Related Experiment Video
Updated: Jan 19, 2026
05:46
A Proinflammatory, Degenerative Organ Culture Model to Simulate Early-Stage Intervertebral Disc Disease.
Published on: February 14, 2021
4.1K
GOLGB1 deficiency accelerates intervertebral disc degeneration by activating the MAPK pathway
Jingyuan Tian1,2,3, Zhiquan Wang3,4, Ruxing Liu2,3
1Department of Orthopedics, Second Hospital of Shanxi Medical University, Taiyuan, 030001, China.
Scientific Reports
|January 17, 2026
Summary
Golgin B1 (GOLGB1) deficiency accelerates intervertebral disc degeneration (IDD) by promoting nucleus pulposus cell apoptosis and extracellular matrix degradation via the MAPK pathway. GOLGB1 acts as a protective factor against IDD progression.
Area of Science:
- Biochemistry
- Cell Biology
- Orthopedics
Background:
- Intervertebral disc degeneration (IDD) is an age-related condition with unclear molecular mechanisms.
- Golgin B1 (GOLGB1) is a Golgi-related protein implicated in various diseases, but its role in IDD is unknown.
Purpose of the Study:
- To investigate the role of GOLGB1 in IDD.
- To determine if GOLGB1 deficiency accelerates disc degeneration and elucidate its underlying mechanism.
Main Methods:
- In vitro studies using nucleus pulposus (NP) cells with GOLGB1 knockdown.
- In vivo IDD mouse model established via caudal vertebra acupuncture.
- Techniques included cell proliferation/apoptosis assays, ECM analysis, western blotting, qPCR, and immunohistochemistry.
Main Results:
- GOLGB1 expression was reduced in degenerated human NP tissues and in IDD mouse models.
- GOLGB1 knockdown worsened NP cell degeneration, inhibited proliferation, increased apoptosis, and disrupted extracellular matrix.
- GOLGB1 knockdown activated the MAPK pathway by increasing p-ERK and p-P38 levels.
Conclusions:
- GOLGB1 acts as a protective factor against IDD.
- GOLGB1 deficiency accelerates IDD by activating the MAPK pathway.
- GOLGB1 represents a potential therapeutic target for IDD.
Keywords:
ApoptosisExtracellular matrixGOLGB1Intervertebral disc degenerationMAPK pathwayProliferationMore Related Videos
Related Concept Videos
01:07MAPK Signaling Cascades
8.0K
Mitogen-activated protein kinase, or MAPK pathway, activates three sequential kinases to regulate cellular responses such as proliferation, differentiation, survival, and apoptosis. The canonical MAPK pathway starts with a mitogen or growth factor binding to an RTK. The activated RTKs stimulate Ras, which recruits Raf or MAP3 Kinase (MAPKKK), the first kinase of the MAPK signaling cascade. Raf further phosphorylates and activates MEK or MAP2 Kinases (MAPKK), which in turn phosphorylates MAP...
8.0K
02:58Regulated Protein Degradation
3.1K
3.1K
02:58Regulated Protein Degradation
8.8K
It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
8.8K
01:16TGF - β Signaling Pathway
10.5K
The TGF-β signaling pathway regulates cell growth, differentiation, adhesion, motility, and development. TGF-β ligands that induce TGF-β signaling are synthesized in their latent form. Several proteases or cell surface receptors such as integrins act upon the latent form, releasing the active ligand. There are three types of mammalian TGF-βs: (TGF-β1, TGF-β2, and TGF-β3) that bind as homodimers or heterodimers to TGF-β receptors. The TGF-β receptors...
10.5K
01:42Microtubule Associated Proteins (MAPs)
5.8K
Microtubule function and architecture are regulated by an array of specialized proteins called microtubule-associated proteins or MAPs. These proteins are widespread across different organisms and have conserved protein motifs, like the multi-TOG domain for tubulin binding found in the CLASP family of MAPs. Some MAPs are lineage-specific based on their conserved domains. Their functions depend upon the cytoskeletal architecture and cell type they are located within. In-plant cells, a specific...
5.8K
01:22Activation and Inactivation of G Proteins
11.1K
Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high...
11.1K