Human blood contains both the uncleaved precursor of anti-Mullerian hormone and a complex of the NH2- and COOH-terminal peptides.

@article{Pankhurst2013HumanBC,
  title={Human blood contains both the uncleaved precursor of anti-Mullerian hormone and a complex of the NH2- and COOH-terminal peptides.},
  author={Michael W. Pankhurst and Ian S McLennan},
  journal={American journal of physiology. Endocrinology and metabolism},
  year={2013},
  volume={305 10},
  pages={
          E1241-7
        }
}
  • M. Pankhurst, I. McLennan
  • Published 15 November 2013
  • Biology
  • American journal of physiology. Endocrinology and metabolism
Anti-Müllerian hormone (AMH) in blood is a marker of ovarian status in women and the presence of cryptic testes in babies. Despite this, the molecular form of AMH in blood has not been verified. AMH is synthesized as an inert proprotein precursor (proAMH), which can be cleaved to yield NH2-terminal (AMHN) and COOH-terminal (AMHC) fragments, that can complex noncovalently (AMHN,C). Developing males have 10-fold more AMH than young adults. We report here that human blood is a mixture of inactive… 
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The Anti-Müllerian Hormone Precursor (proAMH) Is Not Converted to the Receptor-Competent Form (AMHN,C) in the Circulating Blood of Mice.
TLDR
The data suggest that the ratio of proAMH to AMHN,C in the circulation is not altered after it is released from the gonads and that the levels of these 2 circulating forms are likely to reflect AMH activity in the gonad.
A specific immunoassay for proAMH, the uncleaved proprotein precursor of anti-Müllerian hormone
Enzyme-linked immunosorbent assay measurements of antimüllerian hormone (AMH) in human blood are a composite of the uncleaved and bioactive cleaved forms of AMH.
Most Cleaved Anti-Müllerian Hormone Binds Its Receptor in Human Follicular Fluid but Little Is Competent in Serum.
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The results support an autocrine role for AMH in the pathophysiology of PCOS in the follicle and indicate that AMH undergoes interactions or structural changes after cleavage that prevent receptor binding, meaning, unexpectedly, that the level of cleavage in biological fluids does not always reflect thelevel of bioactive AMH.
Relative levels of the proprotein and cleavage‐activated form of circulating human anti‐Müllerian hormone are sexually dimorphic and variable during the life cycle
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The cleavage of circulating AMH varies extensively within the human population, with most individuals having significant levels of proAMH.
Anti-Müllerian hormone is a gonadal cytokine with two circulating forms and cryptic actions.
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Anti-Müllerian hormone is male specific during the initial stage of development, and theoretically should produce male biases throughout the body by adding a male-specific amplification of BMP/GDF signalling.
High Variability of Molecular Isoforms of AMH in Follicular Fluid and Granulosa Cells From Human Small Antral Follicles
TLDR
This study detected several AMH forms in FF and GCs obtained from human small antral follicles, which suggests that intrafollicular processing of AMH is complex and variable, and it may be difficult to develop an antibody-based AMH assay that detects all AMH isoforms.
Conserved Anti-Müllerian Hormone: Anti-Müllerian Hormone Type-2 Receptor Specific Interaction and Intracellular Signaling in Teleosts1
TLDR
Cl cloning sea bass amhr2, the production of a recombinant sea bass Amh, and the functional analysis of this ligand-receptor couple revealed that sea bassamhr2 segregates with Amhr2 from other vertebrates, and revealed that this piscine receptor is capable of activating Smad proteins.
Proteolytic processing of anti-Müllerian hormone differs between human fetal testes and adult ovaries.
TLDR
The present findings suggest that processing of AMH is a tightly regulated process, which is likely to be important for the function of AMh and which differs between the two sexes.
Development of a recombinant CHO cell line Anti-Müllerian Hormone
TLDR
The results of the thesis show that a stable recombinant CHO cell line could be established for AMH by transfection of a vector containing the native AMH sequence, and indicated that the C-terminal purification tag in the expression vector altered expression.
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