Developmental changes of FABP concentration, expression, and intracellular distribution in locust flight muscle.
M-FABP from flight muscle of the locust, Schistocerca gregaria, is similar to mammalian H-FABP in its physical characteristics and amino acid sequence. We have studied developmental changes using ELISA, Northern Blotting, and EM/immuno-gold techniques. M-FABP is found in cytoplasm and nuclei, but not in mitochondria. It is the most abundant soluble muscle protein in fully developed adult locusts, comprising 18% of the total cytosolic protein. However, no FABP is detectable at the beginning of the adult stage. Its concentration rises dramatically during the next 10 days, after which it reaches its maximal value. Expression apparently is turned on after ecdysis and continues for 10 days; thereafter, FABP mRNA diminishes and reaches a constant, but low level, probably needed to maintain the current FABP level. From a series of experiments employing metamorphosis-controlling hormones and antihormones it is evident that the induction of FABP expression is directly linked to metamorphosis.
Haunerland
N H
NH
Department of Biological Sciences, Simon Fraser University, Burnaby, B.C., Canada.
Chen
X
X
Andolfatto
P
P
Chisholm
J M
JM
Wang
Z
Z
D000818:Animals; D002352:Carrier Proteins / Q000096:biosynthesis / Q000378:metabolism*; D004797:Enzyme-Linked Immunosorbent Assay; D050556:Fatty Acid-Binding Proteins; D005227:Fatty Acids / Q000378:metabolism*; D006110:Grasshoppers; D007150:Immunohistochemistry; D024510:Muscle Development; D009132:Muscles / Q000378:metabolism* / Q000648:ultrastructure; D009363:Neoplasm Proteins
D002352:Carrier Proteins; D050556:Fatty Acid-Binding Proteins; D005227:Fatty Acids; D009363:Neoplasm Proteins