Molecular cloning and mRNA tissue distribution of a novel matrix metalloproteinase isolated from porcine enamel organ

作者: John D. Bartlett , James P. Simmer , Jun Xue , Henry C. Margolis , Edgard C. Moreno

DOI: 10.1016/S0378-1119(96)00525-2

关键词: Molecular biologyMMP20Open reading frameCollagenaseMolecular cloningcDNA libraryNorthern blotBiologyComplementary DNAEnamel organ

摘要: A cDNA encoding a novel matrix metalloproteinase (MMP) was isolated from porcine enamel organ-specific library. Multiple tissue northern blot analysis revealed the presence of two mRNA transcripts which were expressed only in organ. The 1968 bp or 3420 length and resulted utilization alternative polyadenylation sites. open reading frame cloned encodes protein composed 483 amino acids. MMP has predicted molecular mass 54.1 kDa, is similar to that stromelysins collagenases, although it not member either these classes MMPs. motif does contain consensus hemopexin-like domain because lacks critical tryptophan proline residue at appropriate positions. Since new gene family its expression appears limited organ, we have named enamelysin.

参考文章(29)
Harald Tschesche, [26] Human neutrophil collagenase Proteolytic Enzymes: Aspartic and Metallo Peptidases. ,vol. 248, pp. 431- 449 ,(1995) , 10.1016/0076-6879(95)48028-5
K A Hasty, T F Pourmotabbed, G I Goldberg, J P Thompson, D G Spinella, R M Stevens, C L Mainardi, Human neutrophil collagenase : a distinct gene product with homology to other matrix metalloproteinases Journal of Biological Chemistry. ,vol. 265, pp. 11421- 11424 ,(1990) , 10.1016/S0021-9258(19)38413-3
S.D. Shapiro, D.K. Kobayashi, T.J. Ley, Cloning and characterization of a unique elastolytic metalloproteinase produced by human alveolar macrophages. Journal of Biological Chemistry. ,vol. 268, pp. 23824- 23829 ,(1993) , 10.1016/S0021-9258(20)80459-1
S.D. Shapiro, G.L. Griffin, D.J. Gilbert, N.A. Jenkins, N.G. Copeland, H.G. Welgus, R.M. Senior, T.J. Ley, Molecular cloning, chromosomal localization, and bacterial expression of a murine macrophage metalloelastase. Journal of Biological Chemistry. ,vol. 267, pp. 4664- 4671 ,(1992) , 10.1016/S0021-9258(18)42885-2
G I Goldberg, S M Wilhelm, A Kronberger, E A Bauer, G A Grant, A Z Eisen, Human fibroblast collagenase. Complete primary structure and homology to an oncogene transformation-induced rat protein. Journal of Biological Chemistry. ,vol. 261, pp. 6600- 6605 ,(1986) , 10.1016/S0021-9258(19)84605-7
I E Collier, S M Wilhelm, A Z Eisen, B L Marmer, G A Grant, J L Seltzer, A Kronberger, C S He, E A Bauer, G I Goldberg, H-ras oncogene-transformed human bronchial epithelial cells (TBE-1) secrete a single metalloprotease capable of degrading basement membrane collagen. Journal of Biological Chemistry. ,vol. 263, pp. 6579- 6587 ,(1988) , 10.1016/S0021-9258(18)68680-6
Jose M Freije, Irene Diez-Itza, Milagros Balbín, Luis M Sánchez, Rafael Blasco, Jorge Tolivia, Carlos López-Otín, Molecular cloning and expression of collagenase-3, a novel human matrix metalloproteinase produced by breast carcinomas. Journal of Biological Chemistry. ,vol. 269, pp. 16766- 16773 ,(1994) , 10.1016/S0021-9258(19)89457-7
S M Wilhelm, I E Collier, B L Marmer, A Z Eisen, G A Grant, G I Goldberg, SV40-transformed human lung fibroblasts secrete a 92-kDa type IV collagenase which is identical to that secreted by normal human macrophages. Journal of Biological Chemistry. ,vol. 264, pp. 17213- 17221 ,(1989) , 10.1016/S0021-9258(18)71480-4
H. Birkedal-Hansen, W.G.I. Moore, M.K. Bodden, L.J. Windsor, B. Birkedal-Hansen, A. DeCarlo, J.A. Engler, Matrix Metalloproteinases: A Review Critical Reviews in Oral Biology & Medicine. ,vol. 4, pp. 197- 250 ,(1993) , 10.1177/10454411930040020401