Molecular characterization of hypoxia inducible factor-1 (HIF-1) from the white shrimp Litopenaeus vannamei and tissue-specific expression under hypoxia

• Published in: Comparative biochemistry and physiology. Toxicology & pharmacology Vol. 150; no. 3; pp. 395 - 405
• Main Authors: Soñanez-Organis, José G., Peregrino-Uriarte, Alma B., Gómez-Jiménez, Silvia, López-Zavala, Alonso, Forman, Henry Jay, Yepiz-Plascencia, Gloria
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.09.2009
• Subjects: Amino Acid Sequence; Anaerobic metabolism; Animals; Aryl Hydrocarbon Receptor Nuclear Translocator - genetics; Base Sequence; Crustaceans; Decapoda; DNA, Complementary - chemistry; Gills - metabolism; Glycolysis; Hepatopancreas - metabolism; Hypoxia; Hypoxia - metabolism; Hypoxia inducible factor 1 (HIF-1); Hypoxia-Inducible Factor 1 - genetics; Hypoxia-Inducible Factor 1 - metabolism; Hypoxia-Inducible Factor 1, alpha Subunit - genetics; Litopenaeus vannamei; Marine; Molecular Sequence Data; Penaeidae - genetics; Penaeidae - metabolism; Phylogeny; Glycolysis; Hypoxia; Anaerobic metabolism; Crustaceans; Hypoxia inducible factor 1 (HIF-1)
• ISSN: 1532-0456; 1878-1659
• DOI: 10.1016/j.cbpc.2009.06.005

Hypoxia inducible factor 1 (HIF-1) is a key transcription factor that regulates a variety of molecular responses to hypoxia. Some marine crustaceans experience changes of oxygen tension in their aquatic environment, but knowledge about the function and expression of HIF-1 is very limited. HIF-1 is a heterodimer composed by α and β subunits. We report the complete cDNA sequences of HIF-1α and HIF-1β from the white shrimp Litopenaeus vannamei. HIF-1α ( LvHIF-1α) is 3672 bp and codes for 1050 amino acids, while HIF-1β is 2135 bp ( LvHIF-1β) and 608 amino acids. Both, the α and β subunits have the helix-loop-helix (bHLH) and PAS domains. HIF-1α also has the oxygen dependent degradation (ODD) and the C-terminal transactivation domain (C-TAD), important for regulation in normoxia. Phylogenetic analyses of the proteins indicate separation of invertebrates from vertebrates. Large differences of HIF-1α and HIF-1β transcripts abundance were detected in gills, hepatopancreas and muscle under normoxia (6 mg/L dissolved oxygen, DO) and hypoxia (2.5 and 1.5 mg/L DO). HIF-1α was more abundant in gills and HIF-1β in hepatopancreas. Large changes in response to hypoxia were detected for HIF-1α in gills, while HIF-1β remained fairly constant. Glucose and lactate in hemolymph increased rapidly in hypoxia in all cases and up to 4.7 and 5.0-fold, respectively, in response to 1.5 mg/L DO for 1 h.