Submaxillary kallikrein
Submaxillary Kallikrein is a form of kallikrein that is specifically found in the submaxillary gland, also known as the submandibular gland. Kallikreins are a group of serine protease enzymes, which are known for their ability to cleave peptide bonds in proteins. They play a crucial role in various physiological processes, including blood pressure regulation, inflammation, and coagulation. Submaxillary kallikrein, in particular, has been studied for its role in the processing of local hormones and in the mechanism of saliva secretion.
Function[edit | edit source]
Submaxillary kallikrein acts primarily in the salivary glands where it facilitates the production and secretion of saliva. This enzyme contributes to the initial steps of digestion by breaking down large protein molecules in the food into smaller peptides. Additionally, it has a role in the local regulation of blood flow within the gland, thereby influencing the rate of saliva production.
Physiological Role[edit | edit source]
The physiological role of submaxillary kallikrein extends beyond its digestive functions. It is involved in the regulation of blood pressure through the kinin-kallikrein system, where it acts to produce kinins, which are potent vasodilators. This mechanism highlights the systemic effects of kallikreins, demonstrating their importance in cardiovascular health.
Clinical Significance[edit | edit source]
Research has indicated that alterations in the expression or activity of submaxillary kallikrein could be linked to various diseases. For instance, abnormal levels of this enzyme have been associated with hypertension and some forms of cancer. Understanding the precise role of submaxillary kallikrein in these conditions could lead to the development of new therapeutic strategies.
Research Directions[edit | edit source]
Ongoing research is focused on elucidating the detailed mechanisms by which submaxillary kallikrein influences both local and systemic physiological processes. Studies are also exploring the potential of targeting this enzyme in the treatment of related diseases, such as hypertension and cancer.
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Contributors: Prab R. Tumpati, MD