The clearance of glycoproteins in diabetic mice

Salvatore V. Pizzo; Mark A. Lehrman; Michael J. Imber; C. Earl Guthrow

doi:10.1016/0006-291X(81)91315-2

The clearance of glycoproteins in diabetic mice

Salvatore V. Pizzo, Mark A. Lehrman, Michael J. Imber, C. Earl Guthrow

Research output: Contribution to journal › Article › peer-review

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Abstract

The clearances of N-acetyl-D-glucosaminyl-bovine serum albumin (GlcNAc-BSA), L-fucosyl-bovine serum albumin (Fuc-BSA) and asialoorosomucoid (ASOR) were evaluated in alloxan-induced diabetic mice and compared to non-diabetic litter mates. The clearances of Fuc-BSA and ASOR were identical in both groups. However, the clearance of GlcNAc-BSA was considerably slower in the diabetic animals. When GlcNAc-BSA was injected into normal mice in the presence of a blood glucose of 25 to 50 mM, competition was observed. No competition was seen with Fuc-BSA or D-galactosyl-BSA (Gal-BSA) in the presence of 50 mM glucose. In, vitro binding studies with purified receptor for GlcNAc/mannose confirm that glucose competes for binding of GlcNAc-BSA to this receptor.

Original language	English (US)
Pages (from-to)	704-708
Number of pages	5
Journal	Biochemical and Biophysical Research Communications
Volume	101
Issue number	2
DOIs	https://doi.org/10.1016/0006-291X(81)91315-2
State	Published - Jul 30 1981

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/0006-291X(81)91315-2

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title = "The clearance of glycoproteins in diabetic mice",

abstract = "The clearances of N-acetyl-D-glucosaminyl-bovine serum albumin (GlcNAc-BSA), L-fucosyl-bovine serum albumin (Fuc-BSA) and asialoorosomucoid (ASOR) were evaluated in alloxan-induced diabetic mice and compared to non-diabetic litter mates. The clearances of Fuc-BSA and ASOR were identical in both groups. However, the clearance of GlcNAc-BSA was considerably slower in the diabetic animals. When GlcNAc-BSA was injected into normal mice in the presence of a blood glucose of 25 to 50 mM, competition was observed. No competition was seen with Fuc-BSA or D-galactosyl-BSA (Gal-BSA) in the presence of 50 mM glucose. In, vitro binding studies with purified receptor for GlcNAc/mannose confirm that glucose competes for binding of GlcNAc-BSA to this receptor.",

author = "Pizzo, {Salvatore V.} and Lehrman, {Mark A.} and Imber, {Michael J.} and Guthrow, {C. Earl}",

note = "Funding Information: This study was supported by grants from the National Heart,",

year = "1981",

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doi = "10.1016/0006-291X(81)91315-2",

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T1 - The clearance of glycoproteins in diabetic mice

AU - Pizzo, Salvatore V.

AU - Lehrman, Mark A.

AU - Imber, Michael J.

AU - Guthrow, C. Earl

N1 - Funding Information: This study was supported by grants from the National Heart,

PY - 1981/7/30

Y1 - 1981/7/30

N2 - The clearances of N-acetyl-D-glucosaminyl-bovine serum albumin (GlcNAc-BSA), L-fucosyl-bovine serum albumin (Fuc-BSA) and asialoorosomucoid (ASOR) were evaluated in alloxan-induced diabetic mice and compared to non-diabetic litter mates. The clearances of Fuc-BSA and ASOR were identical in both groups. However, the clearance of GlcNAc-BSA was considerably slower in the diabetic animals. When GlcNAc-BSA was injected into normal mice in the presence of a blood glucose of 25 to 50 mM, competition was observed. No competition was seen with Fuc-BSA or D-galactosyl-BSA (Gal-BSA) in the presence of 50 mM glucose. In, vitro binding studies with purified receptor for GlcNAc/mannose confirm that glucose competes for binding of GlcNAc-BSA to this receptor.

AB - The clearances of N-acetyl-D-glucosaminyl-bovine serum albumin (GlcNAc-BSA), L-fucosyl-bovine serum albumin (Fuc-BSA) and asialoorosomucoid (ASOR) were evaluated in alloxan-induced diabetic mice and compared to non-diabetic litter mates. The clearances of Fuc-BSA and ASOR were identical in both groups. However, the clearance of GlcNAc-BSA was considerably slower in the diabetic animals. When GlcNAc-BSA was injected into normal mice in the presence of a blood glucose of 25 to 50 mM, competition was observed. No competition was seen with Fuc-BSA or D-galactosyl-BSA (Gal-BSA) in the presence of 50 mM glucose. In, vitro binding studies with purified receptor for GlcNAc/mannose confirm that glucose competes for binding of GlcNAc-BSA to this receptor.

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AN - SCOPUS:0019850263

SN - 0006-291X

VL - 101

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EP - 708

JO - Biochemical and Biophysical Research Communications

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The clearance of glycoproteins in diabetic mice

Abstract

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