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Immature granules are not major sites for segregation of constitutively secreted granule content proteins in NIT-1 insulinoma cells.

Abstract：

:Immature secretory granules (ISG's) are sites of segregation of proteins destined for secretion by unregulated pathways from those stored in mature secretory granules in endocrine cells. To determine whether significant soluble protein sorting occurs in ISG's, the secretion of soluble versions of the pancreatic protein GP2 (GP2-GPI(-)) and placental alkaline phosphatase (SEAP) was analyzed in NIT-1 cells. By immunofluorescence microscopy, neither protein localized to SG's in transfected cells. Their secretion was secretagogue-independent in pulse-chase radiolabeling experiments even at early times of chase, while a small increase in the secretion of amylase, which is known to enter ISG's, could be detected. Finally, in sucrose gradient fractionation experiments, SEAP was present in light density fractions. We conclude that while some proteins, such as amylase, have a limited intrinsic capacity to enter ISG's, the segregation of proteins secreted via the constitutive pathway from SG content proteins occurs primarily in the trans Golgi network.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Rindler MJ,Colomer V,Jin Y

doi

10.1006/bbrc.2001.5889

subject

Has Abstract

pub_date

2001-11-16 00:00:00

pages

1071-7

issue

5

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(01)95889-9

journal_volume

288

pub_type

杂志文章

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