วันศุกร์ที่ 29 มีนาคม 2567 เวลา 09.30 อนุกรรมการสนับสนุนการจัดการดูเเลระยะยาวสำหรับผู้สูงอายุที่มีภาวะพึ่งพิง ประชุมเพื่ออนุมัติเเผนงาน โครงการ จัดบริการดูแลระยะยาวสำหรับผู้สูงอายุที่มีภาวะพึ่งพิงและบุคคลอื่นที่มีภาวะพึ่งพิงแผนการดูแลรายบุคคล ซึ่งที่ประชุมได้มีมติอนุมัติค่าใช้จ่ายตามแผนการดูแลรายบุคคลสำหรับผู้สูงอายุทีมีภาวะพึ่งพิงและบุคคลอื่นที่มีภาวะพึ่งพิง ราย 12 เดือน
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Ipamorelin and Sermorelin are two popular growth hormone-releasing peptides that many people
use to try to boost their natural production of human growth hormone (HGH).
While they share a common goal, they differ in structure, potency, duration of action, side-effect profile, and the way they interact with the body’s pituitary gland.
Understanding these differences can help you decide which
peptide might be better suited for your goals, whether that is muscle gain, anti-aging, or recovery from injury.
Ipamorelin vs. Sermorelin: Here’s What You Need to Know
The first major distinction between Ipamorelin and Sermorelin lies in their molecular makeup.
Ipamorelin is a pentapeptide composed of five amino acids that
mimic the natural growth hormone-releasing factor (GHRF).
Its sequence is designed to bind specifically to the ghrelin receptor on pituitary cells, stimulating them to release HGH without
affecting other hormones. Sermorelin, on the
other hand, is a longer peptide made up of nine amino acids and is
structurally similar to the natural growth hormone-releasing hormone (GHRH).
It binds to GHRH receptors in the pituitary, triggering
the release of HGH as well.
Because Ipamorelin targets the ghrelin receptor, it tends to produce
a more focused stimulation of HGH with minimal influence on prolactin or cortisol levels.
Sermorelin’s action through the GHRH pathway can lead to a
broader hormonal response, sometimes causing mild
increases in other pituitary hormones. This difference often translates into variations in side-effect profiles:
Ipamorelin is generally reported to have fewer side effects such as water retention or increased appetite,
whereas Sermorelin users might notice slight changes in mood or sleep patterns.
Another key point of comparison is potency and dosing frequency.
Ipamorelin’s high affinity for its receptor allows it to
be effective at lower doses (typically 100–200 micrograms per injection).
Users often inject once or twice daily. Sermorelin requires
a slightly higher dose (around 300–400 micrograms) and may need to be administered two to three times each day to achieve comparable HGH peaks.
The more frequent injections required for Sermorelin can be inconvenient for some people.
What are HGH peptides and how do they work?
Human growth hormone-releasing peptides, commonly called
HGH peptides, are short chains of amino acids that mimic natural hormones or signals in the body
that regulate growth hormone secretion. They bind to specific receptors on cells
in the pituitary gland, which is the master regulator of many
endocrine functions. When these receptors are activated, the pituitary releases stored growth hormone into the bloodstream.
Once circulating, HGH travels to various tissues where it promotes protein synthesis, fat metabolism, bone
remodeling, and cell regeneration.
Because HGH peptides stimulate the body’s
own production rather than delivering exogenous growth hormone directly, they typically have a
lower risk of side-effects such as acromegaly or fluid retention that can accompany
direct HGH therapy. They also allow for more physiological timing of hormone release, often mimicking the natural
nightly surge that occurs during deep sleep.
How does Ipamorelin vs. Sermorelin work to stimulate
HGH?
Ipamorelin operates by acting on the ghrelin receptor located on pituitary somatotroph cells.
Ghrelin is a stomach-derived hormone known for stimulating appetite, but it
also signals the pituitary to release growth hormone. By binding to this same receptor, Ipamorelin tricks the body into thinking that ghrelin levels are high, thereby triggering a spike in HGH production. Because its action is highly selective,
it rarely stimulates the release of other pituitary hormones such as prolactin or thyroid-stimulating
hormone.
Sermorelin, conversely, mimics growth hormone-releasing hormone itself.
GHRH is produced in the hypothalamus and travels through the bloodstream to the pituitary where it binds to its
receptor on somatotroph cells. Sermorelin’s nine-amino-acid structure fits this receptor almost exactly, prompting the
same cascade of events that leads to HGH release.
While both peptides ultimately cause the pituitary to secrete growth hormone, the
upstream signals they mimic differ: one follows a stomach-to-pituitary pathway (Ipamorelin), and the
other follows a hypothalamus-to-pituitary route (Sermorelin).
In practical terms, this means that Ipamorelin often produces sharper peaks of HGH with less influence
on other hormones, making it popular for athletes who want to avoid water retention or increased
appetite. Sermorelin’s broader action can be advantageous for people looking for a more
natural hormonal profile or those who have had issues with low growth hormone levels that require a stronger stimulus.
In summary, while both Ipamorelin and Sermorelin are
effective at stimulating endogenous HGH production, their
differences in receptor targeting, dosing schedule, potency, and side-effect
profiles give each a distinct place depending on an individual’s goals,
tolerance for injections, and sensitivity to hormonal changes.
Choosing between them involves weighing the convenience
of fewer daily shots against the desire for more
selective hormone release.
What is mirror life? Scientists are sounding the alarm
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Scientist Kate Adamala doesn’t remember exactly when she realized her lab at the University of Minnesota was working on something potentially dangerous — so dangerous in fact that some researchers think it could pose an existential risk to all life forms on Earth.
She was one of four researchers awarded a $4 million US National Science Foundation grant in 2019 to investigate whether it’s possible to produce a mirror cell, in which the structure of all of its component biomolecules is the reverse of what’s found in normal cells.
The work was important, they thought, because such reversed cells, which have never existed in nature, could shed light on the origins of life and make it easier to create molecules with therapeutic value, potentially tackling significant medical challenges such as infectious disease and superbugs. But doubt crept in.
“It was never one light bulb moment. It was kind of a slow boiling over a few months,” Adamala, a synthetic biologist, said. People started asking questions, she added, “and we thought we can answer them, and then we realized we cannot.”
The questions hinged on what would happen if scientists succeeded in making a “mirror organism” such as a bacterium from molecules that are the mirror images of their natural forms. Could it inadvertently spread unchecked in the body or an environment, posing grave risks to human health and dire consequences for the planet? Or would it merely fizzle out and harmlessly disappear without a trace?
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What is mirror life? Scientists are sounding the alarm
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Scientist Kate Adamala doesn’t remember exactly when she realized her lab at the University of Minnesota was working on something potentially dangerous — so dangerous in fact that some researchers think it could pose an existential risk to all life forms on Earth.
She was one of four researchers awarded a $4 million US National Science Foundation grant in 2019 to investigate whether it’s possible to produce a mirror cell, in which the structure of all of its component biomolecules is the reverse of what’s found in normal cells.
The work was important, they thought, because such reversed cells, which have never existed in nature, could shed light on the origins of life and make it easier to create molecules with therapeutic value, potentially tackling significant medical challenges such as infectious disease and superbugs. But doubt crept in.
“It was never one light bulb moment. It was kind of a slow boiling over a few months,” Adamala, a synthetic biologist, said. People started asking questions, she added, “and we thought we can answer them, and then we realized we cannot.”
The questions hinged on what would happen if scientists succeeded in making a “mirror organism” such as a bacterium from molecules that are the mirror images of their natural forms. Could it inadvertently spread unchecked in the body or an environment, posing grave risks to human health and dire consequences for the planet? Or would it merely fizzle out and harmlessly disappear without a trace?
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