QINGPAN BU, PING LI, YUNFEI XIA, XINPEI WEI, KAI SONG^*

BIOCELL, Vol.47, No.11, pp. 2535-2546, 2023, DOI:10.32604/biocell.2023.030781

Abstract Mannose, a different isomer of the hydroxyl group at the C-2 position of glucose, shares the same transport carrier protein with glucose to enter cells and participate in the regulation of glucose metabolism. It affects cell growth, differentiation, and function and plays an active role in tumor immunity and inflammatory processes. This paper provides theoretical support for expanding the clinical applications of mannose by exploring its constitution, metabolic pathways, and role in regulating immune cell function and treating immunology-related diseases. More > Graphic Abstract

JUAN LIN¹, XUANWEI ZHOU², JIONG FEI², ZHIHUA LIAO¹, WANG JIN¹, XIAOFEN SUN^1,*, KEXUAN TANG^1,2,*

BIOCELL, Vol.30, No.1, pp. 15-25, 2006, DOI:10.32604/biocell.2006.30.015

Abstract A gene encoding a mannose-binding lectin, Pinellia pedatisecta agglutinin (PPA), was isolated from leaves of Pinellia pedatisecta using genomic walker technology. The ppa contained an 1140-bp 5’-upstream region, a 771-bp open reading frame (ORF) and an 829-bp 3’-downstream region. The ORF encoded a precursor polypeptide of 256 amino acid residues with a 24-amino acid signal peptide. There were one putative TATA box and six possible CAAT boxes lying in the 5’-upstream region of ppa. The ppa showed significant similarity at the nucleic acid level with genes encoding mannose-binding lectins from other Araceae species such as Pinellia ternata, Arisaema heterophyllum, Colocasia… More >

ZHONGHAI CHEN¹, YONGZHEN PANG¹, XIAOJUN LIU¹, XINGLONG WANG¹, ZHONGXIANG DENG¹, XIAOFEN SUN¹, KEXUAN TANG^1,2

BIOCELL, Vol.29, No.2, pp. 187-193, 2005, DOI:10.32604/biocell.2005.29.187

Abstract Using RNA extracted from Zantedeschia aethiopica young leaves and primers designed according to the conservative regions of Araceae lectins, the full-length cDNA of Z. aethiopica agglutinin (ZAA) was cloned by rapid amplification of cDNA ends (RACE). The full-length cDNA of zaa was 871 bp and contained a 417 bp open reading frame (ORF) encoding a lectin precursor of 138 amino acids. Through comparative analysis of zaa gene and its deduced amino acid sequence with those of other Araceae species, it was found that zaa encoded a precursor lectin with signal peptide. Secondary and three-dimensional structure analyses showed that ZAA had… More >