title: A novel matrix metalloproteinase gene (XMMP) encoding vitronectin-like motifs is transiently expressed in Xenopus laevis early embryo development.
abstract: To study the role of matrix metalloproteinases (MMPs) in early vertebrate development, we cloned cDNAs for six different MMPs from the frog Xenopus laevis embryos at different stages of development and describe here a novel MMP called XMMP. Xenopus XMMP has 604 amino acids including a putative signal peptide of 22 residues. At the carboxyl-terminal end of the propeptide, XMMP has a 37-amino acid-long insertion domain containing a segment that is 38% identical with a rat vitronectin sequence between residues 108-135. Following this domain is an RRKR motif, a putative cleavage site for intracellular activation by furin proteinases. XMMP lacks a proline-rich linker peptide, or hinge region, typically found in other MMPs between the catalytic domain and carboxyl-terminal "hemopexin/vitronectin-like" domain. In XMMP, the carboxyl-terminal domain is composed of four tandem repeats that are 21-33% identical to a sequence (residues 213-264) encoded by vitronectin exon-5. Interestingly, XMMP gene is transiently expressed during Xenopus embryo development. XMMP mRNA of 3.0 kilobase pairs was undetected in the blastula stage embryo, induced in gastrula embryo, expressed in neurula embryo, and then down-regulated in pretailbud embryo. In comparison, other Xenopus MMP genes that we have cloned show a different developmental regulation. In blastula embryo, the only MMP gene expressed was found to be 92-kDa type IV collagenase, which was also expressed in the gastrula, neurula, and pretailbud embryos. Expression of stromelysin-1, stromelysin-3, and two different membrane type-MMPs was first detected in the neurula and pretailbud embryos. These results suggest that MMPs and the novel XMMP reported here play a role in Xenopus early development.
authors.affiliation: Center for Molecular Medicine and Genetics, and Department of Pathology, Wayne State University School of Medicine, Detroit, Michigan 48202, USA.
authors.forename: M
authors.initials: M
authors.lastname: Yang
authors.forename: M T
authors.initials: MT
authors.lastname: Murray
authors.forename: M
authors.initials: M
authors.lastname: Kurkinen
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D015152:Blotting, Northern; D003001:Cloning, Molecular; D017124:Conserved Sequence; D045683:Furin; D005775:Gastrula / Q000201:enzymology; D018507:Gene Expression Regulation, Developmental; D008666:Metalloendopeptidases / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics*; D008969:Molecular Sequence Data; D016133:Polymerase Chain Reaction; D021382:Protein Sorting Signals / Q000737:chemistry / Q000235:genetics; D012333:RNA, Messenger / Q000378:metabolism; D011898:Ranidae; D051381:Rats; D016415:Sequence Alignment; D013381:Subtilisins / Q000378:metabolism; D019096:Vitronectin / Q000737:chemistry* / Q000235:genetics; D029867:Xenopus Proteins; D014982:Xenopus laevis / Q000196:embryology*
chemical_list: D021382:Protein Sorting Signals; D012333:RNA, Messenger; D019096:Vitronectin; D029867:Xenopus Proteins; D013381:Subtilisins; D045683:Furin; D008666:Metalloendopeptidases; C106346:XMMP protein, Xenopus