Interaction of the anterior fat body protein with the hexamerin receptor in the blowfly Calliphora vicina.
In late larvae of the blowfly, Calliphora vicina, arylphorin and LSP-2 proteins, which belong to the class of hexamerins, are selectively taken up by the fat body from the haemolymph. Hexamerin endocytosis is mediated by a specific membrane-bound receptor, the arylphorin-binding protein (ABP). Using the two-hybrid technique, we found that the anterior fat body protein (AFP) interacts with the hexamerin receptor. AFP, a homologue of the mammalian calcium-binding liver protein regucalcin (senescence marker protein-30), exhibits a strong binding affinity for a naturally occurring C-terminal cleavage fragment of the hexamerin receptor precursor (the P30 peptide) and other receptor cleavage products that contain P30. Expression of AFP mRNA and protein is restricted to the anterior part of the fat body tissue and to haemocytes in last-instar larvae. AFP mRNA occurs in all postembryonic developmental stages. Our results suggest that AFP plays a role in the regulation of hexamerin uptake by fat body cells along the anterior-posterior axis.
Hansen
Immo A
IA
Department of Cell and Developmental Biology, Biocenter of the University, Würzburg, Germany. i.hansen@medizin.uni-wuerzburg.de
Meyer
Susanne R
SR
Schäfer
Ingo
I
Scheller
Klaus
K
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002352:Carrier Proteins / Q000235:genetics / Q000378:metabolism*; D018076:DNA, Complementary; D004175:Diptera / Q000378:metabolism*; D005216:Fat Body / Q000378:metabolism; D019476:Insect Proteins / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D009928:Organ Specificity; D011233:Precipitin Tests; D017422:Sequence Analysis, DNA; D020798:Two-Hybrid System Techniques
C412405:AFP protein, Sarcophaga peregrina; D002352:Carrier Proteins; D018076:DNA, Complementary; D019476:Insect Proteins; C092382:arylphorin-binding proteins, insect