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1.
J Biol Chem ; 275(47): 36934-41, 2000 Nov 24.
Article in English | MEDLINE | ID: mdl-10967093

ABSTRACT

We identified a novel gene of Drosophila melanogaster, Male-specific IDGF (MSI), encoding a transmembrane signaling molecule with exclusive expression in the testis. This molecule (MSI) contains a single transmembrane domain and has 35% amino acid identity with insect-derived growth factor (IDGF), a soluble growth factor for embryonic cells of the flesh fly, Sarcophaga peregrina. When MSI was exogenously expressed in Schneiders's line 2 cells, it was shown to be localized on the cell surface and exhibits growth factor activity, suggesting that MSI is a membrane-bound extracellular signaling molecule. Gene expression studies revealed that MSI mRNA was restricted to mature primary spermatocytes, whereas MSI was detected in the cells at the later developmental stages. Analysis using four meiotic arrest mutants, aly, can, mia, and sa suggested that MSI is involved in spermiogenesis, the final differentiation step of spermatogenesis. These results suggest that MSI is an extracellular signaling molecule participating in spermatogenesis and is a new member of the IDGF family.


Subject(s)
Drosophila Proteins , Drosophila melanogaster/genetics , Membrane Proteins/genetics , Testis/chemistry , Amino Acid Sequence , Animals , Aplysia , Base Sequence , Cells, Cultured , Gene Expression , Male , Molecular Sequence Data , RNA, Messenger/metabolism , Spermatocytes/metabolism , Testis/metabolism
2.
J Biochem ; 128(3): 539-42, 2000 Sep.
Article in English | MEDLINE | ID: mdl-10965055

ABSTRACT

Previously, we identified two proteins with molecular masses of 200 and 210 kDa in basement membranes of Sarcophaga imaginal discs as substrates for cathepsin L [Homma, K. and Natori, S. (1996) Eur. J. Biochem. 240, 443-447]. Here we demonstrated that the same proteins were also present in the basement membranes of larval brains. These proteins were suggested to be digested by cathepsin L secreted from the larval brains in response to 20-HE. From the behavior of these proteins during metamorphosis, we concluded that the basement membranes of larval brains are degraded at the early pupal stage and synthesized again at the late pupal stage, coinciding with the timing of brain remodeling that takes place during metamorphosis. Possibly, the transient disappearance of the basement membranes makes brain remodeling easier, and cathepsin L is suggested to play a crucial role in the degradation of the basement membranes.


Subject(s)
Brain/metabolism , Cathepsins/metabolism , Diptera/physiology , Endopeptidases , Enzyme Precursors/metabolism , Insect Proteins/biosynthesis , Membrane Proteins/biosynthesis , Metamorphosis, Biological , Animals , Basement Membrane/metabolism , Blotting, Western , Cathepsin L , Cell Differentiation , Cysteine Endopeptidases , Ecdysterone/pharmacology , Fluorescent Antibody Technique , Hydrolysis , Larva/metabolism
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