When your CD4 count is low you should eat 2 servings of fruits and 3 servings of vegetables.
You should also eat lean protein foods such as skinless chicken, fish, turkey, egg whites, beans and tofu and use low fat cooking techniques such as baking sauteing and broiling.
You can increase your CD4 naturally by increasing your vitamin and zinc intake and eating a balanced and healthy diet, staying physically active and mentally active and reducing stress and getting enough sleep.
However in order to actually increase your CD4 count you will need to take HIV medication although the above things can also help.
All T cells are not CD4 as several types of T cells exist which include TH1, TH2, TH17, and Treg cells, each with slightly different roles and functions.
All the T cells work together to protect the body from any foreign pathogens and CD4+ T cells primarily activate the other immune cells which include CD8+ T cells.
The thing that kills CD4 T cells is HIV-PLAP of peripheral blood mononuclear cells (PBMCs) and T cell lines leads to rapid depletion of CD4+ T cells and induction of apoptosis.
And the majority of HIV-induced T cell death in vitro involves direct loss of infected cells rather than indirect effects on uninfected bystander cells.
The vitamins that help T cells is vitamin D which can induce many different anti inflammatory functions such as increasing the number or function of T regulatory cells.
Foods that activate T cells are soy, beans, lentils, eggs, fish and chicken.
Avoid foods such as red meats, chicken with the skin or fried meats or other foods with saturated fats.
T cells do have integrins which they use for essentially all of their functions and they use the integrins to migrate in and out of lymph nodes and following and infection to migrate to other tissues.
In apoptosis integrins regulate the apoptotic response to DNA damage through modulation of p53.
In the muscles the integrins are a major laminin binding integrin which stabilizes the muscle plasma membrane and integrin α7 couples with β1 integrin in mature muscle fibers.
Integrins in metastasis increase tumor progression and metastasis.
In endothelial cells the integrins regulate migration, proliferation and survival which is necessary for angiogenesis.
The differences between cadherin and integrin are cadherins mediate homotypic adhesion between cells and integrins mediate adhesion between the cell and it's extracellular matrix.
The connection between actin and integrin is a cyclical liaison, which develops again and again at new adhesion sites only to cease at sites of de-adhesion.
The integrin receptors connect the extracellular matrix to the actin cytoskeleton.
The role of integrin in the immune system is to mediate cell-cell and cell-extracellular matrix adhesion, and also affect the multitude of signal transduction cascades in control of cell survival, proliferation, differentiation and organ development.
The examples of integrin proteins are αIIbβ3 integrin and β2 integrin that predominantly exist in the inactive state.
The examples of integrin receptors are receptors for collagens, laminin-1 and laminin-5, fibronectin, tenascin, thrombospondin, vitronectin, and VCAM-1.
The family of integrins are a family of ubiquitous αβ heterodimeric receptors which exist in multiple conformations and also interact with a diverse group of ligands.
These molecules also mediate interactions between cells and of these cells with the extracellular matrix (ECM) and also serve a critical role in signaling and homeostasis.
Integrins contribute to blood clotting by binding to the adhesive proteins, the integrins mediate platelet adhesion to injured vascular wall and platelet aggregation which is important for the maintenance of hemostasis which prevents excessive bleeding.
In inflammation integrins regulate the cellular growth, migration, proliferation, signaling and cytokine activation and release and play important roles in cell proliferation and migration as well as tissue repair, apoptosis and processes that are critical to inflammation, angiogenesis and infection.
Integrin does bind to collagen and has been reported to be one of the main collagen binding integrins that are present in skin, bone and other internal organs which comprise epithelial cells, platelets, immune cells, fibroblasts, mesenchymal cells and chondrocytes.
The roles of integrin are to function as transmembrane linkers (or “integrators”), mediating the interactions between the cytoskeleton and the extracellular matrix that are required for cells to grip the matrix and they are activated by cytoplasmic tail ligands.
There are 24 different integrins which include 18 subunits and 8 subunits that generate 24 different integrins.
The cells that express integrin are all nucleated cells of multicellular animals and are essential for cell-matrix adhesion and, in vertebrates, cell-cell interactions.
Integrins are activated by cytoplasmic tail ligands.
Talin PTB domain (the head F3 subdomain) binds the first β-NPXY and the membrane proximal helix, whereas kindlin binds the second NPXY.
In skin integrin binds to numerous ligands that are present in the provisional wound ECM which includes the fibronectin (α5β1, α9β1, αvβ6), vitronectin (αvβ5), and tenascin (α9β1, αvβ6), as well as laminin-332 (α3β1, α6β4) that is deposited by migrating keratinocytes.
The integrin binds to the extracellular matrix (ECM) glycoproteins such as laminins and collagens in basement membranes or connective tissue components like fibronectin.
Other integrins also bind to what are known as counterreceptors on neighboring cells, bacterial polysaccharides, or viral coat proteins.
The examples of integrins are αIIbβ3 to platelets; α6β4 to keratinocytes; αEβ7 to T cells, dendritic cells and mast cells in mucosal tissues; α4β1 to leukocytes; α4β7 to a subset of memory T cells; and the β2 integrins to leukocytes.
In mammals some integrins are limited to certain cell types and or tissue types.
In regard to ligand specificity, the mammalian integrins can be broadly grouped into laminin-binding integrins (α1β1, α2β1, α3β1, α6β1, α7β1, and α6β4), collagen-binding integrins (α1β1, α2β1, α3β1, α10β1, and α11β1), leukocyte integrins (αLβ2, αMβ2, αXβ2, and αDβ2), and RGD-recognizing integrins (α5β1, αVβ1, αVβ3.
The function of integrins are to act as transmembrane linkers (or “integrators”), mediating the interactions between the cytoskeleton and the extracellular matrix which are required for the cells to grip the matrix.
Integrins regulate cellular growth, proliferation, migration, signaling, and cytokine activation and release and thereby play important roles in cell proliferation and migration, apoptosis, tissue repair, as well as in all processes critical to inflammation, infection, and angiogenesis.
Cell surface receptors for the extracellular matrix (ECM), such as the integrins, play key roles in the regulation of normal and tumour cell migration and survival.
The integrin family of cell adhesion proteins controls cell attachment to the ECM.
Integrins are the principal receptors used by animal cells to bind to the extracellular matrix.
They are heterodimers and function as transmembrane linkers between the extracellular matrix and the actin cytoskeleton.
A cell can regulate the adhesive activity of its integrins from within.
Integrins are formed through noncovalent association of two type I transmembrane glycoproteins, the α- and the β subunit.
The extracellular parts are approximately 700 amino acids for α - and 1000 amino acids for β subunits and form elongated stalks and a globular ligand-binding head region6.