Actin Filament Organization of Foot Processes in Rat Podocytes

Journal of Histochemistry and Cytochemistry - Tập 51 Số 12 - Trang 1589-1600 - 2003
Koichiro Ichimura1, Hidetake Kurihara1, Tatsuo Sakai1
1Department of Anatomy, Juntendo University School of Medicine, Tokyo, Japan

Tóm tắt

The foot processes of podocytes possess abundant microfilaments and modulate glomerular filtration. We investigated the actin filament organization of foot processes in adult rat podocytes and the formation of the actin cytoskeletal system of immature podocytes during glomerulogenesis. Electron microscopy revealed two populations of actin cytoskeletons in foot processes of adult podocytes. One is the actin bundle running above the level of slit diaphragms and the other is the cortical actin network located beneath the plasmalemma. Immunogold labeling for actin-binding proteins demonstrated that oí-actinin and synaptopodin were localized in the actin bundle, whereas cortactin was in the cortical actin network. Immunofluorescence labeling for actin-binding proteins in immature podocyte showed that α-actinin was localized at the level of the junctional complex, whereas cortactin was distributed beneath the entire plasmalemma. Synaptopodin was first observed along the basal plasmalemma from the advanced S-shaped body to the capillary loop stage. We conclude that foot processes have specialized actin filamentous organization and that its establishment is associated with the expression and redistribution of actin-binding proteins during development.

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Tài liệu tham khảo

10.1038/ki.1981.176

10.1002/ar.1092100102

Drenckhahn D, 1988, Lab Invest, 59, 673

10.1074/jbc.273.45.29745

10.1002/cm.970300405

10.1083/jcb.140.6.1383

10.1038/73456

10.1074/jbc.273.45.29672

10.1016/S1097-2765(00)80057-X

10.1083/jcb.130.1.67

10.1038/ki.1994.47

10.1073/pnas.89.15.7075

Kurihara H, 1995, Am J Physiol, 268, F514

Kurihara H, 1992, Am J Pathol, 141, 805

Kurihara H, 1998, Am J Physiol, 274, F986

10.1007/BF02899534

10.1177/39.8.1856454

Nieset JE, 1997, J Cell Sci, 110, 1013, 10.1242/jcs.110.8.1013

Orlando RA, 2001, J Am Soc Nephrol, 12, 1589, 10.1681/ASN.V1281589

Otey CA, 1993, J Biol Chem, 268, 21193, 10.1016/S0021-9258(19)36909-1

Reeves W, 1978, Lab Invest, 39, 90

10.1007/BF00310191

10.1006/excr.2000.5043

10.1083/jcb.111.3.1255

Schnabel E, 1989, Eur J Cell Biol, 48, 313

Shirato I, 1996, Am J Pathol, 148, 1283

Smoyer WE, 1997, Am J Physiol, 273, F150

Trenchev P, 1976, J Anat, 121, 85

10.1002/ar.1092100104

10.1177/002215549804601011

10.1083/jcb.120.6.1417

Youssoufian H, 1990, Am J Hum Genet, 47, 62

Yuan H, 2002, Am J Physiol, 282, F585, 10.1152/ajpcell.00351.2001