Chitotriosidase, a chitinase, and the 39‐kDa human cartilage glycoprotein, a chitin‐binding lectin, are homologues of family 18 glycosyl hydrolases secreted by human macrophages

Renkema, G. Herma; Boot, Rolf G.; Au, Fung L.; Donker‐Koopman, Wilma E.; Strijland, Anneke; Muijsers, Anton O.; Hřebı́ček, Martin; Aerts, Johannes M. F. G.

doi:10.1046/j.1432-1327.1998.2510504.x

Cited by 368 publications

(289 citation statements)

References 2 publications

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“…According to Renkema et al (1998), human chitotriosidase, which is highly homologous to HC gp-39 but possesses chitinase activity, has a similar amino acid sequence in its catalytic center, the major exception being that it contains the essential Glu residue. When the Glu residue of chitotriosidase was mutated to Leu, a loss of hydrolytic activity resulted.…”

Section: Discussionmentioning

confidence: 99%

CHRK1, a Chitinase-Related Receptor-Like Kinase in Tobacco

et al. 2000

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A cDNA encoding a chitinase-related receptor-like kinase, designated CHRK1, was isolated from tobacco (Nicotiana tabacum). The C-terminal kinase domain (KD) of CHRK1 contained all of the conserved amino acids of serine/threonine protein kinases. The putative extracellular domain was closely related to the class V chitinase of tobacco and to microbial chitinases. CHRK1 mRNA accumulation was strongly stimulated by infection with fungal pathogen and tobacco mosaic virus. Amino acid-sequence analysis revealed that the chitinase-like domain of CHRK1 lacked the essential glutamic acid residue required for chitinase activity. The recombinant chitinase-like domain did not show any catalytic activity for either oligomeric or polymeric chitin substrates. The recombinant KD of CHRK1 exhibited autophosphorylation, but the mutant KD with a mutation in the essential ATP-binding site did not, suggesting that CHRK1 encoded a functional kinase. CHRK1 was detected in membrane fractions of tobacco BY2 cells. Furthermore, CHRK1-GFP fusion protein was localized in plasma membranes when it was expressed in animal cells. This is the first report of a new type of receptor-like kinase containing a chitinase-like sequence in the putative extracellular domain.Plant receptor-like kinases (RLKs) play a fundamental role in various cellular processes, including hormone signaling (

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Section: Discussionmentioning

confidence: 99%

CHRK1, a Chitinase-Related Receptor-Like Kinase in Tobacco

et al. 2000

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“…7 YKL-40 is a member of the mammalian family of 18 glycosyl hydrolases. 8 -10 It is a heparin and chitinbinding lectin 10,11 without chitinase activity. 8,12 The biologic function of YKL-40 is not known in detail, but it has been shown that YKL-40 is a growth factor for connective tissue cells 13,14 and a potent migration factor for endothelial cells.…”

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confidence: 99%

High serum YKL‐40 level after surgery for colorectal carcinoma is related to short survival

Cintin

Johansen

Christensen

et al. 2002

Cancer

126

116

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“…hCHT is a phagocyte-specific chitinase that exists in two isoforms, a major 50 kDa and a C-terminally truncated 39 kDa isoform [2]. The C-terminal domain of the 39 kDa isoform has been shown to be involved in the binding of chitin [3], whereas the 50 kDa form is secreted from macrophages and the truncated form is not.…”

Section: Introductionmentioning

confidence: 99%

“…These include YKL-40 (chitinase 3-like-1), YKL-39 (chitinase 3-like-2), Ym1/2 (chitinase 3-like-3/4), oviduct-specific glycoprotein and stabilin-1-interacting chitinaselike protein [11][12][13][14][15][16][17]. YKL-40 (also termed HC-gp39 or Chi3l1) was found to be secreted, along with chitotriosidase, from activated human macrophages and it was later detected in the culture supernatant of chondrocytes, synovial cells and osteoblasts [2,11]. In vitro experiments demonstrated YKL-40 induction through the cell-stress pathway when chondrocytes were exposed to LPS (lipopolysaccharide) [18].…”

Section: Introductionmentioning

confidence: 99%

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Human YKL-39 is a pseudo-chitinase with retained chitooligosaccharide-binding properties

Schimpl

Rush

Betou

et al. 2012

Biochemical Journal

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The chitinase-like proteins YKL-39 (chitinase 3-like-2) and YKL-40 (chitinase 3-like-1) are highly expressed in a number of human cells independent of their origin (mesenchymal, epithelial or haemapoietic). Elevated serum levels of YKL-40 have been associated with a negative outcome in a number of diseases ranging from cancer to inflammation and asthma. YKL-39 expression has been associated with osteoarthritis. However, despite the reported association with disease, the physiological or pathological role of these proteins is still very poorly understood. Although YKL-39 is homologous to the two family 18 chitinases in the human genome, it has been reported to lack any chitinase activity. In the present study, we show that human YKL-39 possesses a chitinase-like fold, but lacks key active-site residues required for catalysis. A glycan screen identified oligomers of N-acetylglucosamine as preferred binding partners. YKL-39 binds chitooligosaccharides and a newly synthesized derivative of the bisdionin chitinase-inhibitor class with micromolar affinity, through a number of conserved tryptophan residues. Strikingly, the chitinase activity of YKL-39 was recovered by reverting two non-conservative substitutions in the active site to those found in the active enzymes, suggesting that YKL-39 is a pseudo-chitinase with retention of chitinase-like ligand-binding properties.

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Chitotriosidase, a chitinase, and the 39‐kDa human cartilage glycoprotein, a chitin‐binding lectin, are homologues of family 18 glycosyl hydrolases secreted by human macrophages

Cited by 368 publications

References 2 publications

CHRK1, a Chitinase-Related Receptor-Like Kinase in Tobacco

CHRK1, a Chitinase-Related Receptor-Like Kinase in Tobacco

High serum YKL‐40 level after surgery for colorectal carcinoma is related to short survival

Human YKL-39 is a pseudo-chitinase with retained chitooligosaccharide-binding properties

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