Interleukin 10 (IL-10) is a potent anti-inflammatory cytokine that plays a crucial, and often essential, role in preventing inflammatory and autoimmune pathologies. Impaired IL-10 expression or signaling can enhance clearance of pathogens during an acute infection, but also exaggerate inflammatory response, resulting in exacerbated immunopathology and tissue damage. All in all, Il-10 plays a largely nonredundant role in mediating host anti-inflammatory response.

Interleukin (IL)-18 was originally discovered as a factor that enhanced IFN-γ production from anti-CD3-stimulated Th1 cells, especially in the presence of IL-12. IL-18 is also a proinflammatory cytokine that facilitates type 1 responses. It is a cytokine that stimulates various cell types and has pleiotropic functions. IL-18 is a member of the IL-1 family of cytokines. IL-18 demonstrates a unique function by binding to a specific receptor expressed on various types of cells.

Interleukin-1 beta (IL-1β) is a member of the interleukin-1 family that has a broad spectrum of both beneficial and harmful biological actions. IL-1β is one of the important cytokines synthesized by monocytes and phagocytes, involved in initiation and perpetuation of inflammation.

Interleukin 6 (IL-6), promptly and transiently produced in response to infections and tissue injuries, contributes to host defense through the stimulation of acute phase responses, hematopoiesis, and immune reactions. Although its expression is strictly controlled by transcriptional and posttranscriptional mechanisms, dysregulated continual synthesis of IL-6 plays a pathological effect on chronic inflammation and autoimmunity.

Interleukins (IL) are a type of cytokine first thought to be expressed by leukocytes alone but have later been found to be produced by many other body cells. They play essential roles in the activation and differentiation of immune cells, as well as proliferation, maturation, migration, and adhesion. They also have pro-inflammatory and anti-inflammatory properties. The primary function of interleukins is, therefore, to modulate growth, differentiation, and activation during inflammatory and immune responses. Interleukins consist of a large group of proteins that can elicit many reactions in cells and tissues by binding to high-affinity receptors in cell surfaces. They have both paracrine and autocrine function.

Irisin is a novel myokine and adipokine secreted following proteolytic cleavage of its precursor fibronectin type III domain containing 5 (FNDC5). Irisin exerts its major action by increasing the expression of mitochondrial uncoupling protein 1 (UCP 1), which facilitates the conversion of white adipose tissue (WAT) into beige adipose tissue. Irisin is distributed in various body tissues and several actions have been attributed to its presence in those tissues.

Kidney injury molecule 1 (KIM-1) is a type I membrane protein, comprising an extracellular portion and a cytoplasmic portion. It is also named as HAVCR1 (Hepatitis A virus cellular receptor 1) or TIM1 (T-cell immunoglobulin mucin receptor 1), and is expressed in the kidney, liver, and spleen. KIM-1 plays different roles via various molecular targets in immune diseases and kidney injury.

The Klotho proteins, α Klotho and β Klotho, are essential components of endocrine fibroblast growth factor (FGF) receptor complexes, as they are required for the high-affinity binding of FGF19, FGF21 and FGF23 to their cognate FGF receptors (FGFRs). Collectively, these proteins form a unique endocrine system that governs multiple metabolic processes in mammals.

Leptin is a peptide hormone released from adipose tissue and part of the adipokines. While leptin's role is classically described in the regulation of appetite, neuroendocrine function, and energy homeostasis, it seems to influence several other physiological processes. These include metabolism, endocrine regulation, and immune function, with possible other functions still awaiting characterization. Leptin abnormalities have associations with a variety of metabolic syndromes, particularly obesity.

Matrix metalloproteases (MMPs) are a multigene family of zinc-dependent endopeptidases that share a similar structure and which collectively, have the capacity to degrade virtually every component of the extracellular matrix (ECM). MMP activity is inhibited specifically and reversibly by a group of structurally related, endogenous inhibitors known as tissue inhibitors of metalloproteases (TIMPs).