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The Golgi apparatus (/ ˈ ɡ ɒ l dʒ i /), also known as the Golgi complex, Golgi body, or simply the Golgi, is an organelle found in most eukaryotic cells. [1] Part of the endomembrane system in the cytoplasm, it packages proteins into membrane-bound vesicles inside the cell before the vesicles are sent to their destination.
Golgi cell circuit functions also seem to be regulated by metabotropic glutamate receptors. Golgi cells possess mGluR2 receptors, [12] and when these receptors are activated, an inward rectifier K current is enhanced, aiding in the Golgi cell's silencing after a period of intensive granule cell-Golgi cell transmission. [13]
It is located on the trans face of the Golgi apparatus and is made up of cisternae. The cisternae play a crucial role in the packaging, modification, and transport functions for the cell overall. The proteins and polysaccharides that get processed here within the cisterna will then be sent to their specified locations. [3]
The Golgi apparatus is used by the cell for further protein modification. The section of the Golgi apparatus that receives the vesicles from the ER is known as the cis face, and is usually near the ER. The opposite end of the Golgi apparatus is called the trans face, this is where the modified compounds leave.
The Golgi apparatus, which participates in glycosylation and transport of proteins and lipids in the secretory pathway, consists of a series of stacked cisternae (flattened membrane sacs). Interactions between the Golgi and microtubules are thought to be important for the reorganization of the Golgi after it fragments during mitosis. [ 6 ]
Golgi apparatus: The primary function of the Golgi apparatus is to process and package the macromolecules such as proteins and lipids that are synthesized by the cell. Lysosomes and peroxisomes: Lysosomes contain digestive enzymes (acid hydrolases). They digest excess or worn-out organelles, food particles, and engulfed viruses or bacteria.
The Golgi matrix is a collection of proteins involved in the structure and function of the Golgi apparatus. [1] [2] [3] The matrix was first isolated in 1994 as an amorphous collection of 12 proteins that remained associated together in the presence of detergent (which removed Golgi membranes) and 150 m M NaCl (which removed weakly associated proteins). [4]
The protein normally resides in a cell structure called the Golgi apparatus, which modifies and transports newly produced enzymes and other proteins. Here, ATP7A supplies Cu(I) to certain enzymes (e.g. peptidyl-α-monooxygenase , tyrosinase , and lysyl oxidase [ 9 ] ) that are critical for the structures and functions of brain, bone, skin, hair ...