In medicine, proteopathy (Proteo- [pref. protein]; -pathy [suff.
disease]; proteopathies pl.; proteopathic adj.) refers to a class of
diseases in which certain proteins become structurally abnormal, and
thereby disrupt the function of cells, tissues and organs of the body.
Often the proteins fail to fold into their normal configuration; in
this misfolded state, the proteins can become toxic in some way (a
gain of toxic function) or they can lose their normal function. The
proteopathies (also known as proteinopathies, protein conformational
disorders, or protein misfolding diseases), include such diseases as
Alzheimer's disease, Parkinson's disease, prion disease, type 2
diabetes, amyloidosis, and a wide range of other disorders
The concept of proteopathy can trace its origins to the mid-19th
century, when, in 1854, Rudolf Virchow coined the term amyloid
("starch-like") to describe a substance in cerebral corpora amylacea
that exhibited a chemical reaction resembling that of cellulose. In
1859, Friedreich and Kekulé demonstrated that, rather than consisting
of cellulose, "amyloid" actually is rich in protein. Subsequent
research has shown that many different proteins can form amyloid, and
that all amyloids have in common birefringence in cross-polarized
light after staining with the dye Congo Red, as well as a fibrillar
ultrastructure when viewed with an electron microscope. However, some
proteinaceous lesions lack birefringence and contain few or no
classical amyloid fibrils, such as the diffuse deposits of Aβ protein
in the brains of Alzheimer patients. Furthermore, evidence has emerged
that small, non-fibrillar protein aggregates known as oligomers are
toxic to the cells of an affected organ, and that amyloidogenic
proteins in their fibrillar form may be relatively benign
In most, if not all proteopathies, a change in 3-dimensional folding
(conformation) increases the tendency of a specific protein to bind to
itself.[7] In this aggregated form, the protein is resistant to
clearance and can interfere with the normal capacity of the affected
organs. In some cases, misfolding of the protein results in a loss of
its usual function. For example, cystic fibrosis is caused by a
defective cystic fibrosis transmembrane conductance regulator (CFTR)
protein,[3] and in amyotrophic lateral sclerosis / frontotemporal
lobar degeneration (FTLD), certain gene-regulating proteins
inappropriately aggregate in the cytoplasm, and thus are unable to
perform their normal tasks within the nucleus. Because proteins share
a common structural feature known as the polypeptide backbone, all
proteins have the potential to misfold under some circumstances.
However, only a relatively small number of proteins are linked to
proteopathic disorders, possibly due to structural idiosyncrasies of
the vulnerable proteins. For example, proteins that are relatively
unstable as monomers (that is, as single, unbound protein molecules)
are more likely to misfold into an abnormal conformation. In nearly
all instances, the disease-causing molecular configuration involves an
increase in beta-sheet secondary structure of the protein. The
abnormal proteins in some proteopathies have been shown to fold into
multiple 3-dimensional shapes; these variant, proteinaceous structures
are defined by their different pathogenic, biochemical, and
conformational properties. They have been most thoroughly studied with
regard to prion disease, and are referred to as protein strains
PROPHETOPATHIC MEDICINE
Amaranthus, collectively known as amaranth, is a cosmopolitan genus of
herbs. Approximately 60 species are recognized, with inflorescences
and foliage ranging from purple and red to gold. Members of this genus
share many characteristics and uses with members of the closely
related genus Celosia.
Although several species are often considered weeds, people around the
world value amaranths as leaf vegetables, cereals, and ornamentals.
(Oriya); Khada Saga, are a common leaf vegetable throughout the
tropics and in many warm temperate regions. It is very popular in
India
Cooked amaranth leaves are a good source of vitamin A, vitamin C, and
folate; they are also a complementing source of other vitamins such as
thiamine, niacin, and riboflavin, plus some dietary minerals including
calcium, iron, potassium, zinc, copper, and manganese. Cooked amaranth
grains are a complementing source of thiamine, niacin, riboflavin, and
folate, and dietary minerals including calcium, iron, magnesium,
phosphorus, zinc, copper, and manganese - comparable to common grains
such as wheat germ, oats and others.
Amaranth seeds contain lysine, an essential amino acid, limiting in
other grains or plant sources. Most fruits and vegetables do not
contain a complete set of amino acids, and thus different sources of
protein must be used. Amaranth too is limiting in some essential amino
acids, such as leucine and threonine. Amaranth seeds are therefore
promising complement to common grains such as wheat germ, oats, corn
because these common grains are abundant sources of essential amino
acids found to be limited in amaranth.
Amaranth may be a promising source of protein to those who are gluten
sensitive, because unlike the protein found in grains such as wheat
and rye, its protein does not contain gluten. According to a 2007
report, amaranth compares well in nutrient content with gluten-free
vegetarian options such as buckwheat, corn, millet, wild rice, oats
and quinoa.
Several studies have shown that like oats, amaranth seed or oil may be
of benefit for those with hypertension and cardiovascular disease;
regular consumption reduces blood pressure and cholesterol levels,
while improving antioxidant status and some immune parameters. While
the active ingredient in oats appears to be water-soluble fiber,
amaranth appears to lower cholesterol via its content of plant stanols
and squalene.
Amaranth remains an active area of scientific research for both human
nutritional needs and foraging applications. Over 100 scientific
studies suggest a somewhat conflicting picture on possible
anti-nutritional and toxic factors in amaranth, more so in some
particular strains of amaranth. Lehmann, in a review article,
identifies some of these reported anti-nutritional factors in amaranth
to be phenolics, saponins, tannins, phytic acid, oxalates, protease
inhibitors, nitrates, polyphenols and phytohemagglutinins. Of these,
oxalates and nitrates are of more concern when amaranth grain is used
in foraging applications. Some studies suggest thermal processing of
amaranth, particularly in moist environment, prior to its preparation
in food and human consumption may be a promising way to reduce the
adverse effects of amaranth's anti-nutritional and toxic factors.
FOR DETAIL WITH PROTEOPATHIC MEDICINE CONTACT US.
disease]; proteopathies pl.; proteopathic adj.) refers to a class of
diseases in which certain proteins become structurally abnormal, and
thereby disrupt the function of cells, tissues and organs of the body.
Often the proteins fail to fold into their normal configuration; in
this misfolded state, the proteins can become toxic in some way (a
gain of toxic function) or they can lose their normal function. The
proteopathies (also known as proteinopathies, protein conformational
disorders, or protein misfolding diseases), include such diseases as
Alzheimer's disease, Parkinson's disease, prion disease, type 2
diabetes, amyloidosis, and a wide range of other disorders
The concept of proteopathy can trace its origins to the mid-19th
century, when, in 1854, Rudolf Virchow coined the term amyloid
("starch-like") to describe a substance in cerebral corpora amylacea
that exhibited a chemical reaction resembling that of cellulose. In
1859, Friedreich and Kekulé demonstrated that, rather than consisting
of cellulose, "amyloid" actually is rich in protein. Subsequent
research has shown that many different proteins can form amyloid, and
that all amyloids have in common birefringence in cross-polarized
light after staining with the dye Congo Red, as well as a fibrillar
ultrastructure when viewed with an electron microscope. However, some
proteinaceous lesions lack birefringence and contain few or no
classical amyloid fibrils, such as the diffuse deposits of Aβ protein
in the brains of Alzheimer patients. Furthermore, evidence has emerged
that small, non-fibrillar protein aggregates known as oligomers are
toxic to the cells of an affected organ, and that amyloidogenic
proteins in their fibrillar form may be relatively benign
In most, if not all proteopathies, a change in 3-dimensional folding
(conformation) increases the tendency of a specific protein to bind to
itself.[7] In this aggregated form, the protein is resistant to
clearance and can interfere with the normal capacity of the affected
organs. In some cases, misfolding of the protein results in a loss of
its usual function. For example, cystic fibrosis is caused by a
defective cystic fibrosis transmembrane conductance regulator (CFTR)
protein,[3] and in amyotrophic lateral sclerosis / frontotemporal
lobar degeneration (FTLD), certain gene-regulating proteins
inappropriately aggregate in the cytoplasm, and thus are unable to
perform their normal tasks within the nucleus. Because proteins share
a common structural feature known as the polypeptide backbone, all
proteins have the potential to misfold under some circumstances.
However, only a relatively small number of proteins are linked to
proteopathic disorders, possibly due to structural idiosyncrasies of
the vulnerable proteins. For example, proteins that are relatively
unstable as monomers (that is, as single, unbound protein molecules)
are more likely to misfold into an abnormal conformation. In nearly
all instances, the disease-causing molecular configuration involves an
increase in beta-sheet secondary structure of the protein. The
abnormal proteins in some proteopathies have been shown to fold into
multiple 3-dimensional shapes; these variant, proteinaceous structures
are defined by their different pathogenic, biochemical, and
conformational properties. They have been most thoroughly studied with
regard to prion disease, and are referred to as protein strains
PROPHETOPATHIC MEDICINE
Amaranthus, collectively known as amaranth, is a cosmopolitan genus of
herbs. Approximately 60 species are recognized, with inflorescences
and foliage ranging from purple and red to gold. Members of this genus
share many characteristics and uses with members of the closely
related genus Celosia.
Although several species are often considered weeds, people around the
world value amaranths as leaf vegetables, cereals, and ornamentals.
(Oriya); Khada Saga, are a common leaf vegetable throughout the
tropics and in many warm temperate regions. It is very popular in
Cooked amaranth leaves are a good source of vitamin A, vitamin C, and
folate; they are also a complementing source of other vitamins such as
thiamine, niacin, and riboflavin, plus some dietary minerals including
calcium, iron, potassium, zinc, copper, and manganese. Cooked amaranth
grains are a complementing source of thiamine, niacin, riboflavin, and
folate, and dietary minerals including calcium, iron, magnesium,
phosphorus, zinc, copper, and manganese - comparable to common grains
such as wheat germ, oats and others.
Amaranth seeds contain lysine, an essential amino acid, limiting in
other grains or plant sources. Most fruits and vegetables do not
contain a complete set of amino acids, and thus different sources of
protein must be used. Amaranth too is limiting in some essential amino
acids, such as leucine and threonine. Amaranth seeds are therefore
promising complement to common grains such as wheat germ, oats, corn
because these common grains are abundant sources of essential amino
acids found to be limited in amaranth.
Amaranth may be a promising source of protein to those who are gluten
sensitive, because unlike the protein found in grains such as wheat
and rye, its protein does not contain gluten. According to a 2007
report, amaranth compares well in nutrient content with gluten-free
vegetarian options such as buckwheat, corn, millet, wild rice, oats
and quinoa.
Several studies have shown that like oats, amaranth seed or oil may be
of benefit for those with hypertension and cardiovascular disease;
regular consumption reduces blood pressure and cholesterol levels,
while improving antioxidant status and some immune parameters. While
the active ingredient in oats appears to be water-soluble fiber,
amaranth appears to lower cholesterol via its content of plant stanols
and squalene.
Amaranth remains an active area of scientific research for both human
nutritional needs and foraging applications. Over 100 scientific
studies suggest a somewhat conflicting picture on possible
anti-nutritional and toxic factors in amaranth, more so in some
particular strains of amaranth. Lehmann, in a review article,
identifies some of these reported anti-nutritional factors in amaranth
to be phenolics, saponins, tannins, phytic acid, oxalates, protease
inhibitors, nitrates, polyphenols and phytohemagglutinins. Of these,
oxalates and nitrates are of more concern when amaranth grain is used
in foraging applications. Some studies suggest thermal processing of
amaranth, particularly in moist environment, prior to its preparation
in food and human consumption may be a promising way to reduce the
adverse effects of amaranth's anti-nutritional and toxic factors.
FOR DETAIL WITH PROTEOPATHIC MEDICINE CONTACT US.
