BMP-6: Regulation of Wound Healing and Immune Cell Recruition

Target Name: BMP6

NCBI ID: G654

BMP6

BMP-6: Regulation of Wound Healing and Immune Cell Recruition

BMP-6 (Bifferential Molecular Profile 6) is a protein that is expressed in various tissues of the body, including the brain, heart, kidneys, and liver. It is a member of the BMP family, which is a well-known signaling pathway that regulates cellular processes in various organisms, including mammals. BMP-6 has been shown to play a role in various physiological processes in the body, including wound healing, tissue repair, and inflammation.

One of the key features of BMP-6 is its ability to induce a variety of cellular responses, including the production of extracellular matrix (ECM) components, the activation of downstream signaling pathways, and the recruitment of immune cells to the site of injury or inflammation. This is accomplished through the presence of several unique structural features on BMP-6, including a long N-terminal tail, a calcified portion, and a unique dimerization domain.

The N-terminal tail of BMP-6 is a region that is rich in electrostatic interactions and is known to play a role in BMP-6's ability to interact with other proteins. This region is also involved in the formation of a complex with the protein Focal Adhesion Protein (FAX), which is a well-known regulator of cell-cell adhesion. This interaction between BMP-6 and FAX has been shown to play a role in the regulation of various cellular processes, including embryonic development, tissue repair, and inflammation.

The calcified portion of BMP-6 is a unique structural feature that is found in only a small number of proteins. This region is rich in calcium ions and is known to play a role in the regulation of various cellular processes, including cell signaling, cytoskeletal organization, and chromatin structure. The presence of the calcified portion of BMP-6 has been shown to contribute to its ability to induce cellular responses and to participate in various signaling pathways.

The dimerization domain of BMP-6 is a region that is rich in multiple distinct protein-protein interactions. This region is known to play a role in the regulation of various cellular processes, including cell signaling, cytoskeletal organization, and chromatin structure. The presence of the dimerization domain of BMP-6 has been shown to contribute to its ability to induce cellular responses and to participate in various signaling pathways.

BMP-6 has been shown to play a role in a variety of physiological processes in the body, including wound healing, tissue repair, and inflammation. For example, studies have shown that BMP-6 can induce the production of ECM components in response to tissue injury or infection, and that this production is dependent on the presence of BMP-6. Additionally, studies have shown that BMP-6 can recruit immune cells to the site of tissue injury or infection, and that this recruitment is dependent on the presence of BMP-6.

In conclusion, BMP-6 is a protein that is expressed in various tissues of the body and is involved in a variety of cellular processes. Its unique structural features, including the N-terminal tail, calcified portion, and dimerization domain, have been shown to contribute to its ability to induce cellular responses and to participate in various signaling pathways. Further research is needed to fully understand the role of BMP-6 in various biological processes and to develop new treatments for diseases that are dependent on its activity.

Protein Name: Bone Morphogenetic Protein 6

Functions: Growth factor of the TGF-beta superfamily that plays essential roles in many developmental processes including cartilage and bone formation (PubMed:31019025). Also plays an important role in the regulation of hepcidin/HAMP expression and iron metabolism by acting as a ligand for hemojuvelin/HJV (PubMed:26582087). Initiates the canonical BMP signaling cascade by associating with type I receptor ACVR1 and type II receptor ACVR2B (PubMed:18070108). In turn, ACVR1 propagates signal by phosphorylating SMAD1/5/8 that travel to the nucleus and act as activators and repressors of transcription of target. Can also signal through non-canonical pathway such as TAZ-Hippo signaling cascade to modulate VEGF signaling by regulating VEGFR2 expression (PubMed:33021694)

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