{'fraction_non_alphanumeric': 0.03419316136772645, 'fraction_numerical': 0.0065986802639472104, 'mean_word_length': 5.808163265306122, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Burn control, an adipocyte-specific function for galectin-12

Families of molecules often have similar functions—think of kinases, transcription factors, chemokines, or Toll-like receptors. The galectins, an evolutionarily ancient family of carbohydrate binding proteins found in organisms from multicellular fungi to humans, are different (1, 2). Galectins are a family of lectins; the family designation is based on highly conserved structural features, particularly the conserved carbohydrate recognition domains (CRDs) that define the proteins as lectins. In contrast, the pleiotropic functions of galectins do not seem to be conserved. Based on the cell type investigated, galectins have been reported to regulate cell proliferation, migration, adhesion, differentiation, survival, and death, and they also positively and negatively regulate host defense against microbial pathogens. Extracellular functions of galectins typically depend on the carbohydrate binding properties of the lectins, but many different glycoprotein receptors can be recognized by various galectins if the glycoprotein receptors bear the appropriate glycan ligands, resulting in the vast array of cellular functions triggered by galectin binding. In addition, galectins are also found intracellularly, where for example, protein–protein interactions at the cytoplasmic face of the plasma membrane, nucleus, and mitochondria promote association of galectin-3 with K-Ras, β-catenin, and Bcl-2 family members to regulate oncogenesis and cell death (3–5). In PNAS, the work by Yang et al. (6) reports an unexpected function for a galectin, galectin-12, at an unexpected subcellular location.