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Structural basis of the function of endothelin receptor (1999)

Masaki, Tomoh ; Ninomiya, Haruaki ; Sakamoto, Aiji ; [et al.]

Springer

Molecular and cellular biochemistry 190 (1999), S. 153-156

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ISSN: 1573-4919

Keywords: G-protein ; vasoconstriction ; ligand selectivity

Source: Springer Online Journal Archives 1860-2000

Topics: Biology , Chemistry and Pharmacology , Medicine

Notes: Abstract Endothelin receptor is a good model for analysis of the function of heptahelical G-protein coupled receptor. In ligand binding to the heptahelical receptor, the receptor has two functions, i.e. ‘message’ and ‘address’ functions. Each function has been assigned to different domain of the receptor. A different part of the ligand structure also corresponds to each domain of the receptor. Classically, classification of receptor has been done according to the difference of address domain, i.e. affinity difference of the receptor. However, present results predict that the classification of receptor is also possible according to the message domain. After stimulation of ET receptor by a ligand, the receptor transmits a signal to G-protein. Several kinds of G-proteins can possibly be activated. Different structural domains of the receptor are assigned to the coupling of the different Gα-protein. Activated G-protein transmits the message to effector. Each Gα-protein acts on different target molecules, resulting in different responses. However, the activation of each Gα-protein presumably depends on its intracellular level. Even if the same receptor is activated with the same ligand, resulting final response is different from cell to cell. Therefore, classification of receptor according to the function of the receptor is difficult.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1023/A:1006986914326

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Developmental organization of the intestinal brush-border cytoskeleton (1988)

Takemura, Reiko ; Masaki, Tomoh ; Hirokawa, Nobutaka

New York, NY : Wiley-Blackwell

Cell Motility and the Cytoskeleton 9 (1988), S. 299-311

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ISSN: 0886-1544

Keywords: myosin ; fodrin ; TW 260/240 ; terminal web ; Life and Medical Sciences ; Cell & Developmental Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Medicine

Notes: At the terminal web of the chicken intestinal epithelial cell, the actin bundles are cross-linked by a fine filamentous network of actin-associated cross-linkers. Myosin, fodrin, and TW 260/240 have been identified as major components of the cross-linkers. We studied the development of the cross-linkers by quick-freeze, deep-etch electron microscopy, and the expression of cross-linker proteins (myosin, fodrin 240, and TW 260) by immunofluorescence and immunoblotting analysis during the embryogenesis. Microvilli start to form at 5-7 days, and the rootlets begin to elongate at 10 days. At an early stage of the development of the terminal web (13 days), fodrin 240 and a small amount of myosin are expressed, and a few actin-associated cross-linkers are present between the rootlets. However, TW 260 is not expressed at this stage. At an intermediate stage (19 days), the amount of myosin increases, and TW 260 begins to be expressed. The number of cross-linkers associated with the unit length of the rootlets is 24/μm. At the final stage of the terminal web formation (2 days after hatching), the amount of fodrin 240, myosin, and TW 260 is similar to the adult level, and the number of the actin-associated cross-linkers per unit length of the rootlet is 27/μm (∼85% of the adult). These results suggest that the synthesis of cross-linker proteins may be intricately regulated to achieve the desired density of cross-linkages at each developmental stage: at early and intermediate stages, sufficient and not an excess of cross-linkages are formed; and at a final stage, a higher complexity of cross-linkages is achieved. In addition, there is a differential expression of the components of the actin-associated cross-linkers: myosin and fodrin could be early components of the cross-linkers involved in the basic stabilization of the terminal web structure, whereas TW 260/240 becomes incorporated later, possibly involved in the stabilization preparatory to the rapid elongation of microvilli, which occurs after the formation of the terminal web.

Additional Material: 12 Ill.