The JI
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     
 


The Journal of Immunology, 1972, 109: 407-409.
Copyright © 1972 by The American Association of Immunologists, Inc.

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 Similar articles in this journal
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Bernier, G. M.
Right arrow Articles by Fanger, M. W.
Right arrow Search for Related Content
PubMed
Right arrow Articles by Bernier, G. M.
Right arrow Articles by Fanger, M. W.

Synthesis of beta2-Microglobulin by Stimulated Lymphocytes1

George M. Bernier2 and Michael W. Fanger3

From the Departments of Medicine and Microbiology, Case Western Reserve University, School of Medicine, Cleveland, Ohio 44106

Abstract

beta2-microglobulin is a human serum protein of low molecular weight and unknown function (1). Normally present in serum in low concentrations (2 µg/ml), it is degraded by the kidney (2). In the presence of renal failure serum concentrations as high as 70 µg/ml may occur (3, 4). Patients with defective renal tubular function excrete increased amounts of beta2-microglobulin in their urine (4), suggesting that tubular reabsorption is an important step in the catabolism of this protein. In its dependence upon the kidney for degradation, beta2-microglobulin is similar to immunoglobulin light chains (5), although microglobulin is not antigenically related to any known immunoglobulin.

Recently, Smithies and Poulik have reported the partial amino acid sequence of beta2-microglobulin (6). They found significant homology between beta2-microglobulin and two adjacent loops (C2 and C3) of the heavy chain of human {gamma}G globulin. This finding suggested that beta2-microglobulin might be synthesized in lymphoid tissue and prompted us to investigate whether this protein was produced by lymphocytes during in vitro culture.

Footnotes

1 This work was supported by United States Public Health Service Research Grants AM 14700 and AI 10148.

2 Scholar of the Leukemia Society of America.

3 Recipient of a United States Public Health Service Career Development Award (KO4 A125732).







HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
This Website Copyright © 1972 by The American Association of Immunologists, Inc. All rights reserved.
All Contents Copyright © 1972 by The American Association of Immunologists, Inc. All rights reserved.