Disease relevance of Lsp1gamma

• We have isolated chromosomal segments of D. melanogaster DNA that encode the alpha, beta and gamma polypeptides of the major larval serum protein (LSP1) from libraries of recombinant phage [1].

High impact information on Lsp1gamma

• Assays of CAT activity in the homogenates of dissected tissues indicated that the genes are only expressed in the fat body, as are the endogenous LSP1 genes [2].
• Expression of the prokaryotic gene for chloramphenicol acetyl transferase in Drosophila under the control of larval serum protein 1 gene promoters [2].
• We have linked the protein coding region of the prokaryotic gene for chloramphenicol acetyl transferase (CAT) to the promoter region of the Drosophila genes for larval serum protein 1 (LSP1) [2].
• We have determined the nucleotide sequence at the 5' ends of the genes for the alpha, beta and gamma polypeptides of larval serum protein 1 (LSP1) of Drosophila melanogaster [3].
• CAT expression occurs in approximately 1% of the cultured cells following transfection and the accumulation of protein is maximal three to four days after transfection; and it is dependent upon the presence of the LSP1 sequences [2].

Biological context of Lsp1gamma

• In the Drosophila melanogaster genome, three Larval serum protein 1 (Lsp1) genes (alpha, beta and gamma) are present and each of them is located on a different chromosome, suggesting multiple transposition events [4].
• Taken together these data indicate that the 1.65 X 10(3) and 2.25 X 10(3) base segments of DNA upstream from the LSP1 alpha and LSP1 beta genes contain cis-acting regulatory elements necessary for correct tissue and temporal specificity of LSP1 gene expression [2].
• The results obtained demonstrate that the LSP-1 subunit genes are present in equal copies in the genome [5].
• Short intervening sequences close to the 5' ends of the three Drosophila larval serum protein 1 genes [6].
• A family of genes coding for larval serum proteins do not respond similarly in trisomies, suggesting that regulation operates on a process which is not common to their coordinate regulation [7].

Anatomical context of Lsp1gamma

• At the end of the third larval instar of Drosophila melanogaster, larval serum proteins 1 and 2 (LSP-1 and -2) are taken up by cells of the fat body [8].

Associations of Lsp1gamma with chemical compounds

• Two-dimensional peptide mapping of the methionine-containing tryptic peptides showed that half of these peptides are common to all four larval serum protein subunits, and that about two-thirds are common to the three LSP-1 subunits [9].

Other interactions of Lsp1gamma

• The same chromosomal localization and genomic organization, different from that of D. melanogaster, is found in both species for the Lsp1beta and Lsp1gamma genes [4].
• Proteins 9, 10, 11, and 15 correspond to the LSP-1 gamma, beta, and alpha triplet and LSP-2 polypeptide in D. melanogaster [10].

Analytical, diagnostic and therapeutic context of Lsp1gamma

• The molecular cloning of a dispersed set of developmentally regulated genes which encode the major larval serum protein of D. melanogaster [1].
• Northern blots indicate that CAT transcripts are found only in the fat body but their abundance is an order of magnitude lower than endogenous LSP1 transcripts [2].
• Regulation of synthesis of larval serum proteins after transplantation of larval fat body into adult Drosophila melanogaster [11].
• Comparison of the larval serum proteins of Drosophila melanogaster using one and two-dimensional peptide mapping [9].
• We demonstrated by immunoblotting and pulse-labeled experiments followed by 2D SDS-PAGE that these protein bands which constitute the larval serum proteins were internalized into the haemocytes from the serum [12].

References