A monoclonal anti-peptide antibody recognizes the adrenocorticotropic receptor

B. L. Clarke; K. L. Bost

doi:10.1016/0006-291X(90)91131-B

A monoclonal anti-peptide antibody recognizes the adrenocorticotropic receptor

B. L. Clarke
, K. L. Bost

Biomedical Sciences

Research output: Contribution to journal › Article › peer-review

6 Scopus citations

Abstract

We have produced a monoclonal antibody that specifically recognizes the adrenocorticotropic receptor on rat adrenal cells. The immunogen was designed from an RNA sequence complementary to the mRNA coding for ACTH_1-24. This complementary peptide, termed HTCA, has been shown to specifically bind ACTH and was proposed to mimic the ACTH binding site of the hormone receptor. The monoclonal anti-HTCA antibody recognized a restricted domain of the HTCA peptide, bound to Y-1 adrenal cells with a K_D of 1.8 nM, and blocked the binding of ¹²⁵I-ACTH to rat adrenal cells. These findings show that anti-HTCA competes with ACTH for binding to the ACTH receptor.

Original language	English (US)
Pages (from-to)	1020-1026
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	168
Issue number	3
DOIs	https://doi.org/10.1016/0006-291X(90)91131-B
State	Published - May 16 1990

Bibliographical note

Funding Information:
Acknowledgments. We would like to preparation of this manuscript, Todd assistance, and David Pascual for insightful supported by NIDDKD grant DK 39299.

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title = "A monoclonal anti-peptide antibody recognizes the adrenocorticotropic receptor",

abstract = "We have produced a monoclonal antibody that specifically recognizes the adrenocorticotropic receptor on rat adrenal cells. The immunogen was designed from an RNA sequence complementary to the mRNA coding for ACTH1-24. This complementary peptide, termed HTCA, has been shown to specifically bind ACTH and was proposed to mimic the ACTH binding site of the hormone receptor. The monoclonal anti-HTCA antibody recognized a restricted domain of the HTCA peptide, bound to Y-1 adrenal cells with a KD of 1.8 nM, and blocked the binding of 125I-ACTH to rat adrenal cells. These findings show that anti-HTCA competes with ACTH for binding to the ACTH receptor.",

author = "Clarke, \{B. L.\} and Bost, \{K. L.\}",

note = "Funding Information: Acknowledgments. We would like to preparation of this manuscript, Todd assistance, and David Pascual for insightful supported by NIDDKD grant DK 39299.",

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AU - Clarke, B. L.

AU - Bost, K. L.

N1 - Funding Information: Acknowledgments. We would like to preparation of this manuscript, Todd assistance, and David Pascual for insightful supported by NIDDKD grant DK 39299.

PY - 1990/5/16

Y1 - 1990/5/16

N2 - We have produced a monoclonal antibody that specifically recognizes the adrenocorticotropic receptor on rat adrenal cells. The immunogen was designed from an RNA sequence complementary to the mRNA coding for ACTH1-24. This complementary peptide, termed HTCA, has been shown to specifically bind ACTH and was proposed to mimic the ACTH binding site of the hormone receptor. The monoclonal anti-HTCA antibody recognized a restricted domain of the HTCA peptide, bound to Y-1 adrenal cells with a KD of 1.8 nM, and blocked the binding of 125I-ACTH to rat adrenal cells. These findings show that anti-HTCA competes with ACTH for binding to the ACTH receptor.

AB - We have produced a monoclonal antibody that specifically recognizes the adrenocorticotropic receptor on rat adrenal cells. The immunogen was designed from an RNA sequence complementary to the mRNA coding for ACTH1-24. This complementary peptide, termed HTCA, has been shown to specifically bind ACTH and was proposed to mimic the ACTH binding site of the hormone receptor. The monoclonal anti-HTCA antibody recognized a restricted domain of the HTCA peptide, bound to Y-1 adrenal cells with a KD of 1.8 nM, and blocked the binding of 125I-ACTH to rat adrenal cells. These findings show that anti-HTCA competes with ACTH for binding to the ACTH receptor.

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ER -

A monoclonal anti-peptide antibody recognizes the adrenocorticotropic receptor

Abstract

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