TY - JOUR
T1 - Molecular characterization of hypoxia inducible factor-1 (HIF-1) from the white shrimp Litopenaeus vannamei and tissue-specific expression under hypoxia
AU - Soñanez-Organis, J.G.
AU - Peregrino-Uriarte, A.B.
AU - Gómez-Jiménez, S.
AU - López-Zavala, A.
AU - Forman, H.J.
AU - Yepiz-Plascencia, G.
N1 - Funding Information:
We are grateful to Consejo Nacional de Ciencia y Tecnología (CONACYT, Mexico) for financial support, grants 45964 and 98507 and UC-MEXUS-CONACYT for a grant to GYP and HJF. JGSO was a recipient of a fellowship from CONACYT for graduate studies.
PY - 2009
Y1 - 2009
N2 - 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.
AB - 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.
KW - Anaerobic metabolism
KW - Crustaceans
KW - Glycolysis
KW - Hypoxia
KW - Hypoxia inducible factor 1 (HIF-1)
UR - http://www.scopus.com/inward/record.url?eid=2-s2.0-67651008226&partnerID=MN8TOARS
U2 - 10.1016/j.cbpc.2009.06.005
DO - 10.1016/j.cbpc.2009.06.005
M3 - Artículo
SN - 1532-0456
VL - 150
SP - 395
EP - 405
JO - Comparative Biochemistry and Physiology - C Toxicology and Pharmacology
JF - Comparative Biochemistry and Physiology - C Toxicology and Pharmacology
IS - 3
ER -