why formed micelles in the absorption of lipid?

The products of lipid digestion, such as fatty acids, monoglycerides, and glycerol, are not very
soluble. This means they do not dissolve well in water, which is a problem because the
environment in the small intestine is aqueous
To overcome this, the monoglycerides and fatty acids associate with phospholipids and bile salts
to form micelles12. These are very small droplets that aid in the transport of these molecules to
the surface of the epithelial cells12.
Micelles are lipoproteins designed for the transport of lipids3. They facilitate absorption by
microvilli, where the fatty acids and proteins diffuse out to form lipoproteins3.
The micelles break down and add to a pool of fatty acids and monoglycerides that are dissolved
in the small intestine solution surrounding the epithelial cells1. These freely dissolved molecules
enter the epithelial cell by diffusion1.

So, micelles are integral to lipid absorption because they allow the lipids to be transported in an
aqueous environment, and they facilitate the absorption of these lipids into the epithelial cells of
the small intestine

What is the purpose of the lack of the glycerol kinase enzyme in adipose tissues?
Adipose tissue serves as a major energy reservoir in the body. By releasing glycerol and fatty
acids into the bloodstream during times of energy demand, adipose tissue contributes to the
overall energy homeostasis of the organism. The absence of glycerol kinase in adipose tissue
ensures that released glycerol is not reincorporated into triglycerides within the adipocytes,
facilitating its availability for energy production in other tissues.

which is likely the reason that triacylglycerols rather than glycogen were selected in evolution as
the major energy reservoir?
‫بسبب الطاقة العالية‬
‫وبسبب قوة سحب الماء للكلوكوز‬

Why gastric and lingual lipase are limited?

• No emulsification of fats takes place in stomach
• The enzyme secreted in small quantity
• pH of gastric juice is not conducive which is highly acidic
already discussed. Apolipoprotein B (apo B) plays an important role in the transport of
triacylglycerols and cholesterol by forming an amphipathic spherical shell around the
lipids carried in lipoprotein particles . Apo B exists in two forms,

The larger form, synthesized by the liver.

The smaller form, synthesized by the small intestine.
Apo B-48 contains the 2152(240-kDa) N-terminal residues of the 4536-residue(512-kDa) apo B-
100. This truncated molecule can form lipoprotein particles but cannot bind to the low-density-
lipoprotein receptor on cell surfaces.
What is the biosynthetic relation of these two forms of apo B? One possibility a priori is that apo
B-48 is produced by proteolytic cleavage of apo B-100, and another is that the two forms arise
from alternative splicing . The results of experiments show that neither occurs. A totally
unexpected and new mechanism for generating diversity is at work: the changing of the
nucleotide sequence of mRNA after its synthesis . A specific cytidine residue of mRNA is
deaminated to uridine, which changes the codon at residue 2153 from CAA (Gln) to UAA (stop).
The deaminase that catalyzes this reaction is present in the small intestine, but not in the liver,
and is expressed only at certain developmental stages

why Gastric lipase activity requires presence of Ca++?

the activity of many lipases is influenced by Ca++. Calcium ions can stabilize the structure of the enzyme,
enhance its resistance to changes in pH and temperature
Calcium ions can engage in electrostatic interactions with charged amino acid residues on the enzyme
surface

? ‫ بعدم وجود االنسولين‬LPL ‫ ففي حاله الصيام كيف يتفعل‬CII ‫اذا كان االنسولين هو يحفز‬

Bile acids reversibly form thermodynamically stable aggregates, called micelles

what the effector of lipoprotein lipase activity?

1. Apolipoprotein C-II (apoC-II):

 ApoC-II is an activator of lipoprotein lipase. It is a cofactor that associates
with LPL and enhances its catalytic activity. ApoC-II is often found on the
surface of chylomicrons and very-low-density lipoproteins (VLDL) and
stimulates LPL-mediated hydrolysis of their triglycerides.
2. Heparan Sulfate Proteoglycans (HSPG):
 LPL is anchored to the endothelial surface by interacting with heparan
sulfate proteoglycans. These proteoglycans serve as cofactors for LPL
activity by presenting lipoprotein substrates to the enzyme. The interaction
with HSPG is important for the efficient hydrolysis of lipoprotein
triglycerides.
3. Insulin:
 Insulin is a hormone that enhances the activity of lipoprotein lipase. Insulin
promotes the synthesis and release of lipoprotein lipase from cells,
increasing the enzyme's availability. It also stimulates the uptake of fatty
acids into cells, promoting their storage as triglycerides.
4. Adipose Tissue Hormones:
 Hormones released by adipose (fat) tissue, such as adiponectin, can
influence lipoprotein lipase activity. Adiponectin, for example, has been
shown to enhance the expression and activity of LPL.
5. Postprandial State (Fed State):
 LPL activity is generally increased in the postprandial (fed) state when
there is an increased need for the hydrolysis of dietary triglycerides. The
presence of chylomicrons and VLDL in the bloodstream during this state
stimulates LPL activity.
6. Fasting State:
 Conversely, during fasting, when the body needs to mobilize stored
energy, lipoprotein lipase activity may be reduced. This is part of the
regulatory mechanism to balance energy utilization and storage