ABSTRACT
A new mouse cysteine protease, termed cathepsin R, has been identified. The complete nucleotide sequence of this gene was derived from a set of cDNAs generated from 15.5-day mouse placenta. Sequence analysis revealed an open reading frame encoding a 334 amino acid long polypeptide closely related to placentally expressed cathepsins P, Q, and M. RT-PCR analysis indicated that cathepsin R is only expressed in placenta and thus is a new member of the emerging family of cathepsins whose expression is regulated during mouse embryonic development. Modeling and structural analysis suggests that cathepsin R will have a restricted substrate specificity when compared to that of cathepsin L.
Subject(s)
Placenta/enzymology , Serine Endopeptidases/genetics , Amino Acid Sequence , Animals , Base Sequence , Cysteine Endopeptidases/chemistry , Cysteine Endopeptidases/genetics , DNA, Complementary/analysis , Mice , Models, Molecular , Molecular Sequence Data , Polymerase Chain Reaction , Protein Conformation , Sequence Homology, Amino Acid , Serine Endopeptidases/chemistry , Substrate SpecificityABSTRACT
The complete nucleotide sequence of a novel cathepsin cDNA derived from mouse placenta was determined and is termed cathepsin M. The predicted protein of 333 amino acid is a member of the family C1A proteases and is related to mouse cathepsins L and P. Mouse cathepsin M is highly expressed in placenta, whereas no detectable levels were found in lung, spleen, heart, brain, kidney, thymus, testicle, liver, or embryo. Phylogenic analyses of the sequences of human and mouse cathepsins show that cathepsin M is most closely related to cathepsins P and L. However, the differences are sufficiently large to indicate that the enzymes will be found in other species. This is in contrast to human cathepsins L and V, which probably resulted from a gene duplication after divergence of mammalian species.
Subject(s)
Cathepsins/genetics , Cysteine Endopeptidases/genetics , Endopeptidases , Placenta/enzymology , Amino Acid Sequence , Animals , Base Sequence , Binding Sites , Cathepsin K , Cathepsin L , DNA, Complementary/biosynthesis , DNA, Complementary/genetics , Evolution, Molecular , Lysosomes/enzymology , Mice , Molecular Sequence Data , RNA, Messenger/analysis , Reverse Transcriptase Polymerase Chain Reaction , Sequence AlignmentABSTRACT
The complete nucleotide sequence of a novel cathepsin cDNA derived from rat placenta was determined and is termed cathepsin Q. The predicted protein of 343 amino acid is a member of the family C1A protease related to cathepsin L. Rat cathepsin Q and its mouse counterpart were found highly expressed in placenta, whereas no detectable levels were found in lung, spleen, heart, brain, kidney, thymus, testicle, liver, or embryonic tissues. It is predicted that cathepsin Q will differ in catalytic specificity to another placental-specific protease, cathepsin P, indicating that these enzymes will have unique proteolytic functions in extra-embryonic tissues.
Subject(s)
Cathepsins/genetics , Cathepsins/metabolism , Cysteine Endopeptidases/genetics , Cysteine Endopeptidases/metabolism , Placenta/enzymology , Amino Acid Sequence , Animals , Base Sequence , Cathepsin K , Cathepsins/chemistry , Conserved Sequence , Cysteine Endopeptidases/chemistry , Male , Mice , Molecular Sequence Data , Organ Specificity , RNA, Messenger/genetics , Rats , Sequence Alignment , Sequence Homology, Amino AcidABSTRACT
The complete cDNA nucleotide sequence of a novel cathepsin derived from mouse placenta, termed cathepsin P, was determined. mRNA for cathepsin P was expressed in placenta and at lower levels in visceral yolk sac, but could not be detected in a range of adult tissues. The expression pattern of this protease indicates that it probably plays an important role during implantation and fetal development.
