Abstract：
:We have investigated the structure of the carbohydrate moiety of the precursors of the cathepsin B-like proteinase (PCBt). The largest precursor has an apparent molecular size (Mr) of 45-47 Kd and it contains 3 N-linked oligosaccharide chains which were Endo beta N acetylglucosaminidase H (Endo H)-resistant forms. On the other hand, these chains were sequentially removed by Endo beta N acetylglucosaminidase F (Endo F). Both results indicate a complex type structure for these oligosaccharides. As usual in these cases, sialic acids were also found. In the deglycosylated state, PCBt has a Mr value of 36 Kd closely related to the 35.9 Kd Mr for human Pro CB, deduced from the cDNa sequence. These findings may explain the extracellular location of PCBt in malignancy: complex oligosaccharides are in most cases associated with secretory or membrane bound glycoproteins. On the contrary, mannose-rich types are involved in the lysosomal routage.
journal_name
Cancer Lettjournal_title
Cancer lettersauthors
Pagano M,Dalet-Fumeron V,Engler Rdoi
10.1016/0304-3835(89)90030-xsubject
Has Abstractpub_date
1989-04-01 00:00:00pages
13-9issue
1eissn
0304-3835issn
1872-7980pii
0304-3835(89)90030-Xjournal_volume
45pub_type
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