabolism. Repressible operons, such as the bacterial trp operon, are usually “on” but will turn “off” in the presence of a small molecule called a corepressor (e.g., tryptophan). When tryptophan—an essential amino acid—is abundant, tryptophan binds and activates the

 Core: Biology

Endocrine Signaling

JoVE 10719

Endocrine cells produce hormones to communicate with remote target cells found in other organs. The hormone reaches these distant areas using the circulatory system. This exposes the whole organism to the hormone but only those cells expressing hormone receptors or target cells are affected. Thus, endocrine signaling induces slow responses from its target cells but these effects also last longer. There are two types of endocrine receptors: cell surface receptors and intracellular receptors. Cell surface receptors work similarly to other membrane bound receptors. Hormones, the ligand, bind to a hormone specific G-protein coupled receptor. This initiates conformational changes in the receptor, releasing a subunit of the G-protein. The protein activates second messengers which internalize the message by triggering signaling cascades and transcription factors. Many hormones work through cell surface receptors, including epinephrine, norepinephrine, insulin, prostaglandins, prolactin, and growth hormones. Steroid hormones, like testosterone, estrogen, and progesterone, transmit signals using intracellular receptors. These hormones are small hydrophobic molecules so they move directly past the outer cell membrane. Once inside, and if that cell is a target cell, the hormone binds to its receptor. Binding creates a conformational change in the receptor

 Core: Biology

Types of Hormones

JoVE 10988

Hormones can be classified into three main types based on their chemical structures: steroids, peptides, and amines. Their actions are mediated by the specific receptors they bind to on target cells.

Steroid hormones are derived from cholesterol and are lipophilic in nature. This allows them to readily traverse the lipid-rich cell membrane to bind to their intracellular receptors in the cytoplasm or nucleus. Once bound, the cytoplasmic hormone-receptor complex translocates to the nucleus. Here, it binds to regulatory sequences on the DNA to alter gene expression. Peptide hormones are made up of chains of amino acids and are hydrophilic. Hence, they are unable to diffuse across the cell membrane. Instead, they bind to extracellular receptors present on the surface of target cells. Such binding triggers a series of signaling reactions within the cell to ultimately carry out the specific functions of the hormone. Amine hormones are derived from a single amino acid, either tyrosine or tryptophan. This class of hormones is unique because they share their mechanism of action with both steroid as well as peptide hormones. For example, although epinephrine and thyroxine are both derived from the amino acid tyrosine, they mediate their effects through diverse mechanisms. Epinephrine binds to G-protein coupled receptors present on the surface of the plasma

 Core: Biology

An Introduction to Cellular and Molecular Neuroscience

JoVE 5213

Cellular and molecular neuroscience is one of the newest and fastest growing subdisciplines in neuroscience. By investigating the influences of genes, signaling molecules, and cellular morphology, researchers in this field uncover crucial insights into normal brain development and function, as well as the root causes of many pathological conditions.


 Neuroscience

Examination of Rapid Dopamine Dynamics with Fast Scan Cyclic Voltammetry During Intra-oral Tastant Administration in Awake Rats

1Interdepartmental Neuroscience Program, Yale University, 2Department of Biotechnical and Clinical Laboratory Sciences, School of Medicine and Biomedical Sciences, University at Buffalo, 3Department of Psychiatry, Yale School of Medicine, 4Department of Cellular and Molecular Physiology, Yale School of Medicine

JoVE 52468

 Behavior
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