CELA3B

From WikiMD's Food, Medicine & Wellness Encyclopedia

CELA3B (Chymotrypsin-like elastase family member 3B) is a protein that in humans is encoded by the CELA3B gene. This enzyme belongs to the elastase family of serine proteases, which play a significant role in various biological processes, including digestion, immune response, and wound healing. The CELA3B protein is primarily expressed in the pancreas, where it contributes to the breakdown of dietary proteins within the small intestine.

Function[edit | edit source]

CELA3B is an enzyme that catalyzes the cleavage of peptide bonds in proteins, specifically targeting alanine and serine residues. It is secreted by the pancreatic acinar cells as part of the pancreatic juice, which enters the small intestine and aids in the digestion of proteins. This process is crucial for the absorption of nutrients from the diet. In addition to its role in digestion, CELA3B may also be involved in the regulation of various cellular processes, although these functions are less well understood.

Gene[edit | edit source]

The CELA3B gene is located on chromosome 1 (1p36.21) in humans. It is part of a cluster of related elastase genes, which includes CELA3A and CELA2A. These genes share a high degree of sequence similarity, suggesting they have evolved from a common ancestor through gene duplication events. The CELA3B gene consists of several exons and introns, and its expression is tightly regulated to ensure proper levels of the enzyme are produced in response to physiological needs.

Clinical Significance[edit | edit source]

Alterations in the expression or activity of CELA3B can have pathological consequences. Although specific diseases have not been directly linked to mutations in the CELA3B gene, dysregulation of elastase enzymes, in general, has been associated with conditions such as pancreatitis, cystic fibrosis, and chronic obstructive pulmonary disease (COPD). Research is ongoing to better understand the role of CELA3B in health and disease, which may lead to the development of new therapeutic strategies targeting this enzyme.

See Also[edit | edit source]

References[edit | edit source]


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Contributors: Prab R. Tumpati, MD