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Subcellular distribution, secretion, and posttranslational modifications of clusterin in thyrocytes.

Abstract：

:A prominent secretory glycoprotein was detected in the culture medium of porcine thyrocytes which was identified as clusterin by microsequencing. Treatment of thyrocytes with thyroid stimulating hormone revealed a tight regulation of both synthesis and secretion of clusterin, with a distinct fraction of clusterin being always associated with the cells. At least three N-bound glycans were found on each subunit of clusterin, receiving most of the incorporated [(32)P]phosphate-label. Binding of clusterin to the immobilized cation-independent mannose 6-phosphate (M6P) receptor indicated that part of the phosphate label was contained in M6P moieties. Immunolabeling of cultured thyrocytes and of thyrocytes in situ showed clusterin on the apical cell surfaces where it colocalized with gp330/megalin, which is known to serve as a binding site for clusterin. The association with the apical plasma membrane, which, in thyrocytes, carries the iodinating system, was confirmed by biosynthetic iodination, an as yet unknown posttranslational modification of clusterin. On the basolateral plasma membranes clusterin was found within distinct, bipartite patches, suggesting that it is a constituent of cell-adhesion complexes and that it participates in cell-cell and cell-matrix interactions.

journal_name

Exp Cell Res

journal_title

Experimental cell research

authors

Lemansky P,Brix K,Herzog V

doi

10.1006/excr.1999.4555

keywords:

subject

Has Abstract

pub_date

1999-08-25 00:00:00

pages

147-55

issue

1

eissn

0014-4827

issn

1090-2422

pii

S0014-4827(99)94555-X

journal_volume

251

pub_type

杂志文章

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