myelopeptide 2 (mp 2)

Myelopeptide-2 (MP-2) with the sequence Leu-Val-Val-Tyr-Pro-Trp is originally isolated from the supernatant of porcine bone marrow cell culture and is able to restore the mitogen responsiveness of human T lymphocytes inhibited by conditioned medium from H

Myelin P2 protein, also known as PMP2, is a cytosolic protein found primarily in peripheral nerves. It Belongs to the calycin superfamily. Fatty-acid binding protein (FABP) family. PMP2 is a small, basic, and cytoplasmic lipid binding protein of peripheral myelin. It is similar in amino acid sequence and tertiary structure to fatty acid binding proteins found in the liver, adipocytes, and intestine, its expression is limited to the nervous system. PMP2 is detected only in myelin-producing cells of the central and peripheral nervous systems, the oligodendrocytes and Schwann cells, respectively. PMP2 may play a role in lipid transport protein in Schwann cells. It forms a beta-barrel structure that accommodates hydrophobic ligands in its interior.

Myelopeptide-2, a peptide isolated from the supernatant of porcine bone marrow cell cultures, can restore the mitogenic reactivity of human T lymphocytes inhibited by HL-60 leukemia cells or measles virus conditions. It also enhances depressed interleukin-2 (IL-2) synthesis and interleukin-2 receptor (IL-2R) expression, playing a role in immunity homeostasis. This compound shows potential for application in antitumor and antivirus research [1] [2].