What Are the Different Types of Adhesion Treatment?

Adhesion molecules (AMs) refer to a class of molecules produced by cells, existing on the cell surface, and mediating contact and binding between cells and cells or between cells and substrates. Adhesion molecules are mostly glycoproteins, and a few are glycolipids, which are distributed on the cell surface or extracellular matrix (ECM).

Adhesion molecule

Adhesion molecules (AMs) refer to a class of molecules produced by cells, existing on the cell surface, and mediating contact and binding between cells and cells or between cells and substrates. Adhesion molecules are mostly glycoproteins, and a few are glycolipids, which are distributed on the cell surface or extracellular matrix (ECM).

Chinese name

Adhesion molecule

Foreign name

adhesion molecules

Form of action

Receptor-ligand binding

Adhesion molecule

Mediate cell-to-cell contact

Cell adhesion molecules (CAM) are a collective name for many molecules that mediate contact and binding between cells or between cells and extracellular matrix (ECM).

Form of action: in the form of receptor-ligand binding.

Naming: Adhesion molecules and CD molecules are named according to different angles. Adhesion molecules are classified by adhesion function. CD molecules are named by monoclonal antibody recognition and classification. The scope is very wide, including the adhesion molecule group. Therefore, most adhesion molecules have CD numbers, but There are also some adhesion molecules that do not yet have a CD number.

Adhesion molecules are a collective term for molecules that mediate contact or binding between cells or between cells. They are glycoproteins located on the cell surface or in the cell matrix, and function as receptors and ligands. Adhesion molecules make cell-to-cell, cell-to-matrix adhesion, participate in cell recognition, activation and signal transmission, cell proliferation and differentiation, cell extension and movement, make immune response, inflammation, coagulation,

Adhesion molecules are classified according to their structural characteristics

1,

The function of adhesion molecules:

Participate in many important physiological functions of the body and

The role of different adhesion molecules at different stages of the adhesion process

Is a special form of lymphocyte migration

Adhesion molecules are involved in cell-to-cell attachment

During embryonic development, different types of cells form cell-to-cell and cell-to-extracellular matrix attachments in accordance with established rules, and they are assembled in an orderly manner to form different tissues and organs. In this process, adhesion molecules play an important role.

Adhesion molecules and intracellular tyrosine phosphorylation

Intercellular or cell-matrix adhesion molecule interactions are not limited to cell adhesion and attachment. They also have a significant effect on the activation, differentiation, growth, and secretion of cells involved in adhesion, and rely on adhesion molecules to extracellularly Adhesion molecules interact to conduct signals into the cell. The signal transmitted by adhesion molecules may serve as a co-factor and cooperate with the effects of other stimulating factors, such as 31, 41, 51, 61, and L2, and ligands may cooperate with TCR / CD3-mediated lymphocyte proliferation and cytokines Production, suggesting that the role of lymphocytes and extracellular matrix may affect their activation status. In addition, the role of integrin molecules and ligands on the surface of monocytes and neutrophils is also involved in the process of inducing cells to produce inflammatory factors.

Tyrosine phosphorylation is an important pathway for intracellular signaling, and integrin molecules are involved in the occurrence of tyrosine phosphorylation in certain cells. Platelet activation is accompanied by extensive intracellular protein tyrosine phosphorylation. The expression of integrin molecule b3 is a necessary condition for the occurrence of tyrosine phosphorylation in platelets. b3 is not expressed or its interaction with the ligand can be blocked. Impedes tyrosine phosphorylation in platelets. But b3 alone is not enough to cause tyrosine phosphorylation, but only as a necessary auxiliary condition for other stimulation and activation factors. The results of studies on other cells also suggest that the integrin molecule is involved in the process of intracellular tyrosine phosphorylation. For example, after cross-linking the 31 molecule expressed by KB cells (a cancer cell line), a molecular weight of 115 can be found in the cell. -130kDa molecules undergo tyrosine phosphorylation; NIH3T3 cells adhere to dry fibronectin molecules or are stimulated with anti-integrin antibodies, which can cause tyrosine phosphorylation of a protein in the cell.

Some cells (such as fibroblasts, endothelial cells) increase the cytoplasmic pH after adhering to fibronectin. The increase in pH in the cytoplasm is the result of the signal transduction of integin molecules into the cell, which is related to cell extension and growth.

Adhesion Molecules and Cell Membrane Phosphatidylinositol Metabolism

Integrin molecules expressed by phagocytic cells can interact with ligands such as fibronectin or laminin to increase cell phagocytosis. Studies have shown that this phenomenon is related to the integin molecule binding to ligands and affecting the cell membrane phosphatidylinositol metabolism.

A type of leukocyteresponseintegrin (LRI) called leukocyte response integrin cross-reacts with integrin3, but is different from any known integrin molecule. LRI-mediated phagocytosis can be blocked by protein kinase C inhibitors H7 and Staruosporin, and also by pertussis toxin, calcium chelator MAPTAM, and neomycin bound to phosphatidylinositol. The role of the body may cause the activation of G-protein-dependent phospholipase C, leading to the activation of intracellular PKC and an increase in Ca2 concentration. In addition, a 5kDa molecule called integrinassociated protein IAP co-precipitated with LPI was found to belong to a family of multiple transmembrane cell surface molecules. Anti-IAP antibodies can inhibit LRI-mediated phagocytosis enhancement. It is speculated that IAP may be related to the affinity of LRI-binding ligands or participate in LPI signaling processes.