Am J Physiol Cell Physiol Watch the video to learn how APS reaches out to developing nations.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Am J Physiol Cell Physiol 263: C551-C562, 1992;
0363-6143/92 $5.00
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Web of Science (25)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Nie, Z.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Nie, Z.

AJP - Cell Physiology, Vol 263, Issue 3 C551-C562, Copyright © 1992 by American Physiological Society


ARTICLES

Fetuin: its enigmatic property of growth promotion

Z. Nie
Department of Cellular and Molecular Physiology, Harvard Medical School, Boston, Massachusetts 02115.

A variety of cell types in culture respond to fetuin, a glycoprotein from fetal bovine serum, which is often an important supplement to many serum-free media. Bovine fetuin preparation has been shown to inhibit trypsin activity and promote cellular attachment, growth, and differentiation in many different culture systems. In addition, fetuin associates with various growth factors or growth-promoting substances. However, whether the growth-promoting activity of fetuin preparation is due to fetuin per se or to its minor contaminant(s) has been a long-standing puzzle. The present review surveys the literature concerning this enigmatic property of fetuin and summarizes three possibilities: 1) fetuin itself is active, although the majority of studies do not support this; 2) various contaminants of fetuin preparations, including potentially unidentified ones, are responsible for the activity, a possibility supported by numerous reports; and 3) one of the fetuin subspecies, one of its contaminants, or a combination of both of these is responsible for growth of a specific cell type. In addition, the basic physicochemical properties and other biological functions of fetuin have also been presented.


This article has been cited by other articles:


Home page
Am. J. Pathol.Home page
S. P. Hart, C. Jackson, L. M. Kremmel, M. S. McNeill, H. Jersmann, K. M. Alexander, J. A. Ross, and I. Dransfield
Specific Binding of an Antigen-Antibody Complex to Apoptotic Human Neutrophils
Am. J. Pathol., March 1, 2003; 162(3): 1011 - 1018.
[Abstract] [Full Text] [PDF]


Home page
Cancer Res.Home page
W.-Q. Zhu and J. Ochieng
Rapid Release of Intracellular Galectin-3 from Breast Carcinoma Cells by Fetuin
Cancer Res., March 1, 2001; 61(5): 1869 - 1873.
[Abstract] [Full Text]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Visit Other APS Journals Online