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Glycobiology
2011 Dec 01;2112:1580-7. doi: 10.1093/glycob/cwr070.
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A new type of lectin discovered in a fish, flathead (Platycephalus indicus), suggests an alternative functional role for mammalian plasma kallikrein.
Tsutsui S
,
Okamoto M
,
Ono M
,
Suetake H
,
Kikuchi K
,
Nakamura O
,
Suzuki Y
,
Watanabe T
.
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A skin mucus lectin exhibiting a homodimeric structure and an S-S bond between subunits of ~40 kDa was purified from flathead Platycephalus indicus (Scorpaeniformes). This lectin, named FHL (FlatHead Lectin), exhibited mannose-specific activity in a Ca(2+)-dependent manner. Although FHL showed no homology to any previously reported lectins, it did exhibit ~20% identity to previously discovered plasma kallikreins and coagulation factor XIs of mammals and Xenopus laevis. These known proteins are serine proteases and play pivotal roles in the kinin-generating system or the blood coagulation pathway. However, alignment analysis revealed that while FHL lacked a serine protease domain, it was homologous to the heavy-chain domain of plasma kallikreins and coagulation factor XI therefore suggesting that FHL is not an enzyme but rather a novel animal lectin. On the basis of this finding, we investigated the lectin activity of human plasma kallikrein and revealed that it could indeed act as a lectin. Other genes homologous to FHL were also found in the genome databases of some fish species, but not in mammals. In contrast, plasma kallikreins and coagulation factor XI have yet to be identified in fish. The present findings suggest that these mammalian enzymes may have originally emerged as a lectin and may have evolved into molecules with protease activity after separation from common ancestors.
Fig. 1. SDS–PAGE analysis of FHL. Skin mucus extract (lanes 1 and 2) and the affinity-purified lectin (lanes 3 and 4) was subject to either non-reducing (lanes 1 and 3) or reducing (lanes 2 and 4) SDS–PAGE. M, molecular markers.
Fig. 2. Nucleotide sequence of cDNA and the deduced amino acid sequence of FHL. Numbers on the right indicate the nucleotide and amino acid position. The dashed lines indicate internal sequences obtained by protein sequencing. Predicted signal sequence is shown in italics, and the polyadenylation signal (AATAAA) is double underlined. Polymorphic mutations at positions 61 (C to A), 77 (T to C), 125 (C to T), 135 (G to C), 137 (T to G), 260 (T to C) and 696 (A to G) are underlined, and resulting amino acid changes (at amino acid positions 17 and 204) are circled.
Fig. 3. Comparison of the amino acid sequence of FHL with the plasma kallikreins and coagulation factor XIs of mammals and X. laevis. Numbers on the right indicate the amino acid position. Identical (*) and similar (: or .) residues identified by Clustal W are indicated. The cleavage site for enzyme activation in plasma kallikreins is indicated by arrowhead, and the catalytic triad residues (His, Asp and Ser) are boxed. Four apple domains (corresponding to human plasma kallikrein residues 21–104, 111–194, 201–284 and 292–375) are shown by arrows, and the upper line represents the serine protease domain. Abbreviations and accession numbers are as follows: Homo-PK, human H. sapiens plasma kallikrein (BC117351); Mus-PK, mouse M. musculus plasma kallikrein (BC026555); Rattus-PK, rat Rattus norvegicus plasma kallikrein (BC089815); Bos-PK, bovine Bos taurus plasma kallikrein (BC105498); Sus-PK, pig Sus scrofa plasma kallikrein (AB022425); Xenopus-PK, X. laevis plasma kallikrein (BC077417); Homo-fXI, H. sapiens factor XI (BC122863); Mus-fXI, M. musculus factor XI (BC019485); Bos-fXI, Bos taurus factor XI (AB196307) and Oryctolagus-fXI, rabbit Oryctolagus cuniculus factor XI (AF395821).
Fig. 4. Gene expression of FHL in various tissues. Identical amounts of total RNA from the skin (1), gill (2), esophagus (3), stomach (4), intestine (5), liver (6), kidney (7), heart (8), spleen (9), ovary (10) and muscle (11) were isolated and reverse-transcribed to produce cDNA. PCR amplification was performed with specific primer-3 and -4 to amplify a partial sequence of FHL (A). Corresponding β-actin bands for these samples are shown in (B). M, marker; N, negative control.
Fig. 5. Hemagglutination activity of human plasma kallikrein. Human plasma kallikrein was incubated with PBS (+) only (1) or the same buffer including 1 mg/mL of fetuin (2) at room temperature for 1 h. Then, 2% rabbit red blood cell suspension was added. PBS (+) only (3) and fetuin-containing PBS (+) (4) were also used for negative controls.
Fig. 6. Structural relationship among plasma kallikrein, tissue kallikrein, coagulation factor XI and kalliklectin and their possible distribution. Black and white boxes represent the serine protease domain and the apple domain, respectively. Bar indicates S–S bond.
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