Three alternatively spliced variants of the gene coding for the human bone morphogenetic protein-1

1998 ◽  
Vol 76 (2) ◽  
pp. 141-146 ◽  
Author(s):  
Michal Janitz ◽  
Volker Heiser ◽  
U. Böttcher ◽  
Olfert Landt ◽  
R. Lauster
Keyword(s):  
Bone Morphogenetic Protein ◽  
Human Bone ◽  
Morphogenetic Protein ◽  
Gene Coding ◽  
Human Bone Morphogenetic Protein ◽  
Alternatively Spliced ◽  
Bone Morphogenetic Protein 1

The Drosophila dorsal-ventral patterning gene tolloid is related to human bone morphogenetic protein 1

Cell ◽  
1991 ◽  
Vol 67 (3) ◽  
pp. 469-481 ◽  
Author(s):  
Mary Jane Shimell ◽  
Edwin L. Ferguson ◽  
Steven R. Childs ◽  
Michael B. O'Connor
Keyword(s):  
Bone Morphogenetic Protein ◽  
Human Bone ◽  
Morphogenetic Protein ◽  
Human Bone Morphogenetic Protein ◽  
Bone Morphogenetic Protein 1

Characterization of a homolog of human bone morphogenetic protein 1 in the embryo of the sea urchin, Strongylocentrotus purpuratus

Development ◽  
1994 ◽  
Vol 120 (3) ◽  
pp. 559-568 ◽  
Author(s):  
S.P. Hwang ◽  
J.S. Partin ◽  
W.J. Lennarz
Keyword(s):  
Bone Morphogenetic Protein ◽  
Sea Urchin ◽  
Sequence Similarity ◽  
Human Bone ◽  
Blastula Stage ◽  
Morphogenetic Protein ◽  
Sea Urchin Embryo ◽  
Human Bone Morphogenetic Protein ◽  
Maximal Expression ◽  
Bone Morphogenetic Protein 1

A cDNA clone encoding a protein homologous to human bone morphogenetic protein 1 (huBMP1) was isolated from a sea urchin embryo cDNA library. This sea urchin gene, named suBMP, encodes a protein of M(r) of 72 × 10(3). The deduced amino acid sequence of suBMP shares 72% sequence similarity (55% identity) with that of huBMP1. Like huBMP1 it also contains an N-terminal metalloendoprotease domain that shares sequence similarity with the astacin protease from crayfish, a C-terminal domain that is similar to the repeat domain found in C1r or C1s serine proteases, and an EGF-like segment. Although suBMP mRNA was detectable at a low level in the unfertilized egg, maximal expression of mRNA was observed at hatched blastula stage, with only a modest decrease in level at later stages of development. In situ hybridization studies revealed that suBMP mRNA is found in both ectodermal and primary mesenchyme cells in hatched blastula-stage embryos. Maximal expression of suBMP was observed at mesenchyme blastula, just before the onset of primitive skeleton (spicule) formation. SuBMP was found by immunoelectronmicroscopy in all cell types in late gastrula stage embryos. The antibody gold particles appeared in small clusters in the cytoplasm, on the surface of the cells and within the blastocoel. This distribution of suBMP, coupled with the finding that it was associated with membranes but was released by sodium carbonate treatment, suggests that the protein is secreted, and subsequently associates with a cell surface component. Two models for the possible function of suBMP in spiculogenesis in the sea urchin embryo are discussed.

Human Bone Morphogenetic Protein-1-3 (BMP-1-3) and BMP-6 synergistically influence bone healing

Bone ◽  
2009 ◽  
Vol 44 ◽  
pp. S309-S310
Author(s):  
L. Grgurevic ◽  
I. Erjavec ◽  
G. Bicanic ◽  
M. Lipar ◽  
M. Jelic ◽  
...  
Keyword(s):  
Bone Morphogenetic Protein ◽  
Bone Healing ◽  
Human Bone ◽  
Morphogenetic Protein ◽  
Human Bone Morphogenetic Protein ◽  
Bone Morphogenetic Protein 1

Study on Hollow Hydroxyapatite Microspheres as Delivery System for Human Bone Morphogenetic Protein

2011 ◽  
Vol 26 (9) ◽  
pp. 974-978
Author(s):  
Ai-Hua YAO ◽  
Wei XU ◽  
Fan-Rong AI ◽  
Qi CHEN ◽  
De-Ping WANG ◽  
...  
Keyword(s):  
Bone Morphogenetic Protein ◽  
Delivery System ◽  
Human Bone ◽  
Morphogenetic Protein ◽  
Human Bone Morphogenetic Protein
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