A Specific Progesterone-binding Component of Human Breast Cyst Fluid

Pearlman, William H.; Gueriguian, J.L.; Sawyer, Mary

doi:10.1016/s0021-9258(19)43566-7

Cited by 99 publications

(3 citation statements)

References 10 publications

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“…is the major protein constituent of human mammary cyst fluid. It binds with a relatively strong affinity to progesterone and pregnenolone and with a weaker affinity to oestrogen (Pearlman et al, 1973;Lea, 1988;Balbin et al, 1990;Vogt and Skerra, 2001). However, another study shows a lack of interaction between ApoD and β-estradiol, suggesting that oestrogen is possibly not a natural ligand of ApoD (Ruiz et al, 2013).…”

Section: Apod Ligandsmentioning

confidence: 97%

Apolipoprotein D

Rassart¹,

Desmarais

Najyb³

et al. 2020

Gene

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ApoD is a 25 to 30 kDa glycosylated protein, member of the lipocalin superfamily. As a transporter of several small hydrophobic molecules, its known biological functions are mostly associated to lipid metabolism and neuroprotection.ApoD is a multi-ligand, multi-function protein that is involved lipid trafficking, food intake, inflammation, antioxidative response and development and in different types of cancers.An important aspect of ApoD's role in lipid metabolism appears to involve the transport of arachidonic acid, and the modulation of eicosanoid production and delivery in metabolic tissues. ApoD expression in metabolic tissues has been associated positively and negatively with insulin sensitivity and glucose homeostasis in a tissue dependent manner.ApoD levels rise considerably in association with aging and neuropathologies such as Alzheimer's disease, stroke, meningoencephalitis, moto-neuron disease, multiple sclerosis, schizophrenia and Parkinson's disease. ApoD is also modulated in several animal models of nervous system injury/ pathology.

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Section: Apod Ligandsmentioning

confidence: 97%

Apolipoprotein D

Rassart¹,

Desmarais

Najyb³

et al. 2020

Gene

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“…The apoD βbarrel encloses a conical shaped hydrophobic cavity, referred to as the apoD ligand-binding pocket. Early studies suggested that apoD can bind a range of lipids, including arachidonic acid (AA), cholesterol and several steroids (Dilley et al, 1990;Lea, 1988;Morais Cabral et al, 1995;Pearlman et al, 1973). More recent studies indicate that the binding of lipids in the apoD binding pocket is in fact specific (Eichinger et al, 2007;Vogt and Skerra, 2001).…”

Section: Introductionmentioning

confidence: 99%

Identification of a novel tetrameric structure for human apolipoprotein-D

Kielkopf

Low

Mok

et al. 2018

Journal of Structural Biology

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Apolipoprotein-D is a 25 kDa glycosylated member of the lipocalin family that folds into an eight-stranded β-barrel with a single adjacent α-helix. Apolipoprotein-D specifically binds a range of small hydrophobic ligands such as progesterone and arachidonic acid and has an antioxidant function that is in part due to the reduction of peroxidised lipids by methionine-93. Therefore, apolipoprotein-D plays multiple roles throughout the body and is protective in Alzheimer's disease, where apolipoprotein-D overexpression reduces the amyloid-β burden in Alzheimer's disease mouse models. Oligomerisation is a common feature of lipocalins that can influence ligand binding. The native structure of apolipoprotein-D, however, has not been conclusively defined. Apolipoprotein-D is generally described as a monomeric protein, although it dimerises when reducing peroxidised lipids. Here, we investigated the native structure of apolipoprotein-D derived from plasma, breast cyst fluid (BCF) and cerebrospinal fluid. In plasma and cerebrospinal fluid, apolipoprotein-D was present in high-molecular weight complexes, potentially in association with lipoproteins. In contrast, apolipoprotein-D in BCF formed distinct oligomeric species. We assessed apolipoprotein-D oligomerisation using native apolipoprotein-D purified from BCF and a suite of complementary methods, including multi-angle laser light scattering, analytical ultracentrifugation and small-angle X-ray scattering. Our analyses showed that apolipoprotein-D predominantly forms a ∼95 to ∼100 kDa tetramer. Small-angle X-ray scattering analysis confirmed these findings and provided a structural model for apolipoprotein-D tetramer. These data indicate apolipoprotein-D rarely exists as a free monomer under physiological conditions and provide insights into novel native structures of apolipoprotein-D and into oligomerisation behaviour in the lipocalin family.

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“…Curiously, plasma AGP is not the only Lipocalin able to bind progesterone. ApoD was isolated as a progesterone-binding protein from mammary cystic fluid ( Pearlman et al, 1973 ; Rassart et al, 2000 ) and even the complex crystalized ( Eichinger et al, 2007 ). Additionally, recombinant ApoM showed certain ability to interact with progesterone in vitro ( Ahnstrom et al, 2007 ), but no evidences of progesterone being an endogenous ApoM ligand have been presented so far.…”

Section: Agp Ligands and Receptorsmentioning

confidence: 99%

Into the Labyrinth of the Lipocalin α1-Acid Glycoprotein

Ruiz

2021

Front. Physiol.

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α1-acid glycoprotein (AGP), also known as Orosomucoid (ORM), belongs to the Lipocalin protein family and it is well-known for being a positive acute-phase protein. AGP is mostly found in plasma, with the liver as main contributor, but it is also expressed in other tissues such as the brain or the adipose tissue. Despite the vast literature on AGP, the physiological functions of the protein remain to be elucidated. A large number of activities mostly related to protection and immune system modulation have been described. Recently created AGP-knockout models have suggested novel physiological roles of AGP, including regulation of metabolism. AGP has an outstanding ability to efficiently bind endogenous and exogenous small molecules that together with the complex and variable glycosylation patterns, determine AGP functions. This review summarizes and discusses the recent findings on AGP structure (including glycans), ligand-binding ability, regulation, and physiological functions of AGP. Moreover, this review explores possible molecular and functional connections between AGP and other members of the Lipocalin protein family.

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A Specific Progesterone-binding Component of Human Breast Cyst Fluid

Cited by 99 publications

References 10 publications

Apolipoprotein D

Apolipoprotein D

Identification of a novel tetrameric structure for human apolipoprotein-D

Into the Labyrinth of the Lipocalin α1-Acid Glycoprotein

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