ADAM 12-S cleaves IGFBP-3 and IGFBP-5 and is inhibited by TIMP-3.

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Standard

ADAM 12-S cleaves IGFBP-3 and IGFBP-5 and is inhibited by TIMP-3. / Loechel, F; Fox, J W; Murphy, G; Albrechtsen, R; Wewer, U M.

I: Biochemical and Biophysical Research Communications, Bind 278, Nr. 3, 2000, s. 511-5.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Loechel, F, Fox, JW, Murphy, G, Albrechtsen, R & Wewer, UM 2000, 'ADAM 12-S cleaves IGFBP-3 and IGFBP-5 and is inhibited by TIMP-3.', Biochemical and Biophysical Research Communications, bind 278, nr. 3, s. 511-5. https://doi.org/10.1006/bbrc.2000.3835

APA

Loechel, F., Fox, J. W., Murphy, G., Albrechtsen, R., & Wewer, U. M. (2000). ADAM 12-S cleaves IGFBP-3 and IGFBP-5 and is inhibited by TIMP-3. Biochemical and Biophysical Research Communications, 278(3), 511-5. https://doi.org/10.1006/bbrc.2000.3835

Vancouver

Loechel F, Fox JW, Murphy G, Albrechtsen R, Wewer UM. ADAM 12-S cleaves IGFBP-3 and IGFBP-5 and is inhibited by TIMP-3. Biochemical and Biophysical Research Communications. 2000;278(3):511-5. https://doi.org/10.1006/bbrc.2000.3835

Author

Loechel, F ; Fox, J W ; Murphy, G ; Albrechtsen, R ; Wewer, U M. / ADAM 12-S cleaves IGFBP-3 and IGFBP-5 and is inhibited by TIMP-3. I: Biochemical and Biophysical Research Communications. 2000 ; Bind 278, Nr. 3. s. 511-5.

Bibtex

@article{3fdfd4405c7711dd8d9f000ea68e967b,
title = "ADAM 12-S cleaves IGFBP-3 and IGFBP-5 and is inhibited by TIMP-3.",
abstract = "ADAMs are a family of multidomain proteins having proteolytic and cell adhesion activities. We have previously shown that ADAM 12-S, the secreted soluble form of human ADAM 12, is a catalytically active protease. We now describe the purification of full-length recombinant ADAM 12-S and demonstrate that it cleaves insulin-like growth factor binding protein-3 (IGFBP-3). This result supports a role for ADAM 12-S in the degradation of IGFBP-3 in the blood of pregnant women. Furthermore, we tested for proteolysis of other members of the IGF binding protein family and found that ADAM 12-S cleaves IGFBP-5 in addition to IGFBP-3, but does not cleave IGFBP-1, -2, -4, or -6. ADAM 12-S may therefore be the IGFBP-5 protease that is secreted by osteoblasts and other cells. Cleavage of both IGFBP-3 and -5 by ADAM 12-S was inhibited by TIMP-3, raising the possibility that TIMP-3 is a physiological inhibitor of ADAM 12-S.",
author = "F Loechel and Fox, {J W} and G Murphy and R Albrechtsen and Wewer, {U M}",
note = "Keywords: ADAM Proteins; Amino Acid Sequence; Disintegrins; Female; Humans; Insulin-Like Growth Factor Binding Protein 1; Insulin-Like Growth Factor Binding Protein 3; Insulin-Like Growth Factor Binding Protein 5; Membrane Proteins; Metalloendopeptidases; Peptide Fragments; Pregnancy; Recombinant Proteins; Substrate Specificity; Tissue Inhibitor of Metalloproteinase-3",
year = "2000",
doi = "10.1006/bbrc.2000.3835",
language = "English",
volume = "278",
pages = "511--5",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Elsevier",
number = "3",

}

RIS

TY - JOUR

T1 - ADAM 12-S cleaves IGFBP-3 and IGFBP-5 and is inhibited by TIMP-3.

AU - Loechel, F

AU - Fox, J W

AU - Murphy, G

AU - Albrechtsen, R

AU - Wewer, U M

N1 - Keywords: ADAM Proteins; Amino Acid Sequence; Disintegrins; Female; Humans; Insulin-Like Growth Factor Binding Protein 1; Insulin-Like Growth Factor Binding Protein 3; Insulin-Like Growth Factor Binding Protein 5; Membrane Proteins; Metalloendopeptidases; Peptide Fragments; Pregnancy; Recombinant Proteins; Substrate Specificity; Tissue Inhibitor of Metalloproteinase-3

PY - 2000

Y1 - 2000

N2 - ADAMs are a family of multidomain proteins having proteolytic and cell adhesion activities. We have previously shown that ADAM 12-S, the secreted soluble form of human ADAM 12, is a catalytically active protease. We now describe the purification of full-length recombinant ADAM 12-S and demonstrate that it cleaves insulin-like growth factor binding protein-3 (IGFBP-3). This result supports a role for ADAM 12-S in the degradation of IGFBP-3 in the blood of pregnant women. Furthermore, we tested for proteolysis of other members of the IGF binding protein family and found that ADAM 12-S cleaves IGFBP-5 in addition to IGFBP-3, but does not cleave IGFBP-1, -2, -4, or -6. ADAM 12-S may therefore be the IGFBP-5 protease that is secreted by osteoblasts and other cells. Cleavage of both IGFBP-3 and -5 by ADAM 12-S was inhibited by TIMP-3, raising the possibility that TIMP-3 is a physiological inhibitor of ADAM 12-S.

AB - ADAMs are a family of multidomain proteins having proteolytic and cell adhesion activities. We have previously shown that ADAM 12-S, the secreted soluble form of human ADAM 12, is a catalytically active protease. We now describe the purification of full-length recombinant ADAM 12-S and demonstrate that it cleaves insulin-like growth factor binding protein-3 (IGFBP-3). This result supports a role for ADAM 12-S in the degradation of IGFBP-3 in the blood of pregnant women. Furthermore, we tested for proteolysis of other members of the IGF binding protein family and found that ADAM 12-S cleaves IGFBP-5 in addition to IGFBP-3, but does not cleave IGFBP-1, -2, -4, or -6. ADAM 12-S may therefore be the IGFBP-5 protease that is secreted by osteoblasts and other cells. Cleavage of both IGFBP-3 and -5 by ADAM 12-S was inhibited by TIMP-3, raising the possibility that TIMP-3 is a physiological inhibitor of ADAM 12-S.

U2 - 10.1006/bbrc.2000.3835

DO - 10.1006/bbrc.2000.3835

M3 - Journal article

C2 - 11095942

VL - 278

SP - 511

EP - 515

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 3

ER -

ID: 5236432