title: The actin-binding proteins adseverin and gelsolin are both highly expressed but differentially localized in kidney and intestine.
abstract: To understand the distinct functions of the closely related actin-severing proteins adseverin and gelsolin, we examined the expression of these proteins in detail during mouse and human development using a new highly sensitive and specific set of antibody reagents. Immunoblot analysis demonstrated that adseverin was highly expressed in mouse kidney and intestine at all stages of development and in human fetal and adult kidney. In contrast and as reported previously, gelsolin was expressed much more widely in both murine and human tissues. Immunohistochemistry on murine kidney sections revealed a predominantly differential localization of adseverin and gelsolin. Adseverin was expressed in peripolar cells, thin limbs, thick ascending limbs, and principal cells of cortical and medullary collecting ducts where it was diffusely localized in the cytoplasm. Gelsolin was expressed in the distal convoluted tubule, intercalated cells and principal cells of cortical and medullary collecting ducts, and in ureter. In the distal convoluted tubule, gelsolin showed a diffuse distribution and in principal cells of collecting ducts a localization at the basolateral pole. In intercalated cells, gelsolin localization was heterogeneous, either at the apical pole or diffusely in the cytoplasm. In human fetal and adult kidney, adseverin was expressed only in collecting ducts whereas gelsolin was expressed in thick ascending limbs and collecting ducts. In mouse and human intestine adseverin was expressed in enterocytes with a gradient of increasing expression from the duodenum to the colon, and from the crypt to the villus. The observations indicate high level expression of adseverin in specific cells of the kidney and colon, and suggest a previously unrecognized function of adseverin in epithelial cell function.
authors.affiliation: Brigham and Women's Hospital, Harvard Medical School, Department of Medicine, Division of Experimental Medicine, Boston, MA 02115, USA.
authors.forename: A
authors.initials: A
authors.lastname: Lueck
authors.forename: D
authors.initials: D
authors.lastname: Brown
authors.forename: D J
authors.initials: DJ
authors.lastname: Kwiatkowski
mesh_terms: D000328:Adult; D000818:Animals; D000906:Antibodies / Q000737:chemistry / Q000378:metabolism; D005333:Fetus; D018260:Gelsolin / Q000096:biosynthesis* / Q000276:immunology; D018507:Gene Expression Regulation, Developmental; D006801:Humans; D007150:Immunohistochemistry; D007413:Intestinal Mucosa / Q000378:metabolism*; D007668:Kidney / Q000378:metabolism*; D051379:Mice; D008840:Microfilament Proteins / Q000096:biosynthesis* / Q000276:immunology; D009928:Organ Specificity
chemical_list: D000906:Antibodies; D018260:Gelsolin; D008840:Microfilament Proteins; C065395:scinderin