Home LiteratureArticle Details
PMID: 2037622 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Exosome formation during maturation of mammalian and avian reticulocytes: evidence that exosome release is a major route for externalization of obsolete membrane proteins.

Journal of cellular physiology ·Vol. 147 ·No. 1 ·1991-04-00 ·Pages 27-36

Johnstone RM, Mathew A, Mason AB, Teng K

Abstract

We have assessed whether exosome formation is a significant route for loss of plasma membrane functions during sheep reticulocyte maturation in vitro. Although the recovery of transferrin binding activity in exosomes is at best approximately 25-30% of the lost activity, recoveries of over 50% of the lost receptor can be obtained if 125I-labelled transferrin receptor is measured using an that receptor instability may contribute to the less than quantitative recovery of the transferrin receptor. Significantly higher (75-80%) levels of the nucleoside transporter can be recovered in exosomes during red cell maturation using 3H-nitrobenzylthioinosine binding to measure the nucleoside transporter. These data suggest that exosome formation is a major route for removal of plasma membrane proteins during reticulocyte maturation and plasma membrane remodelling. We have also shown that both in vivo and in vitro, embryonic chicken reticulocytes form exosomes which contain the transferrin receptor. Thus, exosome formation is not restricted to mammalian red cells, but also occurs in red cells, which retain organelles, such as nuclei and mitochondria, into the mature red cell stage.

MeSH Terms
Animals Carrier Proteins/metabolism Cell Differentiation Cell Membrane/metabolism,ultrastructure Chickens Exocytosis Hot Temperature Membrane Proteins/metabolism Nucleoside Transport Proteins Receptors, Transferrin/metabolism Reticulocytes/metabolism,ultrastructure Sheep Thioinosine/analogs & derivatives,metabolism Transferrin/metabolism
Chemicals
Carrier Proteins Membrane Proteins Nucleoside Transport Proteins Receptors, Transferrin Transferrin Thioinosine 4-nitrobenzylthioinosine
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Johnstone R M
Department of Biochemistry, McGill University, Montreal, Quebec, Canada.
Mathew A
Mason A B
Teng K
Article Info
Journal
Journal of cellular physiology
Abbr.
J Cell Physiol
ISSN
0021-9541
Published
1991-04-00
Pages
27-36
Language
English
Region
United States
NLM ID
0050222
Subset
IM
Grants
NIDDK NIH HHS · DK 40299 · United States
NIDDK NIH HHS · DK21739 · United States
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com