Journal
JOURNAL OF BIOCHEMISTRY
Volume 151, Issue 1, Pages 57-64Publisher
OXFORD UNIV PRESS
DOI: 10.1093/jb/mvr114
Keywords
complement; blood coagulation; lectin; carbohydrate; genetic
Categories
Funding
- 'Knowledge Cluster Initiative' (2nd Stage, 'Sapporo Biocluster Bio-S')
- Japan Ministry of Education, Culture, Sports, Science, and Technology
- Core Research for Evolutional Science and Technology
- Japan Health Sciences Foundation [KH21011]
- Fuso Pharmaceutical Industry, Co.
- Fugaku Trust for Medical Research
- Smoking Research Foundation
- Akiyama Foundation
- Hokkaido Heart Association
- Takeda Science Foundation
- [19390227]
- [22390113]
- [22590259]
- Grants-in-Aid for Scientific Research [22390113, 23590749, 22590259] Funding Source: KAKEN
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Mannan-binding lectin (MBL) was first discovered as a collectin in animal blood, and was shown to have such unique characteristics as a collage-like domain and a carbohydrate recognition domain. We recently identified human collectin kidney 1 (CL-K1, COLEC11) from a human kidney cDNA library. To quantitate the CL-K1 concentration in blood, we developed several polyclonal and monoclonal antibodies using recombinant human CL-K1 in CHO cells and the CL-K1 fragment in Escherichia coli. Using these antibodies, we established a sandwich enzyme-linked immunosorbent assay (ELISA) system. The concentration of CL-K1 in human plasma was 0.34 +/- 0.13 mu g/ml and that in MBL was 1.72 +/- 1.51 mu g/ml. Concentrations of MBL are often low due to its single nucleotide polymorphisms (SNPs) which seem to be related to an opsonic defect. However, no low concentrations of CL-K1 were observed on testing over two hundred blood samples. We also found that the blood concentration of CL-K1 was not dependent on gender or age and did not correlate completely with that of MBL. The ELISA system developed in this study will be useful for elucidating the physiological and pathophysiological role of CL-K1 in humans.
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