Fatty-acid-binding protein in locust flight muscle. Developmental changes of expression, concentration and intracellular distribution

Eur J Biochem. 1992 Dec 15;210(3):1045-51. doi: 10.1111/j.1432-1033.1992.tb17510.x.

Abstract

Fatty-acid-binding protein (FABP) from the flight muscle of the locust, Schistocerca gregaria, is similar to mammalian heart FABP in its primary structure and biochemical characteristics. We have studied developmental changes using enzyme-linked immunosorbent assays, RNA hybridization and electron microscopy of immunogold-labeled sections. Locust muscle FABP is the most abundant soluble muscle protein in fully developed adult locusts, comprising 18% of the total cytosolic protein. At the beginning of the adult stage, however, no FABP is detectable. Its concentration rises during the following 10 days, after which it reaches its maximal value. FABP mRNA is present shortly after adult ecdysis; its concentration increases for 10 days, before it diminishes and reaches a constant, low level, probably needed to maintain the established FABP level. The protein is abundant in cytosol and nuclei, but virtually absent in mitochondria.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Blotting, Northern
  • Carrier Proteins / genetics
  • Carrier Proteins / isolation & purification
  • Carrier Proteins / metabolism*
  • DNA Probes
  • Enzyme-Linked Immunosorbent Assay
  • Fatty Acid-Binding Proteins
  • Fatty Acids / metabolism
  • Flight, Animal
  • Grasshoppers / metabolism*
  • Microscopy, Immunoelectron
  • Mitochondria, Muscle / metabolism*
  • Mitochondria, Muscle / ultrastructure
  • Muscle Development
  • Muscles / metabolism*
  • Neoplasm Proteins*
  • Polymerase Chain Reaction
  • RNA / genetics
  • RNA / isolation & purification
  • RNA, Messenger / metabolism
  • Subcellular Fractions / metabolism

Substances

  • Carrier Proteins
  • DNA Probes
  • Fatty Acid-Binding Proteins
  • Fatty Acids
  • Neoplasm Proteins
  • RNA, Messenger
  • RNA