TY - JOUR
T1 - Localization of osteogenic protein-1 (bone morphogenetic protein-7) during human embryonic development
T2 - High affinity binding to basement membranes
AU - Vukicevic, Slobodan
AU - Latin, Visnja
AU - Chen, ping
AU - Batorsky, Roberta
AU - Reddi, A. H.
PY - 1994/1/31
Y1 - 1994/1/31
N2 - Osteogenic protein-1 (OP-1) is a member of the bone morphogenetic protein subfamily of the transforming growth factor-beta (TGF-β) superfamily. Since members of the TGF-β superfamily have a role in tissue development the distribution of OP-1 in developing human embryos (gestational age 5-14 weeks) was examined by immunohistochemical methods. Positive staining for OP-1 was observed in: sclerotome, hypertrophied chondrocytes, osteoblasts, periosteum, epithelial cells of the adrenal “provisional cortex” and the convoluted tubules of developing kidneys. In the developing lungs, pancreas and skin, OP-1 was localized in basement membranes underlying the epitheliurn. In vitro binding studies of 125I-OP-1 to various extracellular matrix components revealed high affinity of OP-1 for type IV collagen and less for heparin, collagen types I and VI. Present findings suggest that, in addition to bone formation, OP-1 could have other important regulatory roles in human embryogenesis with high binding affinity to a basement membrane component.
AB - Osteogenic protein-1 (OP-1) is a member of the bone morphogenetic protein subfamily of the transforming growth factor-beta (TGF-β) superfamily. Since members of the TGF-β superfamily have a role in tissue development the distribution of OP-1 in developing human embryos (gestational age 5-14 weeks) was examined by immunohistochemical methods. Positive staining for OP-1 was observed in: sclerotome, hypertrophied chondrocytes, osteoblasts, periosteum, epithelial cells of the adrenal “provisional cortex” and the convoluted tubules of developing kidneys. In the developing lungs, pancreas and skin, OP-1 was localized in basement membranes underlying the epitheliurn. In vitro binding studies of 125I-OP-1 to various extracellular matrix components revealed high affinity of OP-1 for type IV collagen and less for heparin, collagen types I and VI. Present findings suggest that, in addition to bone formation, OP-1 could have other important regulatory roles in human embryogenesis with high binding affinity to a basement membrane component.
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U2 - 10.1006/bbrc.1994.1100
DO - 10.1006/bbrc.1994.1100
M3 - Article
C2 - 8297380
AN - SCOPUS:0028306248
SN - 0006-291X
VL - 198
SP - 693
EP - 700
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 2
ER -