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Endocrinology Vol. 138, No. 11 4837-4843
Copyright © 1997 by The Endocrine Society

ARTICLES

Circulating and Tissue Forms of the Intestinal Growth Factor, Glucagon-Like Peptide-21

Patricia L. Brubaker, Anna Crivici, Angelo Izzo, Peter Ehrlich, Chun-Hui Tsai and Daniel J. Drucker2

Departments of Physiology (P.L.B.) and Medicine (P.L.B., P.E., C.-H.T., D.J.D.) and Banting and Best Diabetes Center (D.J.D.), University of Toronto, Toronto, Canada; and Allelix Biopharmaceuticals, Inc. (A.C.), Mississauga, Ontario, Canada

Address all correspondence and requests for reprints to: Dr. P. L. Brubaker, Room 3366, Medical Sciences Building, University of Toronto, Toronto, Ontario, Canada M5S 1A8. E-mail: p.brubaker{at}utoronto.ca

Glucagon-like peptide-2 (GLP-2) has recently been identified as a stimulator of intestinal epithelial growth, prompting the development of RIA and HPLC methodologies to study this peptide in more detail. A GLP-2-specific antiserum (UTTH-7) was developed that recognizes amino acids 25–30 of human and rat GLP-2-(1–33). UTTH-7 cross-reacts with N- and C-terminally modified forms of GLP-2, proglucagon, and the major proglucagon fragment. Analysis of rat ileal extracts demonstrated the presence of GLP-2-(1–33) as well as significant amounts of GLP-2-(3–33) (16 ± 7% of total GLP-2). The level of total immunoreactive GLP-2 in plasma from fasted rats was 700 ± 71 pg/ml, and this increased 3.6-fold (P < 0.001) in 24-h fed rats. HPLC analysis demonstrated the presence of both GLP-2-(1–33) and GLP-2-(3–33) in plasma from fasted rats, with increments in both peptides in plasma from fed rats. Immunoreactive GLP-2 increased in plasma from human subjects 2 h after a meal, rising from 851 ± 230 to 1106 ± 211 pg/ml (P < 0.05); 15 ± 4% of this immunoreactivity was accounted for by the presence of intact GLP-2. HPLC showed the presence of both GLP-2-(1–33) and GLP-2-(3–33) in plasma from fed humans. Incubation of human GLP-2-(1–33) with the enzyme dipeptidylpeptidase IV resulted in liberation of GLP-2-(3–33), whereas replacement of Ala2 with Gly2 prevented this cleavage. Thus, while GLP-2-(1–33) is a major circulating and tissue form of GLP-2, GLP-2-(3–33) is a significant component of immunoreactive GLP-2 in both intestine and plasma.




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