PMID- 10479448
OWN - NLM
STAT- MEDLINE
DCOM- 19991020
LR  - 20190523
IS  - 0012-1606 (Print)
IS  - 0012-1606 (Linking)
VI  - 213
IP  - 2
DP  - 1999 Sep 15
TI  - Mammalian BMP-1/Tolloid-related metalloproteinases, including novel family member
      mammalian Tolloid-like 2, have differential enzymatic activities and
      distributions of expression relevant to patterning and skeletogenesis.
PG  - 283-300
AB  - Vertebrate bone morphogenetic protein 1 (BMP-1) and Drosophila Tolloid (TLD) are 
      prototypes of a family of metalloproteases with important roles in various
      developmental events. BMP-1 affects morphogenesis, at least partly, via
      biosynthetic processing of fibrillar collagens, while TLD affects dorsal-ventral 
      patterning by releasing TGFbeta-like ligands from latent complexes with the
      secreted protein Short Gastrulation (SOG). Here, in a screen for additional
      mammalian members of this family of developmental proteases, we identify novel
      family member mammalian Tolloid-like 2 (mTLL-2) and compare enzymatic activities 
      and expression domains of all four known mammalian BMP-1/TLD-like proteases
      [BMP-1, mammalian Tolloid (mTLD), mammalian Tolloid-like 1 (mTLL-1), and mTLL-2].
      Despite high sequence similarities, distinct differences are shown in ability to 
      process fibrillar collagen precursors and to cleave Chordin, the vertebrate
      orthologue of SOG. As previously demonstrated for BMP-1 and mTLD, mTLL-1 is shown
      to specifically process procollagen C-propeptides at the physiologically relevant
      site, while mTLL-2 is shown to lack this activity. BMP-1 and mTLL-1 are shown to 
      cleave Chordin, at sites similar to procollagen C-propeptide cleavage sites, and 
      to counteract dorsalizing effects of Chordin upon overexpression in Xenopus
      embryos. Proteases mTLD and mTLL-2 do not cleave Chordin. Differences in
      enzymatic activities and expression domains of the four proteases suggest BMP-1
      as the major Chordin antagonist in early mammalian embryogenesis and in pre- and 
      postnatal skeletogenesis.
CI  - Copyright 1999 Academic Press.
FAU - Scott, I C
AU  - Scott IC
AD  - Department of Pathology and Laboratory Medicine, University of Wisconsin Medical 
      School, 1300 University Avenue, Madison, Wisconsin, 53706, USA.
FAU - Blitz, I L
AU  - Blitz IL
FAU - Pappano, W N
AU  - Pappano WN
FAU - Imamura, Y
AU  - Imamura Y
FAU - Clark, T G
AU  - Clark TG
FAU - Steiglitz, B M
AU  - Steiglitz BM
FAU - Thomas, C L
AU  - Thomas CL
FAU - Maas, S A
AU  - Maas SA
FAU - Takahara, K
AU  - Takahara K
FAU - Cho, K W
AU  - Cho KW
FAU - Greenspan, D S
AU  - Greenspan DS
LA  - eng
GR  - AR43621/AR/NIAMS NIH HHS/United States
GR  - GM46846/GM/NIGMS NIH HHS/United States
GR  - GM54704/GM/NIGMS NIH HHS/United States
GR  - etc.
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Dev Biol
JT  - Developmental biology
JID - 0372762
RN  - 0 (Bone Morphogenetic Proteins)
RN  - 0 (Drosophila Proteins)
RN  - 0 (Glycoproteins)
RN  - 0 (Insect Proteins)
RN  - 0 (Intercellular Signaling Peptides and Proteins)
RN  - 93586-27-7 (chordin)
RN  - EC 3.4.- (Tolloid-Like Metalloproteinases)
RN  - EC 3.4.- (tld protein, Drosophila)
RN  - EC 3.4.24.- (Metalloendopeptidases)
RN  - EC 3.4.24.- (TLL2 protein, human)
RN  - EC 3.4.24.- (Tll2 protein, mouse)
RN  - EC 3.4.24.19 (BMP1 protein, human)
RN  - EC 3.4.24.19 (Bmp1 protein, mouse)
RN  - EC 3.4.24.19 (Bone Morphogenetic Protein 1)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Body Patterning/genetics
MH  - Bone Morphogenetic Protein 1
MH  - Bone Morphogenetic Proteins/*genetics/metabolism
MH  - Bone and Bones/embryology/physiology
MH  - Cloning, Molecular
MH  - *Drosophila Proteins
MH  - Enzyme Activation
MH  - Glycoproteins/*metabolism
MH  - Humans
MH  - Insect Proteins/genetics/metabolism
MH  - *Intercellular Signaling Peptides and Proteins
MH  - Metalloendopeptidases/*genetics/metabolism
MH  - Mice
MH  - Molecular Sequence Data
MH  - Sequence Alignment
MH  - Tolloid-Like Metalloproteinases
EDAT- 1999/09/10 00:00
MHDA- 1999/09/10 00:01
CRDT- 1999/09/10 00:00
PHST- 1999/09/10 00:00 [pubmed]
PHST- 1999/09/10 00:01 [medline]
PHST- 1999/09/10 00:00 [entrez]
AID - 10.1006/dbio.1999.9383 [doi]
AID - S0012-1606(99)99383-1 [pii]
PST - ppublish
SO  - Dev Biol. 1999 Sep 15;213(2):283-300. doi: 10.1006/dbio.1999.9383.