Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.6.4 (chondroitinase)
 2,039 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Heparan sulfate proteoglycan (HSPG) was extracted from human tubular basement membrane (TBM) with guanidine and purified by ion-exchange chromatography and gel filtration. The glycoconjugate was sensitive to heparitinase and resistant to chondroitinase ABC, had an apparent molecular mass of 200-400 kDa and consisted of 70% protein and 30% glycosaminoglycan. The amino acid composition was characterized by its high content of glycine, proline, alanine and glutamic acid. Hydrolysis with trifluoromethanesulfonic acid yielded core proteins of 160 and 110 kDa. The heparan sulfate (HS) chains obtained after alkaline NaBH4 treatment had a molecular mass of about 18 kDa. Results of heparitinase digestion and HNO2 treatment suggest a clustering of sulfate groups in the distal portion of the HS side chains. These chemical data are comparable to those obtained previously on glomerular basement membrane (GBM) HSPG (Van den Heuvel et al. (1989) Biochem. J. 264, 457-465). Peptide patterns obtained after trypsin, clostripain or V8 protease digestion of TBM and GBM HSPG preparations showed a large similarity. Polyclonal antisera and a panel of monoclonal antibodies raised against both HSPG preparations and directed against the core protein showed complete cross-reactivity in ELISA and on Western blots. They stained all basement membranes in an intense linear fashion in indirect immunofluorescence studies on human kidneys. Based on these biochemical and immunological data we conclude that HSPGs from human GBM and TBM are identical, or at least very closely related, proteins.
 ...
PMID:Heparan sulfate proteoglycan from human tubular basement membrane. Comparison with this component from the glomerular basement membrane. 216 19

Heparan sulfate proteoglycan from the Engelbreth-Holm-Swarm mouse tumor was previously separated into two forms: a high density form (Form HD) and low density form (Form LD). In this study, the two forms were radiolabeled either metabolically with [35S]sulfate or [3H]serine or chemically with 125I. Pulse-chase experiments with [35S]sulfate showed no clear precursor-product relationship between the two forms. Analyses of the labeled proteoglycan samples with heparitinase and chondroitinase ABC indicated that Form LD is a large proteoglycan containing heparan sulfate chains attached to a single core molecule (Mr = 450,000), whereas Form HD is a mixture of small proteoglycans with four different size core molecules (Mr = 34,000, 29,000, 27,000, and 21,000), most, if not all, of which bear both heparan sulfate (Mr = 60,000) and chondroitin sulfate (Mr = 17,000) chains. Glycosaminoglycan-enriched fragments obtained from Form HD by V8 protease digestion were also shown to contain both heparitinase-susceptible chains and chondroitinase ABC-susceptible chains. Tryptic peptide maps of 125I-labeled Form HD and the glycosaminoglycan-enriched fragments derived therefrom were quite different from the corresponding maps for Form LD.
 ...
PMID:Multiple forms of heparan sulfate proteoglycans in the Engelbreth-Holm-Swarm mouse tumor. The occurrence of high density forms bearing both heparan sulfate and chondroitin sulfate side chains. 295 17

1. Proteoglycans were isolated from human and equine glomeruli or tubules by guanidine extraction and anion exchange chromatography. 2. These proteoglycan preparations contained about equal amounts of heparan sulfate and chondroitin sulfates. 3. During the preparation of glomerular or tubular basement membranes the main part of proteoglycans (greater than 50%) was extracted in the salt extract. Chondroitin sulfate proteoglycan was mainly found in the water and salt extracts of glomeruli and tubules, heparan sulfate proteoglycan in the deoxycholate extracts and the basement membranes. 4. The glomerular basement membrane (GBM) contains about 12% (human) or 20% (equine) of the proteoglycans of the total glomerulus. They consist of greater than 70% (equine) or 80% (human) of heparan sulfate. 5. Heparan sulfate proteoglycan was isolated from the proteoglycan preparations of human or equine glomeruli and tubules by additional treatment with nucleases and chondroitinase ABC followed by CsCl gradient centrifugation. 6. Protein accounts for about 40% (dry weight) of the heparan sulfate proteoglycans. Their amino acid composition is characterized by a high content of glycine, but 3-hydroxyproline, 4-hydroxyproline and hydroxylysine are lacking. 7. The biochemical characteristics of the heparan sulfate proteoglycan of human or equine glomeruli or tubules differ from that isolated from rat glomeruli by their higher protein content and their amino acid composition. The significance of these differences is discussed.
 ...
PMID:Heparan sulfate proteoglycan from human and equine glomeruli and tubules. 297 41