Alcohol‐related trafficking accidents
Alcohol‐related trafficking accidents
复制标题
与酒精有关的贩运事故
作者:
A. Diehl
Cell-to-cell and cell-to-stroma contacts play important roles in regulating the morphogenesis and differentiated functions of tissues. Delineation of the molecular mechanisms involved in these processes is an area of active investigation. Emerging evidence suggests that adhesion molecules (e.g., cadherins and calciumindependent adhesion molecules) on the surfaces of cells bind homophilically to similar molecules on other cells. Other transmembrane proteins (e.g., integrins) link cytoskeletal elements (e.g., talin, a-actinin) with specific constituents of the extracellular matrix (e.g., laminin, fibronectin). Cell-cell adhesion and cell-matrix adhesion trigger cytoskeletal rearrangements, which in turn modulate cellular polarity, growth and differentiated function (1). The mechanisms by which cytoskeletal rearrangements affect these latter processes remain poorly understood. However, the recent observation that profilin, a membrane-associated, actin-binding protein, also binds to inositol bis-phosphate (PIP21 and influences phospholipase C-induced hydrolysis of PIP2 to diacylglycerol suggests an intimate relationship between cell-cellhell-matrix contact, cytoskeletal elements and membrane phospholipid-initiated second messenger cascades (2-4). Cytoskeletal alterations at the site of cell-cell and cell-matrix attachments are also vital prerequisites for the development of plasma membrane domains. The separation of the plasma membrane into structurally and functionally discrete regions is vital for the function of hepatocytes and other polar epithelial cells that must accomplish directional transport to and from their luminal (canalicular) and basal (sinusoidal) surfaces. Condensation of cytoskeletal elements at the sites of cell-cell and cell-matrix attachments appears to restrict the diffusion of proteins along the membrane and limit them to specific domains. For example, enrichment of sites of cell-matrix attachment with the cytoskeletal proteins ankrin and fodrin anchors Na-K ATPase to the basal (sinusoidal) plasma membrane domain. The attachment prevents the endocytosis and subsequent intracellular degradation of this protein that typically occur when it is inserted into apical (luminal) membrane domains of certain epithelial cells (5-7). Once specific plasma membrane domains are established, other proteins are selectively targeted to particular plasma membrane domains by posttranslational modifications (8). For example, aminopeptidase N and dipeptidase IV are
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影响因子:
5.8
作者:
Casey,CA;Volentine,GD;Jankovich,CJ;Kragskow,SL;Tuma,DJ
通讯作者:
Tuma,DJ
影响因子:
15.9
作者:
BISSELL, DM;ARENSON, DM;ROLL, FJ
通讯作者:
ROLL, FJ
影响因子:
56.9
作者:
RODRIGUEZBOULAN, E;NELSON, WJ
通讯作者:
NELSON, WJ
影响因子:
2.8
作者:
HOEK, JB;RUBIN, E
通讯作者:
RUBIN, E
DOI:
--
发表时间:
1990
期刊:
Molecular biology & medicine
影响因子:
--
作者:
Bissell,DM;Caron,JM;Babiss,LE;Friedman,JM
通讯作者:
Friedman,JM