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Dipeptidyl peptidase (DPP) is a type of enzyme that plays a crucial role in the breakdown of proteins. It is involved in the cleavage of dipeptides, which are molecules consisting of two amino acids linked together. DPPs are found in various organisms, including bacteria, plants, and animals, and they are classified into different families based on their structure and function.
Dipeptidyl Peptidase


== Structure and Function ==
Dipeptidyl peptidase (DPP) is a type of [[enzyme]] that plays a crucial role in the regulation of various physiological processes in the human body. These enzymes are involved in the cleavage of dipeptides from the N-terminus of polypeptides, which is essential for the activation or inactivation of many bioactive peptides.
DPPs are typically membrane-bound proteins that are anchored to the cell surface or located within intracellular compartments. They contain a catalytic domain responsible for the enzymatic activity and may also have additional domains that contribute to their specific functions. The catalytic domain of DPPs is characterized by a conserved amino acid sequence motif known as the DPP domain.


The primary function of DPPs is to hydrolyze the peptide bond between two amino acids in a dipeptide molecule. This process involves the addition of a water molecule, resulting in the formation of two separate amino acids. DPPs exhibit substrate specificity, meaning they can only cleave certain dipeptides based on the amino acid sequence and the presence of specific amino acid residues at the cleavage site.
==Types of Dipeptidyl Peptidases==


== Role in Physiology ==
There are several types of dipeptidyl peptidases, each with distinct functions and substrate specificities. The most well-known types include:
DPPs have been implicated in various physiological processes in different organisms. In humans, one of the most well-known DPPs is dipeptidyl peptidase-4 (DPP-4), also known as CD26. DPP-4 is widely expressed in tissues and is involved in the regulation of glucose metabolism. It plays a crucial role in the degradation of incretin hormones, such as glucagon-like peptide-1 (GLP-1) and glucose-dependent insulinotropic polypeptide (GIP), which are important regulators of insulin secretion.


The inhibition of DPP-4 activity has been targeted as a therapeutic approach for the treatment of type 2 diabetes. By inhibiting DPP-4, the degradation of incretin hormones is reduced, leading to increased insulin secretion and improved glycemic control. Several DPP-4 inhibitors, such as sitagliptin and saxagliptin, have been developed and are currently used as antidiabetic drugs.
* [[Dipeptidyl Peptidase-4]] (DPP-4)
* [[Dipeptidyl Peptidase-8]] (DPP-8)
* [[Dipeptidyl Peptidase-9]] (DPP-9)


== Clinical Significance ==
===Dipeptidyl Peptidase-4 (DPP-4)===
Apart from their role in glucose metabolism, DPPs have also been implicated in other physiological and pathological processes. For example, DPP-4 has been shown to play a role in immune regulation, inflammation, and cancer progression. Inhibition of DPP-4 activity has been investigated as a potential therapeutic strategy for autoimmune diseases, such as rheumatoid arthritis, and certain types of cancer.


== References ==
DPP-4 is a serine exopeptidase that is widely expressed in various tissues, including the [[intestine]], [[liver]], and [[kidney]]. It is involved in the inactivation of incretin hormones such as [[glucagon-like peptide-1]] (GLP-1) and [[glucose-dependent insulinotropic polypeptide]] (GIP), which are important for the regulation of [[blood glucose]] levels.
<references>
<ref>[[Dipeptidyl peptidase-4]] - Wikipedia</ref>
<ref>[[Dipeptidyl peptidase-4 inhibitors]] - Wikipedia</ref>
<ref>[[Dipeptidyl peptidase-4 inhibitors]] - National Center for Biotechnology Information</ref>
</references>


== See Also ==
===Dipeptidyl Peptidase-8 and Dipeptidyl Peptidase-9===
 
DPP-8 and DPP-9 are closely related enzymes that are less well understood compared to DPP-4. They are expressed in various tissues and are thought to play roles in immune regulation and [[cell proliferation]].
 
==Physiological Functions==
 
Dipeptidyl peptidases are involved in numerous physiological processes, including:
 
* Regulation of [[glucose metabolism]]
* Modulation of the [[immune system]]
* Control of [[inflammation]]
* Regulation of [[appetite]] and [[satiety]]
 
==Clinical Significance==
 
Dipeptidyl peptidases, particularly DPP-4, have significant clinical implications. Inhibition of DPP-4 is a therapeutic strategy for the treatment of [[type 2 diabetes mellitus]]. DPP-4 inhibitors, also known as "gliptins," help to prolong the action of incretin hormones, thereby enhancing insulin secretion and lowering blood glucose levels.
 
==DPP-4 Inhibitors==
 
DPP-4 inhibitors are a class of oral hypoglycemic agents used in the management of type 2 diabetes. Some common DPP-4 inhibitors include:
 
* [[Sitagliptin]]
* [[Saxagliptin]]
* [[Linagliptin]]
* [[Alogliptin]]
 
==Potential Side Effects==
 
While DPP-4 inhibitors are generally well-tolerated, they may cause side effects such as:
 
* [[Nasopharyngitis]]
* [[Headache]]
* [[Upper respiratory tract infection]]
 
==Research and Development==
 
Ongoing research is focused on understanding the broader roles of dipeptidyl peptidases in health and disease, as well as developing new therapeutic agents targeting these enzymes for various conditions beyond diabetes.
 
==See Also==
 
* [[Enzyme]]
* [[Protease]]
* [[Protease]]
* [[Enzyme]]
* [[Incretin]]
* [[Glucagon-like peptide-1]]
 
* [[Insulin secretion]]
{{Enzyme-stub}}
* [[Type 2 diabetes]]


[[Category:Enzymes]]
[[Category:Enzymes]]
[[Category:Protein metabolism]]
[[Category:Metabolism]]
[[Category:Diabetes]]
[[Category:Diabetes]]
[[Category:Pharmacology]]
[[Category:Biochemistry]]
[[Category:Physiology]]

Revision as of 12:40, 31 December 2024

Dipeptidyl Peptidase

Dipeptidyl peptidase (DPP) is a type of enzyme that plays a crucial role in the regulation of various physiological processes in the human body. These enzymes are involved in the cleavage of dipeptides from the N-terminus of polypeptides, which is essential for the activation or inactivation of many bioactive peptides.

Types of Dipeptidyl Peptidases

There are several types of dipeptidyl peptidases, each with distinct functions and substrate specificities. The most well-known types include:

Dipeptidyl Peptidase-4 (DPP-4)

DPP-4 is a serine exopeptidase that is widely expressed in various tissues, including the intestine, liver, and kidney. It is involved in the inactivation of incretin hormones such as glucagon-like peptide-1 (GLP-1) and glucose-dependent insulinotropic polypeptide (GIP), which are important for the regulation of blood glucose levels.

Dipeptidyl Peptidase-8 and Dipeptidyl Peptidase-9

DPP-8 and DPP-9 are closely related enzymes that are less well understood compared to DPP-4. They are expressed in various tissues and are thought to play roles in immune regulation and cell proliferation.

Physiological Functions

Dipeptidyl peptidases are involved in numerous physiological processes, including:

Clinical Significance

Dipeptidyl peptidases, particularly DPP-4, have significant clinical implications. Inhibition of DPP-4 is a therapeutic strategy for the treatment of type 2 diabetes mellitus. DPP-4 inhibitors, also known as "gliptins," help to prolong the action of incretin hormones, thereby enhancing insulin secretion and lowering blood glucose levels.

DPP-4 Inhibitors

DPP-4 inhibitors are a class of oral hypoglycemic agents used in the management of type 2 diabetes. Some common DPP-4 inhibitors include:

Potential Side Effects

While DPP-4 inhibitors are generally well-tolerated, they may cause side effects such as:

Research and Development

Ongoing research is focused on understanding the broader roles of dipeptidyl peptidases in health and disease, as well as developing new therapeutic agents targeting these enzymes for various conditions beyond diabetes.

See Also


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