Identification and characterization of a novel human collectin CL-K1.
Collectins are a family of C-type lectins with two characteristic structures, collagen like domains and carbohydrate recognition domains. They recognize carbohydrate antigens on microorganisms and act as host-defense. Here we report the cloning and characterization of a novel collectin CL-K1. RT-PCR analyses showed CL-K1 mRNA is present in all organs. The deduced amino acid sequence and the data from immunostaining of CL-K1 cDNA expressing CHO cells revealed that CL-K1 is expressed as a secreted protein. CL-K1 is found in blood by immunoblotting and partial amino acid analyses. CL-K1 showed Ca(2+)-dependent sugar binding activity of fucose and weakly mannose but not N-acetyl-galactosamine, N-acetyl-glucosamine, or maltose, though mannose-binding lectin (MBL) containing similar amino acid motif. CL-K1 can recognize specially several bacterial saccharides due to specific sugar-binding character. Elucidation of the role of two ancestor collectins of CL-K1 and CL-L1 could lead to see the biological function of collectin family.
Keshi
Hiroyuki
H
Research & Development Center, Fuso Pharmaceutical Industries, Osaka, Osaka, Japan.
Sakamoto
Takashi
T
Kawai
Takao
T
Ohtani
Katsuki
K
Katoh
Tsuyoshi
T
Jang
Seong-Jae
SJ
Motomura
Wataru
W
Yoshizaki
Takayuki
T
Fukuda
Mitsuko
M
Koyama
Satoshi
S
Fukuzawa
Jun
J
Fukuoh
Atsushi
A
Yoshida
Itsuro
I
Suzuki
Yasuhiko
Y
Wakamiya
Nobutaka
N
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D016466:CHO Cells; D037222:Collectins / Q000145:classification / Q000235:genetics* / Q000302:isolation & purification*; D006224:Cricetinae; D003412:Cricetulus; D006801:Humans; D007668:Kidney / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data
C518521:Colec11 protein, human; D037222:Collectins