Release of glomerular heparan-/sup 35/SO/sub 4/ proteoglycan by heparin from glomeruli of streptozocin-induced diabetic rats

Journal Article · Sun Jan 01 00:00:00 EST 1989 · Diabetes; (United States)

OSTI ID:6395100

Klein, D J; Oegema, Jr, T R; Brown, D M

Abnormalities in the incorporation of heparan sulfate proteoglycan into the glomerular basement membrane have been implicated in the pathogenesis of various proteinuric states, including diabetes mellitus. To understand further the interactions between proteoglycans and glomerular extracellular matrices, glomeruli were isolated from normal and streptozocin-induced diabetic rats after in vivo exposure to 35S-labeled sulfate and were treated with heparin in vitro. Heparin treatment released a unique heparan sulfate proteoglycan from glomerular cell surface or extracellular matrix proteoglycan receptors. Another, smaller heparan sulfate proteoglycan was the most abundant proteoglycan released into medium and was released constitutively in medium with or without added heparin. While the two heparin-extracted proteoglycans copurified on anion-exchange and gel-filtration chromatographic columns, they were resolved by composite 0.6% agarose--1.8% polyacrylamide gel electrophoresis. Glomeruli from diabetic rats contained decreased proportions of the heparin-releasable heparan sulfate proteoglycan and more constitutively released heparan sulfate proteoglycan. The apparent molecular weight and intrinsic charge of the heparin-released proteoglycan mixture and the apparent molecular weight and sulfation pattern of their 35S-labeled glycosaminoglycan chains after nitrous acid deaminative cleavage were similar in the two groups. A brief trypsin digestion of heparin-treated glomeruli released proportionately less integral membrane and extracellular matrix 35S-labeled proteoglycans and 35S-labeled glycopeptides from diabetic glomeruli than form control glomeruli. Elution of these 35S-labeled macromolecules from anion-exchange columns and migration in agarose-polyacrylamide gels were similar in the two groups.

• Research Organization: Univ. of Minnesota Medical School, Minneapolis (USA)
• OSTI ID: 6395100
• Journal Information: Diabetes; (United States), Vol. 38:1
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
DIABETES MELLITUS
PATHOGENESIS
GLUCOPROTEINS
SECRETION
CHROMATOGRAPHY
ELECTROPHORESIS
HEPARIN
IN VITRO
KIDNEYS
MOLECULAR WEIGHT
MUCOPOLYSACCHARIDES
RATS
RECEPTORS
SULFATES
SULFUR 35
TRACER TECHNIQUES
TRYPSIN
AMINES
ANIMALS
ANTICOAGULANTS
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
BODY
CARBOHYDRATES
DAYS LIVING RADIOISOTOPES
DISEASES
DRUGS
ENDOCRINE DISEASES
ENZYMES
EVEN-ODD NUCLEI
GLYCOPROTEINS
HEMATOLOGIC AGENTS
HYDROLASES
ISOTOPE APPLICATIONS
ISOTOPES
LIGHT NUCLEI
MAMMALS
MEMBRANE PROTEINS
METABOLIC DISEASES
NUCLEI
ORGANIC COMPOUNDS
ORGANIC SULFUR COMPOUNDS
ORGANS
OXYGEN COMPOUNDS
PEPTIDE HYDROLASES
POLYSACCHARIDES
PROTEINS
RADIOISOTOPES
RODENTS
SACCHARIDES
SEPARATION PROCESSES
SERINE PROTEINASES
SULFUR COMPOUNDS
SULFUR ISOTOPES
VERTEBRATES
550901* - Pathology- Tracer Techniques