Dipeptidyl peptidase II (DPPII), a review

Area of Science:

• Biochemistry
• Molecular Biology
• Enzymology

Background:

• Proline-specific N-terminal processing regulates numerous biological processes.
• Dipeptidyl peptidases (DPPs) are a protease family involved in signaling by peptide hormones.
• Dipeptidyl peptidase II (DPPII) is an intracellular protease found in the vesicular system.

Purpose of the Study:

• To review the current literature on Dipeptidyl peptidase II (DPPII).
• To clarify the dispersed data regarding DPPII's functions and roles.
• To provide a state-of-the-art overview of DPPII research.

Main Methods:

• Literature review of existing studies on DPPII.
• Analysis of reported enzyme localization in cells, body fluids, and organs.
• Examination of suggested physiological and pathological roles of DPPII.

Main Results:

• DPPII prefers cleaving N-terminal dipeptides from oligopeptides with Pro or Ala at the penultimate position, optimally at acidic pH.
• DPPII has been suggested to be involved in cell differentiation, protection from cell death, and degradation of collagen fragments, myofibrillar proteins, and neuropeptides.
• Changes in DPPII levels and distribution suggest roles in disease-related processes.

Conclusions:

• The precise physiological role of DPPII is not yet fully elucidated.
• DPPII's localization and suggested functions point to diverse biological roles.
• Further research is needed to consolidate the understanding of DPPII's functions and implications in health and disease.