c c




 is the process of programmed cell death (PCD) that may occur in multicellular
organisms.[3]Biochemical events lead to characteristic cell changes (morphology) and death. These
changes include blebbing, loss of cell membrane asymmetry and attachment, cell
shrinkage, nuclear fragmentation, chromatin condensation, and chromosomal DNAfragmentation. (See
also Apoptosis DNA fragmentation.) Unlike necrosis, apoptosis produces cell fragments called apoptotic
bodies that surrounding cells are able to engulf and quickly remove before the contents of the cell can
spill out onto surrounding cells and cause damage.

In contrast to necrosis, which is a form of traumatic cell death that results from acute cellular injury,
apoptosis, in general, confers advantages during an organism's life cycle. For example, the differentiation
of fingers and toes in a developing humanembryo occurs because cells between the fingers apoptose;
the result is that the digits are separate. Between 50 and 70 billioncells die each day due to apoptosis in
the average human adult. For an average child between the ages of 8 and 14, approximately 20 billion to
30 billion cells die a day


è


è
 , a hormone secreted by the pancreas, raises blood glucose levels. Its effect is opposite that
of insulin, which lowers blood glucose levels.[1] The pancreas releases glucagon when blood
sugar (glucose) levels fall too low. Glucagon causes the liver to convert stored glycogen into glucose,
which is released into the bloodstream. Glucagon raises blood glucose levels. High blood glucose levels
stimulate the release of insulin. Insulin allows glucose to be taken up and used by insulin-dependent
tissues. Thus, glucagon and insulin are part of a feedback system that keeps blood glucose levels at a
stable level. Glucagon belongs to a family of several other related hormones.

Glucose is stored in the liver in the form of glycogen, which is a starch-like polymer chain made up of
glucose molecules. Liver cells (hepatocytes) have glucagon receptors. When glucagon binds to the
glucagon receptors, the liver cells convert the glycogen polymer into individual glucose molecules, and
release them into the bloodstream, in a process known asglycogenolysis. As these stores become
depleted, glucagon then encourages the liver to synthesize additional glucose by gluconeogenesis.
Glucagon turns off glycolysis in the liver, causing glycolytic intermediates to be shuttled to
gluconeogenesis.

Glucagon also regulates the rate of glucose production through lipolysis.

Glucagon production appears to be dependent on the central nervous system through pathways yet to be
defined. In invertebrate animals, eyestalk removal has been reported to affect glucagon production.
Excising the eyestalk in young crayfish produces glucagon-induced hyperglycemia

°
 

°
 (also known as 

   

 (è) or 

  
  
 (° )) is apeptide hormone that regulates the endocrine system and
affects neurotransmission and cell proliferation via interaction with G-protein-coupled somatostatin
receptors and inhibition of the release of numerous secondary hormones.

Somatostatin has two active forms produced by alternative cleavage of a single preproprotein: one of
14 amino acids, the other of 28 amino acids

Somatostatin is classified as an inhibitory hormone,[1] whose actions are spread to different parts of the
body


  



In the anterior pituitary gland, the effects of somatostatin are:

[5]
Î Inhibit the release of growth hormone (GH) (thus opposing the effects of Growth Hormone-
Releasing Hormone(GHRH))
Î Inhibit the release of thyroid-stimulating hormone (TSH)[6]
Î It is induced by low pH.
Î Inhibit adenylyl cyclase in parietal cells.
Î
Î è   
 


Î Somatostatin is homologous with cortistatin (see somatostatin family) and suppresses the release
of gastrointestinal hormones
Î Gastrin
Î Cholecystokinin (CCK)
Î Secretin
Î Motilin
Î Vasoactive intestinal peptide (VIP)
Î Gastric inhibitory polypeptide (GIP)
Î Enteroglucagon
Î Decrease rate of gastric emptying, and reduces smooth muscle contractions and blood flow within the
intestine[5]
Î Suppresses the release of pancreatic hormones
Î Inhibits insulin release when somatostatin is released from delta cells of pancreas[7]
Î Inhibits the release of glucagon[7]
Î Suppresses the exocrine secretory action of pancreas.
AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA
‘



Proinsulin   was first described in 1967 in connection with the discovery of
the insulin biosynthesis. It serves as an important linker between the A- and the B- chains of insulin and
facilitates the efficient assembly, folding, and processing of insulin in the endoplasmic reticulum.
Equimolar amounts of C-peptide and insulin are then stored in secretory granules of the pancreatic beta
cells and both are eventually released to the portal circulation. Initially, the sole interest in C-peptide was
as a marker of insulin secretion and has as such been of great value in furthering the understanding of
the pathophysiology of type 1 and type 2 diabetes. The first documented use of the C-peptide test was in
1972. During the past decade, however, C-peptide has been found to be a bioactive peptide in its own
right, with effects on microvascular blood flow and tissue health.

C-peptide should not be confused with c-reactive protein or Protein C.


 

   C-peptide has been shown to bind to the surface of a number of cell types
such as neuronal, endothelial, fibroblast and renal tubular, at nanomolar concentrations to a receptor that
is likely G-protein coupled. The signal activates Ca2+ dependent intracellular signaling pathways such as
MAPK, PLCȖ and PKC, leading to upregulation of a range of transcription factors as well as eNOS and
Na+K+ATPase activities. The latter two enzymes are known to have reduced activities in patients with
type I diabetes and have been implicated in the development of long-terms complications of type I
diabetes such as peripheral and autonomic neuropathy. In vivo studies in animal models of type 1
diabetes have established that C-peptide administration results in significant improvements in nerve and
kidney function. Thus, in animals with early signs of diabetes-induced neuropathy, C peptide treatment in
replacement dosage results in improved peripheral nerve function, as evidenced by increased nerve
conduction velocity, increased nerve Na+,K+ ATPase activity, and significant amelioration of nerve
structural changes. Likewise, C-peptide administration in animals that had C-peptide deficiency (type 1
model) with nephropathy improves renal function and structure; it decreases urinary albumin excretion
and prevents or decreases diabetes-induced glomerular changes secondary to mesangial matrix
expansion. C-peptide also has been reported to have anti-inflammatory effects as well as aid repair of
smooth muscle cells