Title : The
isoforms of human
neutrophil elastase and
cathepsin G differ in their carbohydrate side chain structures
Abstract :
- The two proteinases found in human neutrophil granules, elastase and cathepsin G , each are normally isolated as a mixture of isoforms differing only in carbohydrate content
- Elastase has two N-glycosylation sites occupied ( Asn-45 and Asn-144 ), whereas cathepsin G has only one ( Asn-64 )
- Analysis of a minor form of elastase ( E-1) and cathepsin G ( C-1 ) indicates that the carbohydrate structures at each glycosylation site are complex-type bi-antennary chains usually associated with secretory glycoproteins
- In contrast, the isoforms E-3 and C-3 , the major forms of elastase and cathepsin G respectively, contain exclusively truncated, oligomannose-type chains at the same positions in the sequence of each protein
- These data suggest the possibility that certain elastase and cathepsin G isoforms (E-1 and C-1 ) might be destined for secretory, others ( E-3 and C-3 ) for lysosomal functions
Output (sent_index, trigger,
protein,
sugar,
site):
- 2. N-glycosylation, , -, -, Asn-45 and Asn-144
- 2. N-glycosylation, , -, -, sites
- 2. occupied, , -, -, Asn-45 and Asn-144
- 2. occupied, , -, -, sites
- 3. glycoproteins, , glycoproteins, -, -
- 3. glycosylation, , -, -, site
- 3. site, , -, complex-type bi-antennary chains, site
- 3. site, , -, the carbohydrate structures, site
- 4. contain, , C-3, exclusively truncated, oligomannose-type chains, positions
- 4. contain, , E-3, exclusively truncated, oligomannose-type chains, positions
- 4. contain, , isoforms, exclusively truncated, oligomannose-type chains, positions
Output(Part-Of) (sent_index,
protein,
site):
- 2. Elastase, Asn-45 and Asn-144
- 2. Elastase, sites
- 2. cathepsin G, Asn-64
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):
- 2. cathepsin G, -, Asn-45 and Asn-144