Distribution of chitinase in guinea pig tissues and increases in levels of this enzyme after systemic infection with Aspergillus fumigatus.
Intravenous infection of guinea pigs with the fungus Aspergillus fumigatus resulted in increased levels of chitinase in serum and tissues of the animals. The molecular properties of the enzyme were demonstrated to be different from those of the fungal chitinase, but also from guinea pig lysozyme and beta-N-acetylhexosaminidase. Bio-Gel P-100 gel filtration showed that in liver, spleen, heart and lung tissue of control animals there were two molecular mass forms present with apparent molecular masses of 35 kDa and 15 kDa. In brain and serum, only the 35 kDa form was detectable. Kidney showed only the 15 kDa form. Upon infection the 35 kDa form appeared in kidney and increased in the other tissues. When a less pathogenic form of the fungus was used the 35 kDa form remained absent in kidney. In contrast to human serum chitinase, the enzyme from guinea pig serum and tissues did bind to concanavalin A-Sepharose. This was the case for both molecular mass forms. The mode of cleavage of the substrate 4-methylumbelliferyl-tri-N-acetylchitotrioside (MU-[GlcNAc]3, where GlcNAc is N-acetylglucosamine) by the two forms of the enzyme was the same: both [GlcNAc]2 and [GlcNAc]3 were released. The chitinase activity levels in the control tissues showed a large variation in this order: spleen > lung, kidney > liver > heart > brain. The fact that spleen showed the highest chitinase level is in agreement with its major role as a lymphoid organ in cases of systemic infections. The relative increases upon infection were the highest for the tissues that showed low control values.
Overdijk
Bernard
B
Department of Medical Chemistry, Vrije Universiteit, Van der Boechorststraat 7, 1081 BT Amsterdam, The Netherlands.
Van Steijn
Gé J
GJ
Department of Medical Chemistry, Vrije Universiteit, Van der Boechorststraat 7, 1081 BT Amsterdam, The Netherlands.
Odds
Frank C
FC
Janssen Research Foundation, Department of Bacteriology and Mycology, Turnhoutseweg 30, B-2340 Beerse, Belgium.
D000117:Acetylglucosamine / Q000031:analogs & derivatives / Q000378:metabolism / Q000494:pharmacology; D000818:Animals; D001228:Aspergillosis / Q000201:enzymology* / Q000382:microbiology; D001232:Aspergillus fumigatus / Q000201:enzymology / Q000302:isolation & purification; D001921:Brain / Q000201:enzymology / Q000378:metabolism; D002688:Chitinases / Q000037:antagonists & inhibitors / Q000097:blood / Q000737:chemistry / Q000378:metabolism*; D002850:Chromatography, Gel; D003208:Concanavalin A / Q000378:metabolism; D006168:Guinea Pigs; D006923:Hymecromone / Q000031:analogs & derivatives / Q000378:metabolism; D007668:Kidney / Q000201:enzymology / Q000378:metabolism; D008099:Liver / Q000201:enzymology / Q000378:metabolism; D008168:Lung / Q000201:enzymology / Q000378:metabolism; D008970:Molecular Weight; D009206:Myocardium / Q000201:enzymology / Q000378:metabolism; D009844:Oligosaccharides / Q000378:metabolism; D009928:Organ Specificity; D013154:Spleen / Q000201:enzymology / Q000378:metabolism; D013997:Time Factors; D014312:Trisaccharides / Q000494:pharmacology; D001619:beta-N-Acetylhexosaminidases / Q000097:blood / Q000378:metabolism
C015366:4-methylumbelliferyl-N-acetyl-chitotrioside; D009844:Oligosaccharides; D014312:Trisaccharides; C054851:allosamidin; D003208:Concanavalin A; D006923:Hymecromone; D002688:Chitinases; D001619:beta-N-Acetylhexosaminidases; D000117:Acetylglucosamine