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  • Title: Synthesis, sorting, and processing into distinct isoforms of human macrophage chitotriosidase.
    Author: Renkema GH, Boot RG, Strijland A, Donker-Koopman WE, van den Berg M, Muijsers AO, Aerts JM.
    Journal: Eur J Biochem; 1997 Mar 01; 244(2):279-85. PubMed ID: 9118991.
    Abstract:
    Chitotriosidase, the human analogue of chitinases from non-vertebrate species, has recently been identified. The macrophage-derived enzyme is remarkably heterogeneous in molecular mass and isoelectric point. The synthesis and modification of the enzyme in cultured macrophages is reported. Chitotriosidase is synthesized as a 50-kDa protein with a pI of about 6.5 and 7.2. It is predominantly secreted, but in part processed into a 39-kDa form with a pI of 8.0 that accumulates in lysosomes. In the C-terminal extension of the 50-kDa chitotriosidase, sialic-acid containing O-linked glycans are present, causing its heterogeneous acidic isoelectric point. Chitotriosidase lacks N-linked glycans and the mechanism of routing to lysosomes proves to be distinct from that of soluble, N-glycosylated, lysosomal enzymes. It was observed that, in macrophages, alternative splicing generates a distinct chitotriosidase mRNA species, encoding a 40-kDa chitotriosidase that is C-terminally truncated. This enzyme is almost identical to the 39-kDa chitotriosidase formed from the 50-kDa precursor by proteolytic processing. It is concluded that the C-terminus present in the 50-kDa chitotriosidase, but absent in the 39-kDa isoform, was found to mediate tight binding to chitin. In the blood stream the secretory 50-kDa chitotriosidase occurs predominantly, whilst in tissues the 39-kDa form is also abundant. These findings are consistent with the data on the synthesis and processing of chitotriosidase in the cultured macrophage model.
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