[Peptides prevent the forming of secretory phenotype of chondrocytes associated with the aging.]

S N Myakisheva1, N S Linkova1,2,3, E O Kozhevnikova1

  • 1Saint-Petersburg Institute of Bioregulation and Gerontology, 3 pr. Dynamo, St. Petersburg 197110, Russian Federation,

Insights

Aging chondrocytes develop a secretory phenotype (SASP), driving musculoskeletal diseases like osteoarthritis (OA). AED peptide and cartilage polypeptide complex (CPC) normalize SASP, offering potential OA treatments and geroprotective effects.

Area of Science:

  • Molecular gerontology
  • Cellular senescence
  • Biochemistry of aging

Context:

  • Aging chondrocytes exhibit a secretory phenotype (SASP), contributing to musculoskeletal diseases such as osteoarthritis (OA).
  • Identifying effective OA treatments is a critical challenge in molecular gerontology.
  • SASP involves altered expression of key proteins and cytokines.

Purpose:

  • To characterize the secretory phenotype associated with aging (SASP) in chondrocytes.
  • To comparatively assess the effects of AED peptide and cartilage polypeptide complex (CPC) on chondrocyte SASP.
  • To explore the therapeutic potential of AED peptide and CPC for OA and related musculoskeletal conditions.

Summary:

  • Chondrocyte SASP is marked by increased pro-apoptotic proteins (p16, p21, p53), pro-inflammatory cytokines (TNF-α, IL-1α), and decreased Sirt1 synthesis.
  • Both AED peptide and cartilage polypeptide complex (CPC) were found to normalize the synthesis of molecules involved in chondrocyte SASP.
  • These normalizing effects suggest a geroprotective mechanism for AED and CPC.

Impact:

  • The findings provide insights into the molecular mechanisms underlying OA pathogenesis.
  • AED peptide and CPC demonstrate potential as therapeutic agents for OA and other musculoskeletal disorders.
  • This research contributes to the development of novel geroprotective strategies for age-related diseases.

Related Concept Videos

The Effect of Aging on Tissues01:19

The Effect of Aging on Tissues

Several body functions deteriorate with age. The external signs of aging are easily identifiable. For example, the skin becomes dry, less elastic, and thins out, forming wrinkles. The skin of the face begins to appear looser due to a decrease in the levels of elastic and collagen fibers in the connective tissue. Additionally, melanin production in the hair follicle decreases with age, resulting in gray hair. Moreover, the senses of sight and hearing decline, so glasses and hearing aids may...
2.2K
Extracellular Matrix01:26

Extracellular Matrix

Unlike epithelial tissue, which is composed of cells closely packed with little or no extracellular space in between, connective tissue cells are dispersed in a matrix. This extracellular matrix (ECM) is composed of fibrous proteins like collagen, elastin, and fibronectin in a ground substance consisting of interstitial fluid, cell adhesion proteins, and proteoglycans. The proteoglycans form a gel-like material in the spaces between cells and provide hydration, buffering, binding, and force...
3.0K
Bone Disorders01:29

Bone Disorders

Aging and its effect on bone remodeling is the most common cause of bone disorders. In young and healthy people, bone deposition and resorption happen at an equal rate to maintain optimal bone health.
Bone deposition is also affected by the levels of sex hormones like estrogen and testosterone that promote osteoblast activity and bone matrix synthesis. When the level of these hormones decreases due to aging, it causes a reduction in bone deposition. As a result, bone resorption by osteoclasts...
3.7K
Growth of Cartilage and Bone Tissue01:27

Growth of Cartilage and Bone Tissue

Chondrocytes form a temporary cartilaginous model by dividing and secreting a thick gel-like extracellular matrix. Once the chondrocytes undergo programmed cell death, osteoblasts enter the site of the cartilaginous model. The process of replacing the temporary cartilaginous model with bone in an ordered manner is called endochondral ossification. In endochondral ossification, not all of the cartilage is replaced by bone tissue. Some cartilage that performs a protective and supportive function...
3.4K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
18.1K
Bacterial Protein Maturation01:26

Bacterial Protein Maturation

Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
40