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October, 2006
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Endoplasmic Reticulum: A system of cisternae in the Cytoplasm of many cells. In places the endoplasmic reticulum is continuous with the plasma membrane (Cell membrane) or outer membrane of the nuclear envelope. If the outer surfaces of the endoplasmic reticulum membranes are coated with ribosomes, the endoplasmic reticulum is said to be rough-surfaced (Endoplasmic reticulum, Rough); otherwise it is said to be smooth-surfaced (Endoplasmic reticulum, Smooth). (King & Stansfield, A Dictionary of Genetics, 4th ed)

Endoplasmic Reticulum

JoVE 10969

The Endoplasmic Reticulum (ER) in eukaryotic cells is a substantial network of interconnected membranes with diverse functions, from calcium storage to biomolecule synthesis. A primary component of the endomembrane system, the ER manufactures phospholipids critical for membrane function throughout the cell. Additionally, the two distinct regions of the ER specialize in the manufacture of specific lipids and proteins. The rough ER is characterized by the presence of microscopically-visible ribosomes on its surface. As a ribosome begins translation of an mRNA in the cytosol, the presence of a signal sequence directs the ribosome to the surface of the rough ER. A receptor in the membrane of the ER recognizes this sequence and facilitates the entry of the growing polypeptide into the ER lumen through a transmembrane protein complex. With the assistance of chaperones, nascent proteins fold and undergo other functional modifications, including glycosylation, disulfide bond formation, and oligomerization. Properly folded and modified proteins are then packaged into vesicles to be shipped to the Golgi apparatus and other locations in the cell. Chaperones identify improperly folded proteins and facilitate degradation in the cytosol by proteasomes. Lacking ribosomes, the smooth ER is the cellular location of lipid and steroid synthesis, cellular detoxification,

 Core: Biology

Spontaneous Formation and Rearrangement of Artificial Lipid Nanotube Networks as a Bottom-Up Model for Endoplasmic Reticulum

1Centre for Molecular Medicine Norway, Faculty of Medicine, University of Oslo, 2Department of Chemistry, Faculty of Mathematics and Natural Sciences, University of Oslo, 3Department of Chemistry and Chemical Engineering, Chalmers University of Technology

JoVE 58923


Cell Structure- Concept

JoVE 10587


Cells represent the most basic biological units of all organisms, whether it be simple, single-celled organisms like bacteria, or large, multicellular organisms like elephants and giant redwood trees. In the mid 19th century, the Cell Theory was proposed to define a cell, which states:

Every living organism is made up of one or more cells.
The cells…

 Lab Bio

Cross-bridge Cycle

JoVE 10870

As muscle contracts, the overlap between the thin and thick filaments increases, decreasing the length of the sarcomere—the contractile unit of the muscle—using energy in the form of ATP. At the molecular level, this is a cyclic, multistep process that involves binding and hydrolysis of ATP, and movement of actin by myosin.

When ATP, that is attached to the myosin head, is hydrolyzed to ADP, myosin moves into a high energy state bound to actin, creating a cross-bridge. When ADP is released, the myosin head moves to a low energy state, moving actin toward the center of the sarcomere. Binding of a new ATP molecule dissociates myosin from actin. When this ATP is hydrolyzed, the myosin head will bind to actin, this time on a portion of actin closer to the end of the sarcomere. Regulatory proteins troponin and tropomyosin, along with calcium, work together to control the myosin-actin interaction. When troponin binds to calcium, tropomyosin is moved away from the myosin-binding site on actin, allowing myosin and actin to interact and muscle contraction to occur. As a regulator of muscle contraction, calcium concentration is very closely controlled in muscle fibers. Muscle fibers are in close contact with motor neurons. Action potentials in motor neurons cause the release of the neurotransmitter acetylcholine in the vicinity of muscle fibers. This ge

 Core: Biology

Golgi Apparatus

JoVE 10970

As they leave the Endoplasmic Reticulum (ER), properly folded and assembled proteins are selectively packaged into vesicles. These vesicles are transported by microtubule-based motor proteins and fuse together to form vesicular tubular clusters, subsequently arriving at the Golgi apparatus, a eukaryotic endomembrane organelle that often has a distinctive ribbon-like appearance.

The Golgi apparatus is a major sorting and dispatch station for the products of the ER. Newly arriving vesicles enter the cis face of the Golgi—the side facing the ER—and are transported through a collection of pancake-shaped, membrane-enclosed cisternae. Each cisterna contains unique compositions of enzymes and performs specific protein modifications. As proteins progress through the cis Golgi network, some are phosphorylated and undergo removal of certain carbohydrate modifications that were added in the ER. Proteins then move through the medial cisterna, where they may be glycosylated to form glycoproteins. After modification in the trans cisterna, proteins are given tags that define their cellular destination. Depending on the molecular tags, proteins are packaged into vesicles and trafficked to particular cellular locations, including the lysosome and plasma membrane. Specific markers on the membranes of these vesicles allow them to dock

 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

Contact-dependent Signaling

JoVE 10715

Contact-dependent signaling uses specialized cytoplasmic channels between cells that allow the flow of small molecules between them. In animal cells, these channels are called gap junctions. In plants, they are known as plasmodesmata.

Gap junctions form when two hemichannels, or connexons, join; one connexon from one cell coupling to a connexon of an adjacent cell. Each cell’s connexon is formed from six proteins creating a circular channel. There are over 20 different types of these proteins, or connexins, so there is substantial variation in how they come together as connexons and as gap junctions. Connexins have four transmembrane subunits with both their N- and C-terminus endings located intracellularly. The C-terminus has multiple phosphorylation sites so it can be activated by numerous different kinases- further adding to gap junction variety. Depending on the activating kinase, and the C-terminal amino acid residues of connexins that are phosphorylated, gap junctions can be partially or fully opened. This selectively allows small molecules to flow from one cell into another. A gap junction may also exclude by electrochemical charge. The selectivity of gap junctions allows a single cell to coordinate a complex multicellular response. However, some toxic molecules, matching the size and electrochemical preference of the gap junction, can also p

 Core: Biology


JoVE 10692

Ribosomes translate genetic information encoded by messenger RNA (mRNA) into proteins. Both prokaryotic and eukaryotic cells have ribosomes. Cells that synthesize large quantities of protein—such as secretory cells in the human pancreas—can contain millions of ribosomes.

Ribosomes are composed of ribosomal RNA (rRNA) and proteins. Ribosomes are not surrounded by a membrane (i.e., despite their specific cell function, they are not an organelle). In eukaryotes, rRNA is transcribed from genes in the nucleolus—a part of the nucleus that specializes in ribosome production. Within the nucleolus, rRNA is combined with proteins that are imported from the cytoplasm. The assembly produces two subunits of a ribosome—the large and small subunits. These subunits then leave the nucleus through pores in the nuclear envelope. Each one large and small subunit bind to each other once mRNA binds to a site on the small subunit at the start of the translation process. This step forms a functional ribosome. Ribosomes may assemble in the cytosol—called free ribosomes—or while attached to the outside of the nuclear envelope or endoplasmic reticulum—called bound ribosomes. Generally, free ribosomes synthesize proteins used in the cytoplasm, while bound ribosomes synthesize proteins that are inserted into membranes, packaged into org

 Core: Biology

Eukaryotic Compartmentalization

JoVE 10689

One of the distinguishing features of eukaryotic cells is that they contain membrane-bound organelles—such as the nucleus and mitochondria—that carry out particular functions. Since biological membranes are only permeable to a small number of substances, the membrane around an organelle creates a compartment with controlled conditions inside. These microenvironments are often distinct from the environment of the surrounding cytosol and are tailored to the specific functions of the organelle. For example, lysosomes—organelles in animal cells that digest molecules and cellular debris—maintain an environment that is more acidic than the surrounding cytosol, because its enzymes require a lower pH to catalyze reactions. Similarly, pH is regulated within mitochondria, which helps them carry out their function of producing energy. Additionally, some proteins require an oxidative environment for proper folding and processing, but the cytosol is generally reductive. Therefore, these proteins are produced by ribosomes in the endoplasmic reticulum (ER), which maintains the necessary environment. Proteins are often then transported within the cell through membrane-bound vesicles. The genetic material of eukaryotic cells is compartmentalized within the nucleus, which is surrounded by a double membrane called the nuclear envelope. Sma

 Core: Biology
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